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2-amino-6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2-amino-6-mercaptopurine ribotide + diphosphate
-
-
-
-
?
2-hydroxy-6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2-hydroxy-6-mercaptopurine ribotide + diphosphate
-
-
-
-
?
3-hydroxy-2-pyrazinecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
3-oxo-4-(5-O-phosphono-beta-D-ribofuranosyl)-3,4-dihydropyrazine-2-carboxamide + diphosphate
T-1105, poor substrate
-
-
?
3-hydroxy-2-pyrazinecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
T-1105, poor substrate
-
-
?
6-fluoro-3-hydroxy-2-pyrazinecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
6-fluoro-3-oxo-4-(5-O-phosphono-beta-D-ribofuranosyl)-3,4-dihydropyrazine-2-carboxamide + diphosphate
T-705, poor substrate
-
-
?
6-fluoro-3-hydroxy-2-pyrazinecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
T-705, poor substrate
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine riboside 5'-phosphate + diphosphate
-
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-thioinosine monophosphate + diphosphate
-
-
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
thioinosinic monophosphate + diphosphate
-
a thiopurine antimetabolite
a therapeutically active metabolite
-
?
6-thioguanine + 5-phospho-alpha-D-ribose 1-diphosphate
6-thio-GMP + diphosphate
-
-
-
-
?
8-azaguanine + 5-phospho-alpha-D-ribose 1-diphosphate
8-aza-IMP + diphosphate
high activity
-
-
?
8-azahypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
8-aza-IMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
?
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
allopurinol + 5-phospho-alpha-D-ribose 1-diphosphate
?
-
-
-
?
allopurinol + 5-phospho-alpha-D-ribose 1-diphosphate
allopurinol ribonucleoside 5'-monophosphate + diphosphate
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
XMP + diphosphate
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
additional information
?
-
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
-
-
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
-
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
-
-
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
low activity
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
low activity
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
low activity
-
-
?
allopurinol + 5-phospho-alpha-D-ribose 1-diphosphate
allopurinol ribonucleoside 5'-monophosphate + diphosphate
-
low activity
-
?
allopurinol + 5-phospho-alpha-D-ribose 1-diphosphate
allopurinol ribonucleoside 5'-monophosphate + diphosphate
-
-
-
?
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
6-oxopurine salvage pathway reaction
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
low activity
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes, and catalyse the 2 reactions with different specificities
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
binds hypoxanthine 67-times less effectively than guanine and 4-times less effectively than xanthine
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
absolutely specific for guanine
diphosphate binds at Thr70, diphosphate-binding loop sequence: LTGA
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
guanine is utilized more rapidly than hypoxanthine
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
salvage synthesis
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
wild-type enzyme, no activity with mutant F36L
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
wild-type and chimeric mutant enzyme
modeling of GMP binding to the chimeric enzyme
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
wild-type and chimeric mutant enzyme
modeling of GMP binding to the chimeric enzyme
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
hypoxanthine and guanine preferred substrates
-
-
ir
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes, and catalyse the 2 reactions with different specificities
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
a freely reversible Mg2+-dependent conversion
-
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
equilibrium lies far in direction of IMP formation
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
2 assay methods
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
6-oxopurine salvage pathway reaction
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
6-oxopurine salvage pathway reaction
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
binding mechanism and structure of IMP occupying the diphosphate site, overview
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
hypoxanthine is the preferred substrate
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
unlike the hypoxanthine-guanine phosphoribosyltransferase from other sources this enzyme binds hypoxanthine 67-times less effectively than guanine and 4-times less effectively than xanthine
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes, and catalyse the 2 reactions with different specificities
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
binds hypoxanthine 67-times less effectively than guanine and 4-times less effectively than xanthine
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
no activity with hypoxanthine
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
equilibrium lies far in direction of IMP formation
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
salvage synthesis
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
wild-type enzyme, no activity with mutant F36L
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
wild-type and chimeric mutant enzyme
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
the enzyme is involved in the purine salvage pathway
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
wild-type and chimeric mutant enzyme
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
a freely reversible Mg2+-dependent conversion
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
hypoxanthine and guanine preferred substrates, continuous spectrophotometric enzyme assay, pH 7.5, 12 mM MgCl2, 40-70°C, 30 sec
Kd(diphosphate): 4.7 +/-0.1 mM, revealed by quenching of intrinsic fluorescence of the enzyme upon diphosphate-binding
-
ir
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
phosphoribosyltransferases for hypoxanthine and guanine are separate enzymes, and catalyse the 2 reactions with different specificities
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
best substrate
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
best substrate
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
best substrate
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
most effective substrate
diphosphate is bound by Thr47
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
wild-type and chimeric mutant enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
wild-type and chimeric mutant enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
mutant F36L, no activity with the wild-type enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
-
low activity
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
-
wild-type enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
no activity
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
no activity
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
no activity
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
recombinant chimeric mutant DS1
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
wild-type human enzyme does not accept xanthine as substrate, mutant F36L does catalyze the conversion of xanthine to XMP with a kcat much lower than those of hypoxanthine and guanine
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
recombinant chimeric mutant DS1
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
the enzyme also performs the reaction of xanthine phosphoribosyltransferase, EC 2.4.2.22
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
reaction of EC 2.4.2.22
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
reaction of EC 2.4.2.22
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
low catalytic efficiency (kcat/KM), xanthine is not preferred but a usable substrate
-
-
ir
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
no activity
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
poor substrate
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
r
additional information
?
-
-
no substrates: 5-formamido-4-imidazolecarboxamide, uric acid, 8-azaguanine, 2,6-diaminopurine, orotic acid, phosphate
-
-
?
additional information
?
-
-
no substrate: adenine
-
-
?
additional information
?
-
-
the conformation of the flexible loop, containing a 3-10 helix and a unique double serine repeat, is important for substrate binding and activation of the enzyme
-
-
?
additional information
?
-
-
no incorporation of xanthine in vivo
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
?
additional information
?
-
hypoxanthine phosphoribosyltransferase (EcHPRT) has a strong preference for hypoxanthine as the base substrate
-
-
-
additional information
?
-
-
-
-
-
?
additional information
?
-
-
dynamic and conformational properties of purified enzyme alone, in complex with GMP and Mg2+, and in equilibration mixture of enzyme with IMP, Mg2+/diphosphate and hypoxanthine, Mg2+/5-phosphoribosyl 1-diphosphate, and in transition-state analogue complex of enzyme, immucillin-GP and Mg2+/diphosphate
-
-
?
additional information
?
-
-
a mentally retarded child and its asymptomatic uncle have a partial enzyme deficiency, homozygous, while mother and grandmother are heterozygous and not enzyme-deficient
-
-
?
additional information
?
-
-
kinetic study
-
-
?
additional information
?
-
-
locus of Lesch-Nyhan syndrome, activator of the prodrugs 6-mercaptopurine and allopurinol
-
-
?
additional information
?
-
-
locus of Lesch-Nyhan syndrome, activator of the prodrugs 6-mercaptopurine and allopurinol
-
-
?
additional information
?
-
-
substrate binding induces conformational changes required for catalysis
-
-
?
additional information
?
-
the flexibilty of loop IV can influence the substrate specificity
-
-
?
additional information
?
-
-
the flexibilty of loop IV can influence the substrate specificity
-
-
?
additional information
?
-
-
enzyme-deficiency is involved in development of gout
-
-
?
additional information
?
-
-
the enzyme is organized in a branched bi-enzyme system with xanthine oxidase, EC 1.17.3.2
-
-
?
additional information
?
-
-
substrate binding structure involving residue K68 at the AB-dimer interface and residues V96 and D97 of the opposing subunit, overview. Residues E133 and D137 block the binding of 5-phospho-alpha-D-ribose 1-diphosphate, mechanism, overview
-
-
?
additional information
?
-
the binding site for the 5'-phosphate is located at residues 132-141
-
-
?
additional information
?
-
-
the binding site for the 5'-phosphate is located at residues 132-141
-
-
?
additional information
?
-
The substrates bind in a functionally ordered fashion, with 5-phospho-alpha-D-ribose 1-diphosphate binding first in the forward direction and IMP or GMP first in the reverse reaction, transition state structure and 5'-phosphate binding structure on HGPRT, overview
-
-
?
additional information
?
-
-
kinetic study
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
enzyme is essential for salvaging exogenous purine bases
-
-
?
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
?
additional information
?
-
-
the enzyme activity is regulated by stabilization and destabilization of the enzyme through release or binding of product and substrates, overview
-
-
?
additional information
?
-
-
the purified recombinant enzyme shows very low activity
-
-
?
additional information
?
-
-
the parasite depends on the human host purine salvage pathway enzyme hypoxanthine guanine xanthine phosphoribosyltransferase for survival, because it does not have a de novo pathway for synthesis of nucleotides on its own
-
-
?
additional information
?
-
-
the binding site for the 5'-phosphate is located at residues 132-141
-
-
?
additional information
?
-
-
no formation of PRPP and 6-oxopurine by pyrophosphorylysis due to disability of binding to nucleotides IMP, GMP, XMP at 40-70°C and substrate concentrations of up to 0.5 mM
-
-
?
additional information
?
-
-
no substrate: adenine
-
-
?
additional information
?
-
-
kinetic study
-
-
?
additional information
?
-
-
no substrate: adenine
-
-
?
additional information
?
-
purine nucleotide synthesis using TthAPRT and TthHPRT (EC 2.4.2.8). No activity with 2-chloroadenine, 2-fluoroadenine, thymine, 1,2,4-triazole-3-carboxamide, and 1,2,4-triazole-3-carboxy-N-methylamide
-
-
-
additional information
?
-
purine nucleotide synthesis using TthAPRT and TthHPRT (EC 2.4.2.8). No activity with 2-chloroadenine, 2-fluoroadenine, thymine, 1,2,4-triazole-3-carboxamide, and 1,2,4-triazole-3-carboxy-N-methylamide
-
-
-
additional information
?
-
purine nucleotide synthesis using TthAPRT and TthHPRT (EC 2.4.2.8). No activity with 2-chloroadenine, 2-fluoroadenine, thymine, 1,2,4-triazole-3-carboxamide, and 1,2,4-triazole-3-carboxy-N-methylamide
-
-
-
additional information
?
-
-
9-deazaguanine is no substrate
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
-
the two isozymes exhibit similar substrate specificity, kinetic characteristics, and temporal expression patterns, overview
-
-
?
additional information
?
-
-
kinetic study
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
?
additional information
?
-
xanthine is a poor substrate
-
-
-
additional information
?
-
-
forward reaction: transfer of the phosphoribosyl group to N9 position of 6-oxopurines
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
-
formation of dead-end complexes with purine substrates and diphosphate
-
-
?
additional information
?
-
-
L67 side chain participates in hydrophobic interactions between dimer subunits important for the proper positioning of main chain atoms that influence enzyme chemistry and the binding of 5-phospho-alpha-D-ribose 1-diphosphate, diphosphate, and hypoxanthine, residue 69 needs to be small like Gly, which is found there, to avoid sterical interference with binding of 5-phospho-alpha-D-ribose 1-diphosphate and diphosphate as well as the positioning of a metal ion
-
-
?
additional information
?
-
ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview
-
-
-
additional information
?
-
-
ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview
-
-
-
additional information
?
-
ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview
-
-
-
additional information
?
-
ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview
-
-
-
additional information
?
-
ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview
-
-
-
additional information
?
-
ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview
-
-
-
additional information
?
-
ZgHGPRT/AMPK is a bifunctional enzyme, which acts as phosphoribosyltransferase or adenylate kinase depending upon the nature of the substrate. Substrate specificity, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
XMP + diphosphate
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
additional information
?
-
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
GMP + diphosphate
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
6-oxopurine salvage pathway reaction
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
salvage synthesis
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
6-oxopurine salvage pathway reaction
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
6-oxopurine salvage pathway reaction
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
salvage synthesis
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
the enzyme is involved in the purine salvage pathway
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
-
-
?
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
IMP + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
? + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
mutant F36L, no activity with the wild-type enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
-
low activity
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
-
wild-type enzyme
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
reaction of EC 2.4.2.22
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
reaction of EC 2.4.2.22
-
-
?
additional information
?
-
-
no incorporation of xanthine in vivo
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
?
additional information
?
-
-
locus of Lesch-Nyhan syndrome, activator of the prodrugs 6-mercaptopurine and allopurinol
-
-
?
additional information
?
-
-
locus of Lesch-Nyhan syndrome, activator of the prodrugs 6-mercaptopurine and allopurinol
-
-
?
additional information
?
-
-
enzyme-deficiency is involved in development of gout
-
-
?
additional information
?
-
-
the enzyme is organized in a branched bi-enzyme system with xanthine oxidase, EC 1.17.3.2
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
enzyme is essential for salvaging exogenous purine bases
-
-
?
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
?
additional information
?
-
-
the enzyme activity is regulated by stabilization and destabilization of the enzyme through release or binding of product and substrates, overview
-
-
?
additional information
?
-
-
the parasite depends on the human host purine salvage pathway enzyme hypoxanthine guanine xanthine phosphoribosyltransferase for survival, because it does not have a de novo pathway for synthesis of nucleotides on its own
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
additional information
?
-
-
enzyme is essential for salvaging exogenous purine bases
-
-
?
additional information
?
-
-
salvage incorporation of exogenous purine nucleotides, no de novo synthesis
-
-
?
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(1S)-1-(9-deazaguanin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol 5-phosphate
(1S)-1-(9-deazahypoxanthin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol 5-phosphate
(2-[(2,3-dihydroxypropyl)[2-(6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl]amino]ethyl)phosphonic acid
-
(2-[(3R,4R)-3-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-4-[(2R)-2-hydroxy-2-phosphonoethoxy]pyrrolidin-1-yl]-2-oxoethyl)phosphonic acid
(2-[3-(8-bromoguanin-9-yl)-2-(2-(bishydroxyphosphoryl)-ethoxy)propoxy]ethyl)phosphonic acid
(2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl)phosphonic acid
(2-[[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl][2-(2-phosphonoethoxy)ethyl]amino]ethyl)phosphonic acid
-
(3-hydroxy-2-[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]propyl)phosphonic acid
(3-[[(4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]propyl)phosphonic acid
-
competitive. 466fold lower affinity for human enzyme. Treatment of cultured parasites with the bis-pavalate of the inhibitor as a prodrug inhibits growth with an IC50 of 45 microM
(R)-9-[2-(phosphonomethoxy)propyl]hypoxanthine
-
-
(R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]-8-bromoguanine
(R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
(S)-3-(guanin-9-yl)-pyrrolidin-N-ylacetylphosphonic acid
(S)-9-[2-(phosphonomethoxy)propyl]guanine
(S)-9-[2-(phosphonomethoxy)propyl]hypoxanthine
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]-8-azaguanine
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]-8-bromoguanine
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
([2-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-3-(2-phosphonoethoxy)propoxy]methyl)phosphonic acid
([2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-3-(2-phosphonoethoxy)propoxy]methyl)phosphonic acid
([3-(7-deazaguanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
([3-(7-deazahypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
([3-(8-bromoguanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
([3-(8-bromohypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
([3-(guanine-9-yl)-2-((2-phosphonoethoxy)-methyl)propoxy]methyl)phosphonic acid
([3-(hypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
2-((2,3-dihydroxypropyl)(2-(hypoxanthin-9-yl)ethyl)-amino)ethyl phosphonate
weak inhibition
2-((2-(guanin-9-yl)ethyl)(2-((2-hydroxyethyl)((2-phosphonoethyl)amino)ethyl)amino)ethyl)phosphonic acid
-
2-(2-((2-(hypoxanthine-9-yl)ethyl)((2-phosphonoethyl)amino)ethyl)((2-phosphonoethyl)amino)ethyl)phosphonic acid
-
2-([3-(guanin-9-yl)-2-(2-bis(hydroxyphosphoryl)ethoxy)propoxy]ethyl)phosphonic acid
-
2-amino-6-mercaptopurine
-
competitive to hypoxanthine
3-((7-hydroxy-1H-pyrazolo[4,3-d]pyrimidin-3-yl)methylamino)propylphosphonate
4-(2-methyl-4-oxo-(3H) quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
78.12% inhibition at 0.25 mg/ml
4-(2-methyl-6,8-dibromo-4-oxo-(3H)quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
79.07% inhibition at 0.25 mg/ml
4-(2-methyl-6-bromo-4-oxo-(3H) quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
77.06% inhibition at 0.25 mg/ml
4-(2-phenyl-4-oxo-(3H) quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
79.42% inhibition at 0.25 mg/ml
4-(2-phenyl-6,8-dibromo-4-oxo-(3H)quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
79.71% inhibition at 0.25 mg/ml
4-(2-phenyl-6-bromo-4-oxo-(3H) quinazolin-3-yl)-benzoic acid (4-formyl-benzylidene) hydrazide
-
79.55% inhibition at 0.25 mg/ml
5-phospho-alpha-D-ribose 1-diphosphate
6-aminopurine nucleotides
6-Hydroxypurine nucleotides
6-Mercaptopurine
-
competitive to hypoxanthine
6-methylheptyl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
9-beta-Arabinofuranosylhypoxanthine
-
-
9-deazaguanine
uncompetitive inhibitor
9-[(N-phosphonoethyl-N-phosphonobutyl)-2-aminoethyl]hypoxanthine
-
9-[(N-phosphonoethyl-N-phosphonoethoxyethyl)-2-aminoethyl]-hypoxanthine
-
9-[(N-phosphonoethyl-N-phosphonomethoxyethyl)-2-aminoethyl]hypoxanthine
-
9-[(N-phosphonoethyl-N-phosphonomethyl)-2-aminoethyl]-hypoxanthine
-
9-[2-(2-phosphonoethoxy)ethyl]guanine
9-[2-(2-phosphonoethoxy)ethyl]hypoxanthine
9-[2-(phosphonomethoxy)-3-fluoro-propyl]guanine
9-[2-(phosphonomethoxy)ethyl]-6-thioguanine
9-[2-(phosphonomethoxy)ethyl]-7-deaza-8-azahypoxanthine
9-[2-(phosphonomethoxy)ethyl]-8-azaguanine
9-[2-(phosphonomethoxy)ethyl]-8-bromoguanine
9-[2-(phosphonomethoxy)ethyl]guanine
9-[2-(phosphonomethoxy)ethy]-8-hydroxyguanine
acyclic nucleoside phosphonates
cyclic (R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
cyclic (S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
diethyl (2S,15S)-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-8-[(4-oxo-3,4-dihydro-7H-pyrrolo[2,3-d]pyrimidin-7-yl)methyl]-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
diethyl (2S,15S)-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-8-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
diethyl (2S,15S)-2,15-dibenzyl-8-[(8-bromo-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
diethyl (2S,15S)-4,13-bis[[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]amino]-4,13-dioxo-8-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-bis(2-phenylethyl)-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
diethyl (2S,15S)-8-[(2-amino-4-oxo-3,4-dihydro-7H-pyrrolo[2,3-d]pyrimidin-7-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-7,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-4,13-bis[[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]amino]-4,13-dioxo-2,15-bis(2-phenylethyl)-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
diethyl (2S,15S)-8-[(2-amino-8-bromo-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-7,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
diethyl dicarbonate
-
alkylation of Arg155, complete inactivation at pH 9.0, pH dependent
guanine ribose 5'-phosphate
hypoxanthine ribose 5'-phosphate
immucillin-G 5'-phosphate
active site contacts in the HGPRT/immucillin-G 5'-phosphate/diphosphate complex, overview
immucillin-H
-
transition state analogue, binds tightly to the active site, inhibition mechanism and kinetics
immucillin-H 5'-phosphate
Inosine
-
slight inhibition
isoniazid
-
99% inhibition at 0.25 mg/ml
Mg2+
-
inhibitory effects are noncompetitive against 5-phosphoribose 1-diphosphate
monophosphonate-2-(phosphonoethoxy)ethyl hypoxanthine
PEEHx
p-chloromercuribenzoate
-
reversed by dithiothreitol or 2-mercaptoethanol
Phenylglyoxal
-
irreversible, complete inactivation, alkylation of Arg155, GMP protects, no alkylation of mutant R155K
propan-2-yl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
rifampicin
-
99% inhibition at 0.25 mg/ml
Tetranitromethane
-
complete inactivation at pH 9.0, pH dependent, modifies Tyr96 in the active site
triethyl-2-phosphonobutyrate
-
[(+/-)-2(R/S)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
[(+/-)-2(R/S)-[([2-chloro-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
[(1S)-1-hydroxy-2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl]phosphonic acid
[(2R)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
[(2R)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
[(2S)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
[(2S,3R)-2,4-dihydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butoxy]phosphonic acid
[(3R)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
[(3S)-1,1-difluoro-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
[(3S)-3-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-1,1-difluoro-4-hydroxybutyl]phosphonic acid
[(3S)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
[(3S)-4-hydroxy-3-[[(4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]butyl]phosphonic acid
-
competitive. 592fold lower affinity for human enzyme
[2-([2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl][2-[(2-hydroxyethyl)(2-phosphonoethyl)amino]ethyl]amino)ethyl]phosphonic acid
-
[2-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl] phosphonic acid
[2-[(2-hydroxyethyl)(2-[[2-(6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl](2-phosphonoethyl)amino]ethyl)amino]ethyl]phosphonic acid
-
[2-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]ethyl]phosphonic acid
[2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethoxy]phosphonic acid
[3-(6-oxo-1,6-dihydro-9H-purin-9-yl)propyl]phosphonic acid
a competitive inhibitor
[3-(guanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methylphosphonic acid
[3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-2-(hydroxymethyl)propoxy]phosphonic acid
[3-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]propyl]phosphonic acid
[3R,4R]-4-guanin-9-yl-3-((S)-2-hydroxy-2-phosphonoethyl)oxy-1-N-(phosphonopropionyl)pyrrolidine
[4-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)butyl]phosphonic acid
a competitive inhibitor
[4-(6-oxo-1,6-dihydro-9H-purin-9-yl)butyl]phosphonic acid
a competitive inhibitor, enzyme binding structure analysis, crystal structure, overview. In the complex with the inhibitor there is no association with K145 located away from the purine base and the base itself rotated slightly compared to when GMP is bound, such that the distance between the 6-oxo group and this lysine is 3.9 A at its closest approach. A sulfate ion is also observed in the active site, and is located in the diphosphate binding pocket where it interacts with the amide nitrogen of G55, the side-chain of R179 and one magnesium ion. A second magnesium is located between E113 and D114, which is a Mg2+ binding site in the 6-oxopurine PRTs
[5-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)pentyl]phosphonic acid
a competitive inhibitor
[5-(6-oxo-1,6-dihydro-9H-purin-9-yl)pentyl]phosphonic acid
a competitive inhibitor, enzyme binding structure analysis, crystal structure, overview
[6-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)hexyl]phosphonic acid
a competitive inhibitor, enzyme binding structure analysis, crystal structure, overview
[6-(6-oxo-1,6-dihydro-9H-purin-9-yl)hexyl]phosphonic acid
a competitive inhibitor
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethyl]phosphonic acid
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]phosphonic acid
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]pentyl]phosphonic acid
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl]phosphonic acid
[[2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]propane-1,3-diyl]bis(oxymethylene)]bis(phosphonic acid)
[[[(4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]azanediyl]di(propane-3,1-diyl)]bis(phosphonic acid)
-
(1S)-1-(9-deazaguanin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol 5-phosphate
-
(1S)-1-(9-deazaguanin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol 5-phosphate
-
-
(1S)-1-(9-deazahypoxanthin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol 5-phosphate
-
(1S)-1-(9-deazahypoxanthin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol 5-phosphate
-
-
(2-[(3R,4R)-3-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-4-[(2R)-2-hydroxy-2-phosphonoethoxy]pyrrolidin-1-yl]-2-oxoethyl)phosphonic acid
enzyme-bound crystal structure analysis
(2-[(3R,4R)-3-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-4-[(2R)-2-hydroxy-2-phosphonoethoxy]pyrrolidin-1-yl]-2-oxoethyl)phosphonic acid
enzyme-bound crystal structure analysis; enzyme-bound crystal structure analysis
(2-[3-(8-bromoguanin-9-yl)-2-(2-(bishydroxyphosphoryl)-ethoxy)propoxy]ethyl)phosphonic acid
-
(2-[3-(8-bromoguanin-9-yl)-2-(2-(bishydroxyphosphoryl)-ethoxy)propoxy]ethyl)phosphonic acid
-
(2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl)phosphonic acid
-
(2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl)phosphonic acid
-
(3-hydroxy-2-[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]propyl)phosphonic acid
-
-
(3-hydroxy-2-[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]propyl)phosphonic acid
-
(R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]-8-bromoguanine
-
(R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]-8-bromoguanine
-
-
(R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
is toxic to cells and arrests cell growth
(R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
is toxic to cells and arrests cell growth
(S)-3-(guanin-9-yl)-pyrrolidin-N-ylacetylphosphonic acid
-
(S)-3-(guanin-9-yl)-pyrrolidin-N-ylacetylphosphonic acid
-
(S)-9-[2-(phosphonomethoxy)propyl]guanine
-
(S)-9-[2-(phosphonomethoxy)propyl]guanine
-
-
(S)-9-[2-(phosphonomethoxy)propyl]hypoxanthine
-
(S)-9-[2-(phosphonomethoxy)propyl]hypoxanthine
-
-
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]-8-azaguanine
-
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]-8-azaguanine
-
-
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]-8-bromoguanine
-
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]-8-bromoguanine
-
-
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
is toxic to cells and arrests cell growth
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
is toxic to cells and arrests cell growth
([2-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-3-(2-phosphonoethoxy)propoxy]methyl)phosphonic acid
-
([2-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-3-(2-phosphonoethoxy)propoxy]methyl)phosphonic acid
-
([2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-3-(2-phosphonoethoxy)propoxy]methyl)phosphonic acid
-
([2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-3-(2-phosphonoethoxy)propoxy]methyl)phosphonic acid
-
([3-(7-deazaguanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(7-deazaguanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(7-deazahypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(7-deazahypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(8-bromoguanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(8-bromoguanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(8-bromohypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(8-bromohypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(guanine-9-yl)-2-((2-phosphonoethoxy)-methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(guanine-9-yl)-2-((2-phosphonoethoxy)-methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(hypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(hypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
3-((7-hydroxy-1H-pyrazolo[4,3-d]pyrimidin-3-yl)methylamino)propylphosphonate
-
-
3-((7-hydroxy-1H-pyrazolo[4,3-d]pyrimidin-3-yl)methylamino)propylphosphonate
-
5-phospho-alpha-D-ribose 1-diphosphate
-
competitive against GMP; product inhibition
5-phospho-alpha-D-ribose 1-diphosphate
-
product inhibition
5-phospho-alpha-D-ribose 1-diphosphate
-
competitive versus diphosphate and GMP or IMP
6-aminopurine nucleotides
-
-
6-aminopurine nucleotides
-
-
6-Hydroxypurine nucleotides
-
-
6-Hydroxypurine nucleotides
-
-
6-methylheptyl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
-
6-methylheptyl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
-
-
6-thioguanine
-
competitive to hypoxanthine
6-thioguanine
-
competitive to hypoxanthine
9-[2-(2-phosphonoethoxy)ethyl]guanine
-
9-[2-(2-phosphonoethoxy)ethyl]guanine
-
-
9-[2-(2-phosphonoethoxy)ethyl]hypoxanthine
-
9-[2-(2-phosphonoethoxy)ethyl]hypoxanthine
-
-
9-[2-(phosphonomethoxy)-3-fluoro-propyl]guanine
-
9-[2-(phosphonomethoxy)-3-fluoro-propyl]guanine
-
-
9-[2-(phosphonomethoxy)ethyl]-6-thioguanine
-
9-[2-(phosphonomethoxy)ethyl]-6-thioguanine
-
-
9-[2-(phosphonomethoxy)ethyl]-7-deaza-8-azahypoxanthine
-
9-[2-(phosphonomethoxy)ethyl]-7-deaza-8-azahypoxanthine
-
-
9-[2-(phosphonomethoxy)ethyl]-8-azaguanine
-
9-[2-(phosphonomethoxy)ethyl]-8-azaguanine
-
-
9-[2-(phosphonomethoxy)ethyl]-8-bromoguanine
-
9-[2-(phosphonomethoxy)ethyl]-8-bromoguanine
-
-
9-[2-(phosphonomethoxy)ethyl]guanine
is toxic to cells and arrests cell growth
9-[2-(phosphonomethoxy)ethyl]guanine
-
is toxic to cells and arrests cell growth
9-[2-(phosphonomethoxy)ethy]-8-hydroxyguanine
-
9-[2-(phosphonomethoxy)ethy]-8-hydroxyguanine
-
-
acyclic nucleoside phosphonates
analogues of the nucleotide reaction product, comprising a purine base joined by a linker to a phosphonate moiety, inhibitor design and potencies, overview. The inhibitors are selectivity for the enzyme of the human parasite Plasmodium falciparum, up to factor 58, compared to the human enzyme, overview
acyclic nucleoside phosphonates
-
analogues of the nucleotide reaction product, comprising a purine base joined by a linker to a phosphonate moiety, inhibitor design and potencies, overview. Selectivity for the parasite enzyme of up to 58 compared to the Homo sapiens enzyme, overview, design of potent and selective acyclic nucleoside phosphonates inhibitors of Plasmodium falciparum HGXPRT as antimalarial drug leads
adenine
-
no inhibition
AMP
-
no inhibition
AMP
-
mutant K134S, competitive
Ba2+
-
-
Ca2+
-
strong
cyclic (R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
is toxic to cells and arrests cell growth
cyclic (R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
is toxic to cells and arrests cell growth
cyclic (S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
is toxic to cells and arrests cell growth
cyclic (S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
is toxic to cells and arrests cell growth
diethyl (2S,15S)-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-8-[(4-oxo-3,4-dihydro-7H-pyrrolo[2,3-d]pyrimidin-7-yl)methyl]-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-8-[(4-oxo-3,4-dihydro-7H-pyrrolo[2,3-d]pyrimidin-7-yl)methyl]-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-8-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-8-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-2,15-dibenzyl-8-[(8-bromo-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-2,15-dibenzyl-8-[(8-bromo-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-4,13-bis[[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]amino]-4,13-dioxo-8-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-bis(2-phenylethyl)-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
-
diethyl (2S,15S)-4,13-bis[[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]amino]-4,13-dioxo-8-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-bis(2-phenylethyl)-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
-
diethyl (2S,15S)-8-[(2-amino-4-oxo-3,4-dihydro-7H-pyrrolo[2,3-d]pyrimidin-7-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-8-[(2-amino-4-oxo-3,4-dihydro-7H-pyrrolo[2,3-d]pyrimidin-7-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-7,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-7,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-4,13-bis[[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]amino]-4,13-dioxo-2,15-bis(2-phenylethyl)-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
-
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-4,13-bis[[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]amino]-4,13-dioxo-2,15-bis(2-phenylethyl)-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
-
diethyl (2S,15S)-8-[(2-amino-8-bromo-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-7,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-8-[(2-amino-8-bromo-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-7,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diphosphate
-
-
diphosphate
-
product inhibition
diphosphate
-
competitive versus 5-phospho-alpha-D-ribose 1-diphosphate, uncompetitive versus hypoxanthine or guanine
EDTA
-
-
GDP
-
-
GMP
-
mixed inhibition
GMP
competitive inhibitor
GMP
-
competitive against 5-phospho-alpha-D-ribose 1-diphosphate; product inhibition
GMP
-
0.3 mM, 50% inhibition of guanine phosphoribosyltransferase activity
GMP
competitive inhibitor with respect to guanine, xanthine, and 5-phospho-alpha-D-ribose 1-diphosphate
GMP
-
competitive versus 5-phospho-alpha-D-ribose 1-diphosphate, noncompetitive versus guanine
GTP
-
-
guanine
-
substrate inhibition
guanine
-
0.06 mM, 50% inhibition of hypoxanthine phosphoribosyltransferase activity
guanine
-
competitve against hypoxanthine
guanine ribose 5'-phosphate
-
guanine ribose 5'-phosphate
-
-
Hg2+
-
complete inhibition at 3 mM after 3 min at 0°C
Hg2+
-
complete inhibition at 3 mM after 3 min at 0°C
hypoxanthine
-
substrate inhibition
hypoxanthine
-
competitive
hypoxanthine
-
0.16 mM, 50% inhibition of guanine phosphoribosyltransferase activity
hypoxanthine
-
competitive against guanine
hypoxanthine ribose 5'-phosphate
-
hypoxanthine ribose 5'-phosphate
-
-
IDP
-
-
immucillin-H 5'-phosphate
5'-phosphate binding structure on HGPRT, overview
immucillin-H 5'-phosphate
-
transition state analogue, binds tightly to the active site, inhibition mechanism and kinetics
IMP
-
feedback inhibition, competitive versus 5-phospho-alpha-D-ribose 1-diphosphate, binding mode
IMP
competitive inhibitor
IMP
-
competitive versus 5-phospho-alpha-D-ribose 1-diphosphate, noncompetitive versus hypoxanthine
KCl
-
no inhibition
nucleotides
-
all free 5'-nucleotides are inhibitory, 6-OH purine nucleotides are most inhibitory, while 6-NH2 purine only at high concentrations
-
nucleotides
-
all free 5'-nucleotides are inhibitory, 6-OH purine nucleotides are most inhibitory, while 6-NH2 purine only at high concentrations
-
Pb2+
-
inhibits the enzyme in erythrocytes about 20% at 0.0005 mM and about 12% at 0.0001 mM, and participates in hemolysis, the intensity of which negatively correlates with the activity of phosphoribosyltransferases, HPRT inhibition as one of the mechanisms of lead toxicity
Pb2+
-
moderately inhibits both the enzyme in erythrocytes even at very low concentrations, and participates in hemolysis, the intensity of which negatively correlates with the activity of phosphoribosyltransferases, HPRT inhibition as one of the mechanisms of lead toxicity
ppGpp
-
strong
propan-2-yl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
-
propan-2-yl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
-
-
purine nucleotides
-
and analogues, overview
-
xanthine
-
weak, competitive
XMP
-
-
Zn2+
-
strong
[(+/-)-2(R/S)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
-
-
[(+/-)-2(R/S)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
-
[(+/-)-2(R/S)-[([2-chloro-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
-
[(+/-)-2(R/S)-[([2-chloro-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
[(1S)-1-hydroxy-2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl]phosphonic acid
-
[(1S)-1-hydroxy-2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl]phosphonic acid
-
[(2R)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
-
[(2R)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
[(2R)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
-
-
[(2R)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
-
[(2S)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
-
[(2S)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
[(2S,3R)-2,4-dihydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butoxy]phosphonic acid
-
-
[(2S,3R)-2,4-dihydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butoxy]phosphonic acid
-
[(3R)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[(3R)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
[(3S)-1,1-difluoro-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[(3S)-1,1-difluoro-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
[(3S)-3-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-1,1-difluoro-4-hydroxybutyl]phosphonic acid
-
-
[(3S)-3-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-1,1-difluoro-4-hydroxybutyl]phosphonic acid
-
[(3S)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[(3S)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
[2-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl] phosphonic acid
-
-
[2-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl] phosphonic acid
-
[2-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]ethyl]phosphonic acid
-
-
[2-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]ethyl]phosphonic acid
-
[2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethoxy]phosphonic acid
-
-
[2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethoxy]phosphonic acid
-
[3-(guanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methylphosphonic acid
structure bound in the active site of human HGPRT (PDB ID 4IJQ), molecular docking. The crystal structure shows that a magnesium ion is coordinated to one of the sulfate oxygen atoms and one of the phosphonate oxygen atoms of the inhibitor
[3-(guanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methylphosphonic acid
-
[3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-2-(hydroxymethyl)propoxy]phosphonic acid
-
-
[3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-2-(hydroxymethyl)propoxy]phosphonic acid
-
[3-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]propyl]phosphonic acid
-
-
[3-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]propyl]phosphonic acid
-
[3R,4R]-4-guanin-9-yl-3-((S)-2-hydroxy-2-phosphonoethyl)oxy-1-N-(phosphonopropionyl)pyrrolidine
-
[3R,4R]-4-guanin-9-yl-3-((S)-2-hydroxy-2-phosphonoethyl)oxy-1-N-(phosphonopropionyl)pyrrolidine
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethyl]phosphonic acid
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]phosphonic acid
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]pentyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]pentyl]phosphonic acid
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl]phosphonic acid
-
-
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl]phosphonic acid
-
[[2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]propane-1,3-diyl]bis(oxymethylene)]bis(phosphonic acid)
-
[[2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]propane-1,3-diyl]bis(oxymethylene)]bis(phosphonic acid)
-
[[2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]propane-1,3-diyl]bis(oxymethylene)]bis(phosphonic acid)
-
additional information
-
overview: inhibition constant of purines and purine analogs
-
additional information
EcHPRT inhibitor design, synthesis and optimization. Several acyclic nucleoside phosphonates (ANPs) have previously been identified as inhibitors of EcXGPRT and EcHPRT, and the most potent of these have Ki values as low as 10 nM for EcXGPRT and 0.8 mM for EcHPRT. Inhibitors binding structures, detailed overview
-
additional information
cytotoxicity studies using human lung carcinoma A549 cells at 37°C. The binding site for the 5'-phosphate is located at residues 132-141. No inhibition by (R)-9-[2-(phosphonomethoxy)propyl]hypoxanthine
-
additional information
-
cytotoxicity studies using human lung carcinoma A549 cells at 37°C. The binding site for the 5'-phosphate is located at residues 132-141. No inhibition by (R)-9-[2-(phosphonomethoxy)propyl]hypoxanthine
-
additional information
design of Plasmodium vivax hypoxanthine-guanine phosphoribosyltransferase inhibitors as potential antimalarial therapeutics, rational structure-based methods, binding structure and comparison to the human enzyme, overview
-
additional information
synthesis and evaluation of asymmetric acyclic nucleoside bisphosphonates as inhibitors of human hypoxanthine-guanine phosphoribosyltransferase
-
additional information
-
synthesis and evaluation of asymmetric acyclic nucleoside bisphosphonates as inhibitors of human hypoxanthine-guanine phosphoribosyltransferase
-
additional information
-
no effect of iodoacetate, phenylglyoxal, p-chloromercuribenzoate, acetic anhydride, ethyl dimethylaminopropylcarbodiimide/ammonium acetate, and diisopropyl fluorophosphate
-
additional information
-
guanine phosphoribosyltransferase activity: IMP and AMP are not inhibitory at concentrations up to 0.6 mM, adenine and xanthine are not inhibitory at concentrations up to 0.5 mM. Adenine and xanthine do not inhibit hypoxanthine phosphoribosyltransferase activity
-
additional information
the antimicrobial activity of acyclic nucleoside phosphonates (ANP) prodrugs diethyl (2R,15S)-7-[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl]-2-benzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-10-(2-hydroxyethyl)-4,13-dioxo-15-(2-phenylethyl)-3,7,10,14-tetraaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate and diethyl (2R,15S)-2-benzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-10-(2-hydroxyethyl)-4,13-dioxo-7-[2-(6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl]-15-(2-phenylethyl)-3,7,10,14-tetraaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate is not attributable to inhibition of HGPRT
-
additional information
-
the antimicrobial activity of acyclic nucleoside phosphonates (ANP) prodrugs diethyl (2R,15S)-7-[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl]-2-benzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-10-(2-hydroxyethyl)-4,13-dioxo-15-(2-phenylethyl)-3,7,10,14-tetraaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate and diethyl (2R,15S)-2-benzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-10-(2-hydroxyethyl)-4,13-dioxo-7-[2-(6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl]-15-(2-phenylethyl)-3,7,10,14-tetraaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate is not attributable to inhibition of HGPRT
-
additional information
-
no inhibition by EGTA
-
additional information
design of Plasmodium vivax hypoxanthine-guanine phosphoribosyltransferase inhibitors as potential antimalarial therapeutics, rational structure-based methods, overview; design of Plasmodium vivax hypoxanthine-guanine phosphoribosyltransferase inhibitors as potential antimalarial therapeutics, rational structure-based methods, overview
-
additional information
design of Plasmodium vivax hypoxanthine-guanine phosphoribosyltransferase inhibitors as potential antimalarial therapeutics, rational structure-based methods, overview; design of Plasmodium vivax hypoxanthine-guanine phosphoribosyltransferase inhibitors as potential antimalarial therapeutics, rational structure-based methods, overview
-
additional information
-
design of Plasmodium vivax hypoxanthine-guanine phosphoribosyltransferase inhibitors as potential antimalarial therapeutics, rational structure-based methods, overview; design of Plasmodium vivax hypoxanthine-guanine phosphoribosyltransferase inhibitors as potential antimalarial therapeutics, rational structure-based methods, overview
-
additional information
spectrometric enzyme-inhibitor binding analysis, molecular docking and molecular dynamics studies, computational binding affinity analysis, binding mode and kinetics, overview. Iso-mukaadial acetate and ursolic acid acetate ligands are docked into the binding sites of Plasmodium falciparum and human hypoxanthine-guanine phosphoribosyl transferases protein using the glide docking module, binding structure comparisons
-
additional information
synthesis and evaluation of asymmetric acyclic nucleoside bisphosphonates as inhibitors of Plasmodium falciparum hypoxanthine-guanine-(xanthine) phosphoribosyltransferase. Low Ki values are achieved by inserting an extra carbon atom in the linker connecting the N9 atom of guanine to one of the phosphonate groups
-
additional information
-
synthesis and evaluation of asymmetric acyclic nucleoside bisphosphonates as inhibitors of Plasmodium falciparum hypoxanthine-guanine-(xanthine) phosphoribosyltransferase. Low Ki values are achieved by inserting an extra carbon atom in the linker connecting the N9 atom of guanine to one of the phosphonate groups
-
additional information
the activity of HGXPRTase was unaffected by the triphosphates ATP, GTP, CTP or UTP
-
additional information
-
the activity of HGXPRTase was unaffected by the triphosphates ATP, GTP, CTP or UTP
-
additional information
-
mechanism of product inhibition; no inhibition by ADP, ATP, dAMP, UMP, and UTP
-
additional information
structural differences between the Tbr and human enzymes suggest that selective inhibitors for the Tbr enzyme can be designed. Crystal structures of the enzyme in complex with GMP and IMP and with three acyclic nucleoside phosphonate (ANP) inhibitors are determined. Evaluation of acyclic nucleoside phosphonate inhibitors, overview
-
additional information
-
product inhibition study, the substrates/products protect the enzyme against digestion by trypsin, especially hypoxanthine with diphosphate
-
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4.069
3-hydroxy-2-pyrazinecarboxamide
at pH 7.4 and 37°C
0.001 - 3.668
5-phospho-alpha-D-ribose 1-diphosphate
0.127 - 0.138
5-phosphoribosyl 1-diphosphate
6.426
6-fluoro-3-hydroxy-2-pyrazinecarboxamide
at pH 7.4 and 37°C
0.0062
6-Mercaptopurine
-
-
0.36
8-Azahypoxanthine
-
-
0.0346
adenine
-
mutant K134S
0.0117 - 0.135
allopurinol
0.0039 - 0.968
diphosphate
0.00052 - 0.126
hypoxanthine
0.0054 - 0.09
inosine monophosphate
additional information
additional information
-
0.001
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 22°C, recombinant mutant F36L, with xanthine
0.0044
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 22°C, recombinant mutant F36K, with hypoxanthine
0.0053
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.0065
5-phospho-alpha-D-ribose 1-diphosphate
with guanine as cosubstrate, at pH 7.5 and 25°C
0.011
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 22°C, recombinant mutant F36G, with hypoxanthine
0.0141
5-phospho-alpha-D-ribose 1-diphosphate
with hypoxanthine as cosubstrate, at pH 7.5 and 25°C
0.015
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.0191
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type enzyme
0.025
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant IMP-activated wild-type enzyme
0.026
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type enzyme
0.027
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 22°C, recombinant mutant F36L, with hypoxanthine
0.0282
5-phospho-alpha-D-ribose 1-diphosphate
-
+/-0.0015 mM, 60°C
0.029
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 22°C, recombinant mutant F36K, with guanine
0.03
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant wild-type enzyme, with hypoxanthine
0.031
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant wild-type enzyme, with hypoxanthine
0.032
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type enzyme
0.032
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.032
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant wild-type enzyme, with guanine
0.033
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.035
5-phospho-alpha-D-ribose 1-diphosphate
-
recombinant enzyme, with hypoxanthine
0.035
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 22°C, recombinant wild-type enzyme, with hypoxanthine
0.0369
5-phospho-alpha-D-ribose 1-diphosphate
-
+/-0.0024 mM, 70°C
0.041
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 22°C, recombinant mutant F36L, with guanine
0.0412
5-phospho-alpha-D-ribose 1-diphosphate
-
+/-0.0016 mM, 50°C
0.0428
5-phospho-alpha-D-ribose 1-diphosphate
-
+/-0.0009 mM, 40°C
0.05
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.05
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 22°C, recombinant mutant F36G, with guanine
0.053
5-phospho-alpha-D-ribose 1-diphosphate
IMP-activated enzyme, at pH 7.4 and 23°C
0.06
5-phospho-alpha-D-ribose 1-diphosphate
with guanine as cosubstrate, wild type enzyme, at pH 7.5 and 25°C
0.063
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.065
5-phospho-alpha-D-ribose 1-diphosphate
-
recombinant enzyme, with guanine
0.076
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 22°C, recombinant wild-type enzyme, with guanine
0.079
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant wild-type enzyme, with xanthine
0.083
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant mutant G69S
0.094
5-phospho-alpha-D-ribose 1-diphosphate
activated enzyme, with xanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.094
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant IMP-activated mutant W181Y
0.1
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.102
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant L44F, with hypoxanthine
0.103
5-phospho-alpha-D-ribose 1-diphosphate
recombinant wild-type enzyme, pH 7.4, 25°C
0.104
5-phospho-alpha-D-ribose 1-diphosphate
with guanine as cosubstrate, mutant enzyme R76S, at pH 7.5 and 25°C
0.112
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 50°C, with guanine
0.116
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant L44F, with guanine
0.116
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, with guanine
0.119
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, with hypoxanthine
0.123
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 25°C, with hypoxanthine
0.125
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 25°C, with guanine
0.132
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant mutant L67M
0.133
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 12 mM MgCl2
0.134
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type enzyme
0.138
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 50°C, with hypoxanthine
0.151
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant mutant L44F, with xanthine
0.183
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with hypoxanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.185
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E196D
0.2
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E196Q
0.201
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 22°C, recombinant wild-type enzyme, with guanine
0.22
5-phospho-alpha-D-ribose 1-diphosphate
recombinant enzyme, pH 8.0, 70°C
0.233
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant IMP-activated mutant W181F
0.251
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant IMP-activated mutant W181S
0.256
5-phospho-alpha-D-ribose 1-diphosphate
activated enzyme, with hypoxanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.263
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with guanine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.275
5-phospho-alpha-D-ribose 1-diphosphate
activated enzyme, with guanine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.277
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with xanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.327
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 12 mM MgCl2, in presence of 0.05 mM IMP
0.36
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 25°C, recombinant enzyme, with guanine
0.5
5-phospho-alpha-D-ribose 1-diphosphate
-
natural mutant I137T
0.546
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 28°C, recombinant chimeric mutant enzyme with substrate hypoxanthine
0.546
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 28°C, recombinant chimeric mutant enzyme with substrate hypoxanthine
0.659
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E196R
0.972
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with hypoxanthine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
1.075
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 28°C, recombinant chimeric mutant enzyme, with substrate guanine
1.075
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 28°C, recombinant chimeric mutant enzyme, with substrate guanine
1.08
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, at pH 7.4 and 23°C
1.084
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with xanthine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
1.084
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant nonactivated wild-type enzyme
1.156
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E196A
1.548
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with guanine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
2.039
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 25°C, recombinant enzyme, with hypoxanthine
2.286
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant nonactivated mutant W181S
2.783
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant nonactivated mutant W181Y
3.668
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant nonactivated mutant W181F
0.127
5-phosphoribosyl 1-diphosphate
recombinant enzyme, with guanine
0.138
5-phosphoribosyl 1-diphosphate
recombinant enzyme, with hypoxanthine
0.0117
allopurinol
-
recombinant enzyme
0.135
allopurinol
-
recombinant enzyme
0.0039
diphosphate
unactivated enzyme, at pH 7.4 and 23°C
0.0042
diphosphate
IMP-activated enzyme, at pH 7.4 and 23°C
0.016
diphosphate
-
pH 7.5, 37°C, recombinant wild-type enzyme, with IMP
0.0175
diphosphate
-
wild-type enzyme
0.022
diphosphate
-
pH 7.5, 37°C, recombinant wild-type enzyme, with GMP
0.025
diphosphate
-
recombinant enzyme, with inosine monophosphate
0.035
diphosphate
-
wild-type enzyme
0.035
diphosphate
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.103
diphosphate
-
wild-type enzyme
0.135
diphosphate
-
pH 7.5, 37°C, recombinant mutant L67M
0.214
diphosphate
-
pH 7.5, 37°C, recombinant mutant G69S
0.324
diphosphate
-
wild-type enzyme, reverse reaction
0.968
diphosphate
-
mutant E196D
0.0225
GMP
-
wild-type enzyme, reverse reaction
0.029
GMP
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.001
guanine
-
below
0.001
guanine
-
pH 7.4, 22°C, recombinant wild-type enzyme
0.0011
guanine
-
recombinant chimeric mutant DS1
0.0011
guanine
-
recombinant chimeric mutant DS1
0.0011
guanine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.0011
guanine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.0014
guanine
-
recombinant enzyme, with other purine
0.0019
guanine
-
recombinant enzyme, with other purine
0.002
guanine
pH 7.4, 22°C, recombinant mutant F36L
0.002
guanine
-
pH 7.4, 22°C, recombinant mutant L44F
0.002
guanine
unactivated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.0021
guanine
-
native enzyme
0.0023
guanine
recombinant wild-type enzyme, pH 7.4, 25°C
0.0025
guanine
activated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.0027
guanine
-
native enzyme
0.0028
guanine
recombinant enzyme, with 5-phospho-alpha-D-ribose 1-diphosphate
0.0029
guanine
pH 7.4, 22°C, recombinant mutant F36K
0.0032
guanine
pH 7.4, 50°C
0.00326
guanine
-
+/-0.00029 mM, 70°C
0.0035
guanine
-
recombinant enzyme
0.0036
guanine
pH 7.4, 25°C
0.0042
guanine
pH 7.4, 37°C
0.0045
guanine
pH 7.4, 22°C, recombinant wild-type enzyme
0.0048
guanine
unactivated enzyme, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.00485
guanine
-
+/-0.00056 mM, 50°C
0.005
guanine
-
wild-type enzyme
0.005
guanine
-
wild-type enzyme
0.0054
guanine
at pH 7.4 and 37°C
0.0061
guanine
pH 7.4, 22°C, recombinant mutant F36G
0.0074
guanine
pH 7.9, 25°C
0.01
guanine
-
wild-type enzyme
0.01
guanine
at pH 7.5 and 25°C
0.0105
guanine
with guanine as cosubstrate, wild type enzyme, at pH 7.5 and 25°C
0.012
guanine
-
wild-type enzyme
0.012
guanine
-
mutant enzyme
0.012
guanine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.016
guanine
-
wild-type enzyme
0.022
guanine
-
pH 7.5, 37°C, recombinant mutant G69S
0.025
guanine
-
pH 7.4, 25°C, recombinant enzyme, with 5-phospho-alpha-D-ribose 1-diphosphate
0.028
guanine
recombinant enzyme, pH 8.0, 70°C
0.029
guanine
pH 7.5, 37°C, recombinant isozyme HGPRT-1
0.134
guanine
-
recombinant enzyme, with 5-phosphoribosyl 1-diphosphate, pH 8.5
0.135
guanine
with guanine as cosubstrate, mutant enzyme R76S, at pH 7.5 and 25°C
0.2
guanine
-
pH 9.0, 37°C
0.294
guanine
pH 7.4, 25°C
0.362
guanine
-
recombinant enzyme, with 5-phosphoribosyl 1-diphosphate
0.00052
hypoxanthine
-
-
0.0009
hypoxanthine
-
recombinant enzyme, with other purine
0.001
hypoxanthine
-
wild-type enzyme
0.001
hypoxanthine
-
below
0.001
hypoxanthine
-
with 6-mercaptopurine
0.001
hypoxanthine
-
pH 7.4, 22°C, recombinant wild-type enzyme and mutant L44F
0.0014
hypoxanthine
-
recombinant chimeric mutant DS1
0.0014
hypoxanthine
-
recombinant chimeric mutant DS1
0.0014
hypoxanthine
pH 7.4, 22°C, recombinant wild-type enzyme
0.0016
hypoxanthine
pH 7.4, 22°C, recombinant mutant F36K
0.0018
hypoxanthine
pH 7.4, 22°C, recombinant mutant F36G
0.0018
hypoxanthine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.0018
hypoxanthine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.0024
hypoxanthine
-
recombinant enzyme
0.0024
hypoxanthine
pH 7.4, 25°C
0.0027
hypoxanthine
pH 7.4, 50°C
0.0028
hypoxanthine
-
mutant E196R
0.0031
hypoxanthine
-
recombinant enzyme, with other purine
0.0033
hypoxanthine
pH 7.4, 37°C
0.0036
hypoxanthine
-
mutant E196Q
0.0036
hypoxanthine
at pH 7.4 and 37°C
0.0037
hypoxanthine
-
native enzyme
0.0038
hypoxanthine
-
wild-type enzyme
0.00388
hypoxanthine
-
+/-0.00033 mM, 40°C
0.0039
hypoxanthine
pH 7.9, 25°C
0.0042
hypoxanthine
-
recombinant enzyme
0.0044
hypoxanthine
recombinant enzyme, with 5-phospho-alpha-D-ribose 1-diphosphate
0.0044
hypoxanthine
pH 7.4, 22°C, recombinant mutant F36L
0.0048
hypoxanthine
-
mutant enzyme
0.00483
hypoxanthine
-
+/-0.00049 mM, 60°C
0.0049
hypoxanthine
-
mutant E196D
0.005
hypoxanthine
unactivated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.005
hypoxanthine
unactivated enzyme, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.0055
hypoxanthine
recombinant wild-type enzyme, pH 7.4, 25°C
0.0061
hypoxanthine
-
wild-type enzyme
0.0061
hypoxanthine
-
+/-0.00143 mM, 70°C
0.0063
hypoxanthine
-
mutant E196A
0.0064
hypoxanthine
-
wild-type enzyme
0.00702
hypoxanthine
-
+/-0.00104 mM, 50°C
0.0075
hypoxanthine
activated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.0086
hypoxanthine
-
wild-type enzyme
0.0086
hypoxanthine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.0125
hypoxanthine
pH 7.4, 25°C
0.013
hypoxanthine
recombinant enzyme, pH 8.0, 70°C
0.015
hypoxanthine
-
pH 9.0, 37°C
0.0192
hypoxanthine
-
pH 7.5, 37°C, recombinant mutant L67M
0.023
hypoxanthine
-
natural mutant I137T
0.026
hypoxanthine
at pH 7.5 and 25°C
0.0339
hypoxanthine
-
pH 7.5, 37°C, recombinant mutant G69S
0.038
hypoxanthine
-
mutant K134S
0.047
hypoxanthine
pH 7.5, 37°C, recombinant isozyme HGPRT-1
0.05
hypoxanthine
-
pH 7.4, 25°C, recombinant enzyme, with 5-phospho-alpha-D-ribose 1-diphosphate
0.06
hypoxanthine
-
recombinant enzyme, with 5-phosphoribosyl 1-diphosphate
0.126
hypoxanthine
-
recombinant enzyme, with 5-phosphoribosyl 1-diphosphate, pH 8.5
0.0016
IMP
unactivated enzyme, at pH 7.4 and 23°C
0.0024
IMP
-
wild-type enzyme
0.007
IMP
IMP-activated enzyme, at pH 7.4 and 23°C
0.0147
IMP
-
mutant E196Q
0.016
IMP
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.027
IMP
-
pH 7.5, 37°C, recombinant wild-type enzyme and mutant L67M
0.0726
IMP
-
mutant E196D
0.08
IMP
-
pH 7.5, 37°C, recombinant mutant G69S
0.0054
inosine monophosphate
-
recombinant enzyme
0.027
inosine monophosphate
-
wild-type enzyme
0.09
inosine monophosphate
-
wild-type enzyme
0.036
xanthine
activated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.045
xanthine
unactivated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.078
xanthine
unactivated enzyme, at pH 7.4 and 23°C
0.078
xanthine
unactivated enzyme, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.095
xanthine
-
+/-0.0084 mM, 70°C
0.101
xanthine
IMP-activated enzyme, at pH 7.4 and 23°C
0.1012
xanthine
-
+/-0.0101 mM, 50°C
0.17
xanthine
-
recombinant enzyme, with 5-phosphoribosyl 1-diphosphate, pH 8.5
0.261
xanthine
-
pH 7.4, 22°C, recombinant wild-type enzyme
0.287
xanthine
pH 7.4, 22°C, recombinant mutant F36L
0.3
xanthine
-
above, purified recombinant chimeric enzyme DS1
0.3
xanthine
-
above, purified recombinant chimeric enzyme DS1
0.332
xanthine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.332
xanthine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.42
xanthine
-
recombinant enzyme, pH 8.5
0.853
xanthine
-
pH 7.4, 22°C, recombinant mutant L44F
additional information
additional information
-
-
-
additional information
additional information
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-
-
additional information
additional information
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-
-
additional information
additional information
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kinetics
-
additional information
additional information
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kinetics
-
additional information
additional information
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kinetics
-
additional information
additional information
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kinetics
-
additional information
additional information
-
Km-values of mutant enzymes
-
additional information
additional information
-
Km-values, loop II-deletion mutant
-
additional information
additional information
-
wild-type and mutant T47K
-
additional information
additional information
-
Km values of mutant enzymes for hypoxanthine, guanine, diphosphate, 5-phosphoribosyl 1-diphosphate, inosine monophosphate
-
additional information
additional information
-
wild-type and mutants: Km values for substrates hypoxanthine, guanine, xanthine, IMP, GMP, XMP
-
additional information
additional information
-
steady-state kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
kinetic analysis in the forward and reverse reaction of the wild-type enzyme and diverse mutant enzymes, overview
-
additional information
additional information
-
steady-state kinetics and dissociation constants
-
additional information
additional information
-
kinetic analysis of the branched bi-enzyme system, detailed overview
-
additional information
additional information
-
steady-state kinetics, recombinant enzyme, overview
-
additional information
additional information
-
no significant change in KM with temperature (40-70°C) for all substrates tested
-
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0.0139 - 74.8
5-phospho-alpha-D-ribose 1-diphosphate
0.001 - 77
inosine monophosphate
additional information
additional information
-
0.0139
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 25°C, recombinant enzyme, with guanine
0.04
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with guanine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.05
5-phospho-alpha-D-ribose 1-diphosphate
-
loop II-deletion mutant
0.1
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with guanine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.1
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with hypoxanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.1
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant IMP-activated mutant W181F
0.1
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant nonactivated mutant W181Y
0.2
5-phospho-alpha-D-ribose 1-diphosphate
activated enzyme, with hypoxanthine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.2
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, at pH 7.4 and 23°C
0.2
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with hypoxanthine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.2
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with xanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.2
5-phospho-alpha-D-ribose 1-diphosphate
unactivated enzyme, with xanthine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.2
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant nonactivated mutant W181F
0.2
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant nonactivated wild-type enzyme
0.3
5-phospho-alpha-D-ribose 1-diphosphate
activated enzyme, with hypoxanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.32
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant nonactivated mutant W181S
0.4
5-phospho-alpha-D-ribose 1-diphosphate
activated enzyme, with guanine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.4
5-phospho-alpha-D-ribose 1-diphosphate
activated enzyme, with guanine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.48
5-phospho-alpha-D-ribose 1-diphosphate
-
+/-0.02, 50°C
0.5
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant IMP-activated mutant W181Y
0.66
5-phospho-alpha-D-ribose 1-diphosphate
-
+/-0.03, 40°C
0.67
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant IMP-activated mutant W181S
0.97
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 25°C, recombinant enzyme, with hypoxanthine
1
5-phospho-alpha-D-ribose 1-diphosphate
activated enzyme, with xanthine as cosubstrate, in 10 mM potassium phosphate, at pH 7.4 and 23°C
1.6
5-phospho-alpha-D-ribose 1-diphosphate
activated enzyme, with xanthine as cosubstrate, in 100 mM Tris-HCl, at pH 7.4 and 23°C
1.6
5-phospho-alpha-D-ribose 1-diphosphate
IMP-activated enzyme, at pH 7.4 and 23°C
1.6
5-phospho-alpha-D-ribose 1-diphosphate
pH 7.4, 37°C, recombinant IMP-activated wild-type enzyme
1.68
5-phospho-alpha-D-ribose 1-diphosphate
-
+/-0.06, 60°C
2.5
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type enzyme
2.8
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E196R
3.05
5-phospho-alpha-D-ribose 1-diphosphate
-
+/-0.07, 70°C
4.26
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 12 mM MgCl2
4.7
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant mutant L67M
6
5-phospho-alpha-D-ribose 1-diphosphate
recombinant enzyme, pH 8.0, 70°C
10.9
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E196Q
14.2
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E196D
20
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant mutant G69S
20.3
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E196A
23.2
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type enzyme
23.2
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant wild-type enzyme
23.2
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant enzyme, with hypoxanthine
32.2
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, recombinant enzyme, with guanine
36.3
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type enzyme
74.8
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type enzyme, forward reaction
0.002
diphosphate
-
loop II-deletion mutant
0.041
diphosphate
-
wild-type enzyme
0.1
diphosphate
-
pH 7.5, 37°C, recombinant enzyme, with GMP
0.12
diphosphate
-
pH 7.5, 37°C, recombinant mutant L67M
0.31
diphosphate
-
pH 7.5, 37°C, recombinant mutant G69S
0.33
diphosphate
-
mutant E196D
0.47
diphosphate
-
pH 7.5, 37°C, recombinant enzyme, with IMP
0.477
diphosphate
-
wild-type enzyme
0.48
diphosphate
-
pH 7.5, 37°C, recombinant wild-type enzyme
90
diphosphate
-
wild-type enzyme
0.09
GMP
-
pH 7.5, 37°C, recombinant enzyme
5.8
GMP
-
wild-type enzyme, reverse reaction
0.0024
guanine
pH 7.4, 25°C
0.0027
guanine
pH 7.4, 50°C
0.0033
guanine
pH 7.4, 37°C
0.013
guanine
-
purified recombinant chimeric enzyme DS1
0.013
guanine
-
purified recombinant chimeric enzyme DS1
0.039
guanine
-
loop II-deletion mutant
0.06
guanine
unactivated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.1
guanine
unactivated enzyme, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.14
guanine
-
pH 7.4, 25°C, recombinant enzyme, with 5-phospho-alpha-D-ribose 1-diphosphate
0.193
guanine
at pH 7.5 and 25°C
0.21
guanine
-
+/-0.01, 50°C
0.3
guanine
activated enzyme, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.37
guanine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.37
guanine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.4
guanine
activated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
1.1
guanine
-
pH 7.4, 22°C, recombinant mutant L44F
1.2
guanine
-
pH 7.4, 22°C, recombinant wild-type enzyme
1.2
guanine
pH 7.4, 28°C, wild-type enzyme
1.43
guanine
-
+/-0.02, 70°C
2
guanine
recombinant enzyme, pH 8.0, 70°C
3.4
guanine
pH 7.4, 22°C, recombinant mutant F36G
4.3
guanine
-
native enzyme
5
guanine
-
recombinant enzyme
5.7
guanine
-
wild-type enzyme
6.3
guanine
pH 7.4, 22°C, recombinant mutant F36K
10.5
guanine
-
wild-type enzyme
12.1
guanine
-
wild-type enzyme
15.8
guanine
-
mutant enzyme
18
guanine
pH 7.4, 22°C, recombinant mutant F36L
22.1
guanine
-
pH 7.5, 37°C, recombinant mutant G69S
23.8
guanine
recombinant wild-type enzyme, pH 7.4, 25°C
25.5
guanine
pH 7.4, 22°C, recombinant wild-type enzyme
25.5
guanine
pH 7.4, 28°C, wild-type enzyme
32.9
guanine
-
wild-type enzyme
32.9
guanine
-
pH 7.5, 37°C, recombinant wild-type enzyme
32.9
guanine
-
pH 7.5, 37°C, recombinant enzyme
41.3
guanine
-
wild-type enzyme
76.7
guanine
-
wild-type, forward reaction
0.06
hypoxanthine
-
loop II-deletion mutant
0.073
hypoxanthine
-
purified recombinant chimeric enzyme DS1
0.073
hypoxanthine
-
purified recombinant chimeric enzyme DS1
0.1
hypoxanthine
unactivated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.2
hypoxanthine
unactivated enzyme, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.3
hypoxanthine
-
pH 7.5, 37°C, recombinant mutant L67M
0.3
hypoxanthine
activated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.3
hypoxanthine
activated enzyme, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.38
hypoxanthine
-
+/-0.01, 40°C
0.47
hypoxanthine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.47
hypoxanthine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.83
hypoxanthine
-
+/-0.04, 50°C
0.89
hypoxanthine
at pH 7.5 and 25°C
0.9
hypoxanthine
-
pH 7.4, 25°C, recombinant enzyme, with 5-phospho-alpha-D-ribose 1-diphosphate
0.94
hypoxanthine
-
pH 7.4, 22°C, recombinant mutant L44F
1.13
hypoxanthine
-
pH 7.4, 22°C, recombinant wild-type enzyme
1.13
hypoxanthine
pH 7.4, 28°C, wild-type enzyme
1.38
hypoxanthine
-
+/-0.03, 60°C
2.4
hypoxanthine
-
native enzyme
2.6
hypoxanthine
-
wild-type enzyme
2.6
hypoxanthine
-
recombinant enzyme
3.1
hypoxanthine
pH 7.4, 22°C, recombinant mutant F36G
3.16
hypoxanthine
-
+/-0.08, 70°C
3.4
hypoxanthine
pH 7.4, 22°C, recombinant mutant F36K
3.8
hypoxanthine
-
mutant E196R
4.12
hypoxanthine
pH 7.4, 25°C
5.4
hypoxanthine
pH 7.4, 22°C, recombinant mutant F36L
5.7
hypoxanthine
-
wild-type enzyme
5.7
hypoxanthine
-
wild-type enzyme
6.2
hypoxanthine
-
mutant enzyme
6.71
hypoxanthine
-
mutant T47K
7.1
hypoxanthine
pH 7.4, 22°C, recombinant wild-type enzyme
7.1
hypoxanthine
pH 7.4, 28°C, wild-type enzyme
7.97
hypoxanthine
pH 7.4, 37°C
8.5 - 9.3
hypoxanthine
-
recombinant enzyme
8.54
hypoxanthine
-
wild-type enzyme
9
hypoxanthine
recombinant enzyme, pH 8.0, 70°C
9.1
hypoxanthine
pH 7.9, 25°C
13.7
hypoxanthine
-
mutant E196Q
13.8
hypoxanthine
-
mutant E196D
15.9
hypoxanthine
pH 7.4, 50°C
17.1
hypoxanthine
recombinant wild-type enzyme, pH 7.4, 25°C
20.3
hypoxanthine
-
mutant E196A
22
hypoxanthine
-
pH 7.5, 37°C, recombinant mutant G69S
22.9
hypoxanthine
-
wild-type enzyme
22.9
hypoxanthine
-
pH 7.5, 37°C, recombinant wild-type enzyme
22.9
hypoxanthine
-
pH 7.5, 37°C, recombinant enzyme
0.0036
IMP
unactivated enzyme, at pH 7.4 and 23°C
0.0042
IMP
IMP-activated enzyme, at pH 7.4 and 23°C
0.038
IMP
-
wild-type enzyme
0.07
IMP
-
pH 7.5, 37°C, recombinant mutant L67M
0.19
IMP
-
pH 7.5, 37°C, recombinant mutant G69S
0.46
IMP
-
pH 7.5, 37°C, recombinant enzyme
0.47
IMP
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.001
inosine monophosphate
-
loop II-deletion mutant
0.23 - 0.3
inosine monophosphate
-
recombinant enzyme, reverse reaction
0.472
inosine monophosphate
-
wild-type enzyme
77
inosine monophosphate
-
wild-type enzyme
0.062
xanthine
-
purified recombinant chimeric enzyme DS1
0.062
xanthine
-
purified recombinant chimeric enzyme DS1
0.07
xanthine
pH 7.4, 22°C, recombinant mutant F36L
0.08
xanthine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.08
xanthine
pH 7.4, 28°C, recombinant chimeric mutant enzyme
0.2
xanthine
unactivated enzyme, at pH 7.4 and 23°C
0.2
xanthine
unactivated enzyme, in 100 mM Tris-HCl, at pH 7.4 and 23°C
0.3
xanthine
unactivated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
0.68
xanthine
-
+/-0.04, 50°C
0.8
xanthine
activated enzyme, in 10 mM potassium phosphate, at pH 7.4 and 23°C
1
xanthine
activated enzyme, in 100 mM Tris-HCl, at pH 7.4 and 23°C
1.2
xanthine
-
pH 7.4, 22°C, recombinant mutant L44F
1.6
xanthine
IMP-activated enzyme, at pH 7.4 and 23°C
2.2
xanthine
-
+/-0.08, 70°C
2.9
xanthine
-
pH 7.4, 22°C, recombinant wild-type enzyme
2.9
xanthine
pH 7.4, 28°C, wild-type enzyme
additional information
additional information
-
kinetics
-
additional information
additional information
-
kcat of mutant enzymes
-
additional information
additional information
-
wild-type and mutants: kcat for substrates hypoxanthine, guanine, xanthine, IMP, GMP, XMP, diphosphate, 5-phosphoribosyl 1-diphosphate
-
additional information
additional information
-
wild-type and diverse mutant enzymes, overview
-
additional information
additional information
-
increasing kcat with temperature (40-70°C) for all substrates tested
-
additional information
additional information
-
kcat/KM for 5-phospho-alpha-D-ribose 1-diphosphate = 0.00093 mM(-1)*min(-1) at 40°C, 0.00069 mM(-1)*min(-1) at 50°C, 0.00357 mM(-1)*min(-1) at 60°C, 0.00496 mM(-1)*min(-1) at 70°C
-
additional information
additional information
-
kcat/KM for guanine = 0.00262 mM(-1)*min(-1) at 50°C, 0.02631 mM(-1)*min(-1) at 70°C
-
additional information
additional information
-
kcat/KM for hypoxanthine = 0.00579 mM(-1)*min(-1) at 40°C, 0.00708 mM(-1)*min(-1) at 50°C, 0.01719 mM(-1)*min(-1) at 60°C, 0.03107 mM(-1)*min(-1) at 70°C
-
additional information
additional information
-
kcat/KM for hypoxanthine similar to kcat/KM for guanine, kcat/KM for xanthine approximately 20 times lower
-
additional information
additional information
-
kcat/KM for xanthine = 0.00040 mM(-1)*min(-1) at 50°C, 0.00139 mM(-1)*min(-1) at 70°C
-
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0.037
(2-[(2,3-dihydroxypropyl)[2-(6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl]amino]ethyl)phosphonic acid
0.1 M Tris-HCl, 12 mM MgCl2, pH 7.4, 25°C
0.000008 - 0.00006
(2-[(3R,4R)-3-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-4-[(2R)-2-hydroxy-2-phosphonoethoxy]pyrrolidin-1-yl]-2-oxoethyl)phosphonic acid
0.000014 - 0.00008
(2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl)phosphonic acid
0.0014
(2-[[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl][2-(2-phosphonoethoxy)ethyl]amino]ethyl)phosphonic acid
0.1 M Tris-HCl, 12 mM MgCl2, pH 7.4, 25°C
0.00049 - 0.01
(3-hydroxy-2-[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]propyl)phosphonic acid
0.00001
(3-[[(4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]propyl)phosphonic acid
-
pH 7.6, 37°C
0.02 - 0.041
(R)-9-[2-(phosphonomethoxy)propyl]-8-bromoguanine
0.4373
(R)-9-[2-(phosphonomethoxy)propyl]hypoxanthine
-
pH 8.5, 25°C
0.0006 - 0.0059
(R,S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
0.0004 - 0.073
(S)-3-(guanin-9-yl)-pyrrolidin-N-ylacetylphosphonic acid
0.015 - 0.045
(S)-9-[2-(phosphonomethoxy)propyl]-8-azaguanine
0.011 - 0.3
(S)-9-[2-(phosphonomethoxy)propyl]-8-bromoguanine
0.0648 - 0.1823
(S)-9-[2-(phosphonomethoxy)propyl]hypoxanthine
0.0284 - 0.1768
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
0.0000276 - 0.01
3-((7-hydroxy-1H-pyrazolo[4,3-d]pyrimidin-3-yl)methylamino)propylphosphonate
0.037 - 0.423
5-phospho-alpha-D-ribose 1-diphosphate
0.5 - 1
6-methylheptyl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
0.0134
9-[(N-phosphonoethyl-N-phosphonobutyl)-2-aminoethyl]hypoxanthine
0.1 M Tris-HCl, 12 mM MgCl2, pH 7.4, 25°C
0.00075
9-[(N-phosphonoethyl-N-phosphonoethoxyethyl)-2-aminoethyl]-hypoxanthine
0.1 M Tris-HCl, 12 mM MgCl2, pH 7.4, 25°C
0.00167
9-[(N-phosphonoethyl-N-phosphonomethoxyethyl)-2-aminoethyl]hypoxanthine
0.1 M Tris-HCl, 12 mM MgCl2, pH 7.4, 25°C
0.0218
9-[(N-phosphonoethyl-N-phosphonomethyl)-2-aminoethyl]-hypoxanthine
0.1 M Tris-HCl, 12 mM MgCl2, pH 7.4, 25°C
0.0001 - 0.001
9-[2-(2-phosphonoethoxy)ethyl]guanine
0.0003 - 0.0036
9-[2-(2-phosphonoethoxy)ethyl]hypoxanthine
0.0036 - 0.0227
9-[2-(phosphonomethoxy)-3-fluoro-propyl]guanine
0.1 - 1
9-[2-(phosphonomethoxy)ethyl]-6-thioguanine
0.0043 - 0.0072
9-[2-(phosphonomethoxy)ethyl]-7-deaza-8-azahypoxanthine
0.003 - 0.175
9-[2-(phosphonomethoxy)ethyl]-8-azaguanine
0.01 - 0.4
9-[2-(phosphonomethoxy)ethyl]-8-bromoguanine
0.0016 - 0.0559
9-[2-(phosphonomethoxy)ethyl]guanine
0.0012 - 0.068
9-[2-(phosphonomethoxy)ethy]-8-hydroxyguanine
0.0254
ADP
-
mutant K134S, competitive versus 5-phospho-alpha-D-ribose 1-diphosphate
0.001 - 0.019
cyclic (R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
0.008 - 0.1151
cyclic (S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
0.093 - 0.302
diphosphate
0.0058 - 0.01
guanine ribose 5'-phosphate
0.023 - 0.08
hypoxanthine
0.0036 - 0.0054
hypoxanthine ribose 5'-phosphate
0.017
monophosphonate-2-(phosphonoethoxy)ethyl hypoxanthine
pH and temperature not specified in the publication
0.14 - 0.2
propan-2-yl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
0.000019 - 0.01
[(+/-)-2(R/S)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
0.0094 - 0.01
[(+/-)-2(R/S)-[([2-chloro-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
0.0000013 - 0.000006
[(1S)-1-hydroxy-2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl]phosphonic acid
0.0000143 - 0.01
[(2R)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
0.0000024 - 0.01
[(2R)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
0.00065 - 0.01
[(2S)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
0.00098 - 0.01
[(2S,3R)-2,4-dihydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butoxy]phosphonic acid
0.0000012 - 0.042
[(3R)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
0.000087 - 0.01
[(3S)-1,1-difluoro-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
0.0001 - 0.01
[(3S)-3-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-1,1-difluoro-4-hydroxybutyl]phosphonic acid
0.00000065 - 0.00038
[(3S)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
0.00000065
[(3S)-4-hydroxy-3-[[(4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]butyl]phosphonic acid
-
pH 7.6, 37°C
0.0000091 - 0.01
[2-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl] phosphonic acid
0.00062 - 0.01
[2-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]ethyl]phosphonic acid
0.01 - 0.0144
[2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethoxy]phosphonic acid
0.000006 - 0.00007
[3-(guanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methylphosphonic acid
0.01 - 0.0153
[3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-2-(hydroxymethyl)propoxy]phosphonic acid
0.01132 - 0.02
[3-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]propyl]phosphonic acid
0.000003 - 0.00002
[3R,4R]-4-guanin-9-yl-3-((S)-2-hydroxy-2-phosphonoethyl)oxy-1-N-(phosphonopropionyl)pyrrolidine
0.00049 - 0.01
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
0.0019 - 0.01
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethyl]phosphonic acid
0.01 - 0.02
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]phosphonic acid
0.0086 - 0.01
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]pentyl]phosphonic acid
0.0000106 - 0.0049
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl]phosphonic acid
0.0008
[[2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]propane-1,3-diyl]bis(oxymethylene)]bis(phosphonic acid)
0.1 M Tris-HCl, 12 mM MgCl2, pH 7.4, 25°C
0.0028
[[[(4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]azanediyl]di(propane-3,1-diyl)]bis(phosphonic acid)
0.1 M Tris-HCl, 12 mM MgCl2, pH 7.4, 25°C
additional information
additional information
-
0.000008
(2-[(3R,4R)-3-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-4-[(2R)-2-hydroxy-2-phosphonoethoxy]pyrrolidin-1-yl]-2-oxoethyl)phosphonic acid
pH not specified in the publication, 37°C
0.00001
(2-[(3R,4R)-3-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-4-[(2R)-2-hydroxy-2-phosphonoethoxy]pyrrolidin-1-yl]-2-oxoethyl)phosphonic acid
pH not specified in the publication, 37°C
0.00006
(2-[(3R,4R)-3-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)-4-[(2R)-2-hydroxy-2-phosphonoethoxy]pyrrolidin-1-yl]-2-oxoethyl)phosphonic acid
pH not specified in the publication, 37°C
0.000014
(2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl)phosphonic acid
pH not specified in the publication, 37°C
0.00008
(2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl)phosphonic acid
pH not specified in the publication, 37°C
0.00049
(3-hydroxy-2-[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]propyl)phosphonic acid
at pH 7.6 and 37°C
0.01
(3-hydroxy-2-[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]propyl)phosphonic acid
-
at pH 7.6 and 37°C
0.02
(R)-9-[2-(phosphonomethoxy)propyl]-8-bromoguanine
-
pH 7.4, 25°C
0.041
(R)-9-[2-(phosphonomethoxy)propyl]-8-bromoguanine
pH 7.4, 25°C
0.0006
(R,S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
pH 7.4, 25°C
0.0059
(R,S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
pH 7.4, 25°C
0.0004
(S)-3-(guanin-9-yl)-pyrrolidin-N-ylacetylphosphonic acid
pH not specified in the publication, 37°C
0.0026
(S)-3-(guanin-9-yl)-pyrrolidin-N-ylacetylphosphonic acid
pH not specified in the publication, 37°C
0.073
(S)-3-(guanin-9-yl)-pyrrolidin-N-ylacetylphosphonic acid
pH not specified in the publication, 37°C
0.015
(S)-9-[2-(phosphonomethoxy)propyl]-8-azaguanine
pH 7.4, 25°C
0.045
(S)-9-[2-(phosphonomethoxy)propyl]-8-azaguanine
-
above, pH 7.4, 25°C
0.011
(S)-9-[2-(phosphonomethoxy)propyl]-8-bromoguanine
-
pH 7.4, 25°C
0.3
(S)-9-[2-(phosphonomethoxy)propyl]-8-bromoguanine
above, pH 7.4, 25°C
0.0648
(S)-9-[2-(phosphonomethoxy)propyl]hypoxanthine
-
pH 8.5, 25°C
0.1823
(S)-9-[2-(phosphonomethoxy)propyl]hypoxanthine
pH 8.5, 25°C
0.0284
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
pH 8.5, 25°C
0.1768
(S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
pH 8.5, 25°C
0.0000276
3-((7-hydroxy-1H-pyrazolo[4,3-d]pyrimidin-3-yl)methylamino)propylphosphonate
at pH 7.6 and 37°C
0.01
3-((7-hydroxy-1H-pyrazolo[4,3-d]pyrimidin-3-yl)methylamino)propylphosphonate
-
at pH 7.6 and 37°C
0.037
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, product inhibition versus IMP, substrate hypoxanthine, recombinant enzyme
0.138
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, product inhibition versus diphosphate, substrate hypoxanthine, recombinant enzyme
0.298
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, product inhibition versus diphosphate, substrate guanine, recombinant enzyme
0.423
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37°C, product inhibition versus GMP, substrate guanine, recombinant enzyme
0.5
6-methylheptyl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
-
above, pH 7.4, 25°C
1
6-methylheptyl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
above, pH 7.4, 25°C
0.0001
9-[2-(2-phosphonoethoxy)ethyl]guanine
-
pH 7.4, 25°C
0.001
9-[2-(2-phosphonoethoxy)ethyl]guanine
pH 7.4, 25°C
0.0003
9-[2-(2-phosphonoethoxy)ethyl]hypoxanthine
-
pH 7.4, 25°C
0.0036
9-[2-(2-phosphonoethoxy)ethyl]hypoxanthine
pH 7.4, 25°C
0.0036
9-[2-(phosphonomethoxy)-3-fluoro-propyl]guanine
-
pH 8.5, 25°C
0.0227
9-[2-(phosphonomethoxy)-3-fluoro-propyl]guanine
pH 8.5, 25°C
0.1
9-[2-(phosphonomethoxy)ethyl]-6-thioguanine
-
above, pH 7.4, 25°C
1
9-[2-(phosphonomethoxy)ethyl]-6-thioguanine
above, pH 7.4, 25°C
0.0043
9-[2-(phosphonomethoxy)ethyl]-7-deaza-8-azahypoxanthine
pH 7.4, 25°C
0.0072
9-[2-(phosphonomethoxy)ethyl]-7-deaza-8-azahypoxanthine
-
pH 7.4, 25°C
0.003
9-[2-(phosphonomethoxy)ethyl]-8-azaguanine
-
pH 7.4, 25°C
0.175
9-[2-(phosphonomethoxy)ethyl]-8-azaguanine
pH 7.4, 25°C
0.01
9-[2-(phosphonomethoxy)ethyl]-8-bromoguanine
-
pH 7.4, 25°C
0.4
9-[2-(phosphonomethoxy)ethyl]-8-bromoguanine
above, pH 7.4, 25°C
0.0016
9-[2-(phosphonomethoxy)ethyl]guanine
-
pH 7.4, 25°C
0.0189
9-[2-(phosphonomethoxy)ethyl]guanine
-
pH 8.5, 25°C
0.029
9-[2-(phosphonomethoxy)ethyl]guanine
pH 7.4, 25°C
0.0559
9-[2-(phosphonomethoxy)ethyl]guanine
pH 8.5, 25°C
0.0012
9-[2-(phosphonomethoxy)ethy]-8-hydroxyguanine
-
pH 7.4, 25°C
0.068
9-[2-(phosphonomethoxy)ethy]-8-hydroxyguanine
pH 7.4, 25°C
0.001
cyclic (R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
pH 7.4, 25°C
0.0014
cyclic (R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
pH 8.5, 25°C
0.0123
cyclic (R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
pH 8.5, 25°C
0.019
cyclic (R)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
pH 7.4, 25°C
0.008
cyclic (S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
pH 7.4, 25°C
0.0377
cyclic (S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
-
pH 8.5, 25°C
0.09
cyclic (S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
pH 7.4, 25°C
0.1151
cyclic (S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine
pH 8.5, 25°C
0.093
diphosphate
-
pH 7.5, 37°C, product inhibition versus 5-phospho-alpha-D-ribose 1-diphosphate, substrate guanine, recombinant enzyme
0.122
diphosphate
-
pH 7.5, 37°C, product inhibition versus 5-phospho-alpha-D-ribose 1-diphosphate, substrate hypoxanthine, recombinant enzyme
0.122
diphosphate
-
pH 7.5, 37°C, product inhibition versus hypoxanthine, substrate hypoxanthine, recombinant enzyme
0.302
diphosphate
-
pH 7.5, 37°C, product inhibition versus guanine, substrate guanine, recombinant enzyme
0.02
GMP
-
pH 7.5, 37°C, product inhibition versus 5-phospho-alpha-D-ribose 1-diphosphate, substrate guanine, recombinant enzyme
0.0305
GMP
recombinant wild-type enzyme, pH 7.4, 25°C
0.1
GMP
-
pH 7.5, 37°C, product inhibition versus guanine, substrate guanine, recombinant enzyme
0.004
guanine
-
-
0.0058
guanine ribose 5'-phosphate
pH 7.4, 25°C
0.01
guanine ribose 5'-phosphate
-
pH 7.4, 25°C
0.023
hypoxanthine
-
-
0.0036
hypoxanthine ribose 5'-phosphate
-
pH 7.4, 25°C
0.0054
hypoxanthine ribose 5'-phosphate
pH 7.4, 25°C
0.037
IMP
-
pH 7.5, 37°C, product inhibition versus 5-phospho-alpha-D-ribose 1-diphosphate, substrate hypoxanthine, recombinant enzyme
0.045
IMP
-
pH 7.4, 12 mM MgCl2, versus 5-phospho-alpha-D-ribose 1-diphosphate
0.0773
IMP
recombinant wild-type enzyme, pH 7.4, 25°C
0.138
IMP
-
pH 7.5, 37°C, product inhibition versus hypoxanthine, substrate hypoxanthine, recombinant enzyme
0.14
propan-2-yl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
pH 7.4, 25°C
0.2
propan-2-yl hydrogen {[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethoxy]methyl}phosphonate
-
above, pH 7.4, 25°C
0.000019
[(+/-)-2(R/S)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
at pH 7.6 and 37°C
0.01
[(+/-)-2(R/S)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
-
at pH 7.6 and 37°C
0.0094
[(+/-)-2(R/S)-[([2-chloro-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
at pH 7.6 and 37°C
0.01
[(+/-)-2(R/S)-[([2-chloro-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
at pH 7.6 and 37°C
0.0000013
[(1S)-1-hydroxy-2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl]phosphonic acid
pH not specified in the publication, 37°C
0.000002
[(1S)-1-hydroxy-2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl]phosphonic acid
pH not specified in the publication, 37°C
0.000006
[(1S)-1-hydroxy-2-[[(3R,4R)-4-(6-oxo-1,6-dihydro-9H-purin-9-yl)-1-(phosphonoacetyl)pyrrolidin-3-yl]oxy]ethyl]phosphonic acid
pH not specified in the publication, 37°C
0.0000143
[(2R)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
at pH 7.6 and 37°C
0.01
[(2R)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
at pH 7.6 and 37°C
0.0000024
[(2R)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
at pH 7.6 and 37°C
0.01
[(2R)-3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propoxy]phosphonic acid
-
at pH 7.6 and 37°C
0.00065
[(2S)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
at pH 7.6 and 37°C
0.01
[(2S)-2-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-3-hydroxypropoxy]phosphonic acid
-
at pH 7.6 and 37°C
0.00098
[(2S,3R)-2,4-dihydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butoxy]phosphonic acid
at pH 7.6 and 37°C
0.01
[(2S,3R)-2,4-dihydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butoxy]phosphonic acid
-
at pH 7.6 and 37°C
0.0000012
[(3R)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
at pH 7.6 and 37°C
0.0000234
[(3R)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
at pH 7.6 and 37°C
0.016
[(3R)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
at pH 7.6 and 37°C
0.042
[(3R)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
at pH 7.6 and 37°C
0.000087
[(3S)-1,1-difluoro-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
at pH 7.6 and 37°C
0.01
[(3S)-1,1-difluoro-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
at pH 7.6 and 37°C
0.0001
[(3S)-3-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-1,1-difluoro-4-hydroxybutyl]phosphonic acid
at pH 7.6 and 37°C
0.01
[(3S)-3-[([2-amino-4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-1,1-difluoro-4-hydroxybutyl]phosphonic acid
-
at pH 7.6 and 37°C
0.00000065
[(3S)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
at pH 7.6 and 37°C
0.00038
[(3S)-4-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
at pH 7.6 and 37°C
0.0000091
[2-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl] phosphonic acid
at pH 7.6 and 37°C
0.01
[2-hydroxy-3-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl] phosphonic acid
-
at pH 7.6 and 37°C
0.00062
[2-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]ethyl]phosphonic acid
at pH 7.6 and 37°C
0.01
[2-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]ethyl]phosphonic acid
-
at pH 7.6 and 37°C
0.01
[2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethoxy]phosphonic acid
-
at pH 7.6 and 37°C
0.0144
[2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethoxy]phosphonic acid
at pH 7.6 and 37°C
0.000006
[3-(guanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methylphosphonic acid
pH 7.4, temperature not specified in the publication
0.00007
[3-(guanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methylphosphonic acid
pH 7.4, temperature not specified in the publication
0.01
[3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-2-(hydroxymethyl)propoxy]phosphonic acid
-
at pH 7.6 and 37°C
0.0153
[3-hydroxy-2-[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]-2-(hydroxymethyl)propoxy]phosphonic acid
at pH 7.6 and 37°C
0.01132
[3-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]propyl]phosphonic acid
-
at pH 7.6 and 37°C
0.02
[3-[(2-[4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]ethyl)amino]propyl]phosphonic acid
at pH 7.6 and 37°C
0.000003
[3R,4R]-4-guanin-9-yl-3-((S)-2-hydroxy-2-phosphonoethyl)oxy-1-N-(phosphonopropionyl)pyrrolidine
pH not specified in the publication, 37°C
0.000007
[3R,4R]-4-guanin-9-yl-3-((S)-2-hydroxy-2-phosphonoethyl)oxy-1-N-(phosphonopropionyl)pyrrolidine
pH not specified in the publication, 37°C
0.000008
[3R,4R]-4-guanin-9-yl-3-((S)-2-hydroxy-2-phosphonoethyl)oxy-1-N-(phosphonopropionyl)pyrrolidine
pH not specified in the publication, 37°C
0.00002
[3R,4R]-4-guanin-9-yl-3-((S)-2-hydroxy-2-phosphonoethyl)oxy-1-N-(phosphonopropionyl)pyrrolidine
pH not specified in the publication, 37°C
0.00049
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
at pH 7.6 and 37°C
0.01
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]butyl]phosphonic acid
-
at pH 7.6 and 37°C
0.0019
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethyl]phosphonic acid
at pH 7.6 and 37°C
0.01
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]ethyl]phosphonic acid
-
at pH 7.6 and 37°C
0.01
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]phosphonic acid
-
at pH 7.6 and 37°C
0.02
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]methyl]phosphonic acid
at pH 7.6 and 37°C
0.0086
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]pentyl]phosphonic acid
at pH 7.6 and 37°C
0.01
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]pentyl]phosphonic acid
-
at pH 7.6 and 37°C
0.0000106
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl]phosphonic acid
at pH 7.6 and 37°C
0.0049
[[([4-hydroxy-5H-pyrrolo[3,2-d]pyrimidin-7-yl]methyl)amino]propyl]phosphonic acid
-
at pH 7.6 and 37°C
additional information
additional information
-
kinetics of product inhibition in forward reaction
-
additional information
additional information
-
overview, inhibition constants for diverse purine nucleotides and analogues
-
additional information
additional information
-
kinetics for product inhibition in forward and reverse reaction, wild-type enzyme
-
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evolution
adenylate kinase (EC 2.7.4.3, AMPK) belongs to nucleoside-5'-monophosphate kinase (NMPK) family. ZgHGPRT/AMPK belongs to class I PRTs, which display a conserved 13-residue fingerprint region (PRPP binding-motif) in their amino acid sequence
evolution
four substitutions are identified in the region of the active site between SmHGPRT and human HGPRT: Ile149Met, Pro176Arg, Val189Ile, and Arg192Lys
evolution
-
adenylate kinase (EC 2.7.4.3, AMPK) belongs to nucleoside-5'-monophosphate kinase (NMPK) family. ZgHGPRT/AMPK belongs to class I PRTs, which display a conserved 13-residue fingerprint region (PRPP binding-motif) in their amino acid sequence
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evolution
-
adenylate kinase (EC 2.7.4.3, AMPK) belongs to nucleoside-5'-monophosphate kinase (NMPK) family. ZgHGPRT/AMPK belongs to class I PRTs, which display a conserved 13-residue fingerprint region (PRPP binding-motif) in their amino acid sequence
-
evolution
-
adenylate kinase (EC 2.7.4.3, AMPK) belongs to nucleoside-5'-monophosphate kinase (NMPK) family. ZgHGPRT/AMPK belongs to class I PRTs, which display a conserved 13-residue fingerprint region (PRPP binding-motif) in their amino acid sequence
-
evolution
-
adenylate kinase (EC 2.7.4.3, AMPK) belongs to nucleoside-5'-monophosphate kinase (NMPK) family. ZgHGPRT/AMPK belongs to class I PRTs, which display a conserved 13-residue fingerprint region (PRPP binding-motif) in their amino acid sequence
-
evolution
-
adenylate kinase (EC 2.7.4.3, AMPK) belongs to nucleoside-5'-monophosphate kinase (NMPK) family. ZgHGPRT/AMPK belongs to class I PRTs, which display a conserved 13-residue fingerprint region (PRPP binding-motif) in their amino acid sequence
-
malfunction
a deficiency in HPRT activity leads to overproduction of uric acid, hyperuricemia, with gouty arthritis, nephrolithiasis, and mild neurologic symptoms. According to the degree of enzymatic deficiency, a large spectrum of neurologic features can also be observed, ranging from mild or no neurologic involvement to complete Lesch-Nyhan disease
malfunction
-
complete deficiency of hypoxanthine-guanine phosphoribosyltransferase causes the Lesch-Nyhan disease, a genetic disorder associated with motor and psychiatric disturbance and self-injurious behaviour, the role of serotonin receptor 2C, HTR2C, might be involved, overview
malfunction
-
HPRT deficiency influences early developmental processes controlling the dopaminergic phenotype, and is involved in Lesch-Nyhan disease pathogenesis
malfunction
-
mutations in the gene encoding the purine biosynthetic enzyme HPRT cause the resulting intractable and largely untreatable neurological impairment of Lesch-Nyhan disease. The disorder is associated with a defect in basal ganglia DA pathways, phenotype mechanisms analysis in human embryonic carcinoma neurogenesis model, overview
malfunction
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enzyme knockdown causes a marked switch from neuronal to glial gene expression and dysregulates expression of Sox2 and its regulator, genes vital for stem cell pluripotency and for the neuronal/glial cell fate decision. In addition, enzyme deficiency dysregulates many cellular functions controlling cell cycle and proliferation mechanisms, RNA metabolism, DNA replication and repair, replication stress, lysosome function, membrane trafficking, signaling pathway for platelet activation multiple neurotransmission systems and sphingolipid, sulfur and glycan metabolism
malfunction
deletion of the HGPRT gene (DELTAhgprt) in the model organism Mycobacterium smegmatis confirms that this enzyme is not essential for Mycobacterium smegmatis' growth
malfunction
the Lesch-Nyhan disease (LND) is a rare X-linked inherited neurogenetic disorder of purine metabolism in which the enzyme hypoxanthine-guanine phosphoribosyltransferase (HGprt) is defective. The role of the amyloid precursor protein (APP) gene in neuropathology is associated with HGprt-deficiency in LND. Classical features of LND include hyperuricemia and its sequelae (gout, nephrolithiasis, and tophi), motor disability (dystonia, chorea, and spasticity), intellectual impairment, and self-injurious behaviors such as self-biting, self-hitting, eye poking, and others. Self-injurious behavior is universal in LND. It usually emerges before 4 years of age, but may be delayed until the second decade of life. Etiology involves a mutation of the housekeeping hypoxanthine phosphoribosyltransferase 1 (HPRT1) gene that is located on the long arm of the X chromosome (Xq26.1)
malfunction
-
deletion of the HGPRT gene (DELTAhgprt) in the model organism Mycobacterium smegmatis confirms that this enzyme is not essential for Mycobacterium smegmatis' growth
-
malfunction
-
deletion of the HGPRT gene (DELTAhgprt) in the model organism Mycobacterium smegmatis confirms that this enzyme is not essential for Mycobacterium smegmatis' growth
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metabolism
-
comparison of growth characteristics including intracellular protein levels, RNA content, and nucleotide pool sizes between the extreme halophile Halobacterium halobium and the moderate halophile Haloferax volcanii. The differences in the metabolism of purine bases and nucleosides and the sensitivity to purine analogs between the two halobacteria are reflected in differences in purine enzyme levels
metabolism
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comparison of growth characteristics including intracellular protein levels, RNA content, and nucleotide pool sizes between the extreme halophile Halobacterium halobium and the moderate halophile Haloferax volcanii. The differences in the metabolism of purine bases and nucleosides and the sensitivity to purine analogs between the two halobacteria are reflected in differences in purine enzyme levels
metabolism
analysis of the molecular basis to understand the 6-oxopurine salvage in Trypansoma brucei
metabolism
in Escherichia coli, the purine salvage pathway has two 6-oxopurine phosphoribosyltransferases (PRTs), xanthine-guanine PRT (EcXGPRT, EC 2.4.2.22) and hypoxanthine PRT (EcHPRT, EC 2.4.2.8). Escherichia coli can utilize both purine salvage and de novo pathways for the production of the nucleoside monophosphates required for incorporation into DNA and RNA. Escherichia coli is highly unusual in that it is one of only a few organisms that possess two distinct salvage enzymes for 6-oxopurine nucleoside monophosphate production
metabolism
Schistosoma mansoni parasite lacks the de novo purine biosynthetic pathway and depends entirely on the purine salvage pathway for the supply of purines. Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is a key enzyme of the purine salvage pathway
metabolism
-
the enzyme is important in the purine metabolism pathways. Analysis and comparison of plasma and red blood cell hypoxanthine and inosine monophosphate concentrations and enzyme activities from bottlenose dolphins (Tursiops truncatus) and humans, overview. Hypoxanthine and inosine monophosphate concentrations are higher in plasma from dolphins than humans. Plasma hypoxanthine-guanine phosphoribosyltransferase (HGPRT) activity in dolphins suggests an elevated purine recycling rate, and a mechanism for avoiding accumulation of non-recyclable purines (xanthine and uric acid). Red blood cell concentrations of hypoxanthine, adenosine diphosphate, ATP, and guanosine triphosphate are lower in dolphins than in humans. Adenosine monophosphate and nicotinamide adenine dinucleotide concentrations are higher in dolphins. HGPRT activity in red blood cells is higher in humans than in dolphins. The lower concentrations of purine catabolism and recycling by-products in plasma from dolphins ca be beneficial in providing substrates for recovery of ATP-depletion during diving or vigorous swimming. The results suggest that purine salvage in dolphins could be a mechanism for delivering nucleotide precursors to tissues with high ATP and guanosine triphosphate requirements
metabolism
the enzyme is important in the purine metabolism pathways. Analysis and comparison of plasma and red blood cell hypoxanthine and inosine monophosphate concentrations and enzyme activities from bottlenose dolphins (Tursiops truncatus) and humans, overview. Hypoxanthine and inosine monophosphate concentrations are higher in plasma from dolphins than humans. Red blood cell concentrations of hypoxanthine, adenosine diphosphate, ATP, and guanosine triphosphate are lower in dolphins than in humans. Adenosine monophosphate and nicotinamide adenine dinucleotide concentrations are higher in dolphins. HGPRT activity in red blood cells is higher in humans than in dolphins
metabolism
the metabolism of the protozoan parasite Trypanosoma cruzi depends on the salvage of exogenous purines for nucleotide synthesis. In this context, TcHPRT plays a key role in the survival of trypanosomes in their hosts
physiological function
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HPRT is a housekeeping enzyme responsible for recycling purines, it regulates early developmental programming of dopamine neurons
physiological function
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the enzyme enables the reutilization of purine base adenine converting it to mononucleotide AMP, substrate for the synthesis of high-energy nucleotides
physiological function
-
the enzyme enables the reutilization of purine base adenine converting it to mononucleotide AMP, substrate for the synthesis of high-energy nucleotides
physiological function
-
the enzyme is involved in the specification and development of neurons, including dopaminergic neurons, as well as in the regulation of dopaminergic transcription factors, overview
physiological function
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the purine salvage enzyme HGXPRT is essential for purine nucleotide and hence nucleic acid synthesis in the malaria parasite
physiological function
production of enzyme-deficient human Coxsackievirus-induced pluripotent stem cells and human HUES11 embryonic stem cells using shRNA. Both cells show >99% enzyme knock-down and demonstrate markedly decreased expression of the purinergic P2Y1 receptor mRNA. In Coxsackievirus-induced cells, P2Y1 mRNA and protein down-regulation by hypoxanthine phosphoribosyltransferase knockdown is refractory to activation by the P2Y1 receptor agonist ATP and shows aberrant purinergic signaling, as reflected by marked deficiency of the transcription factor pCREB and constitutive activation of the MAP kinases phospho-ERK1/2. Moreover, hypoxanthine phosphoribosyltransferase-knockdown Coxsackievirus-induced cells also demonstrate marked reduction of phosphorylated beta-catenin
physiological function
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treatment of cells with guanosine and GMP results in statistically significant decreases in cell growth after 48 h and 72 h in the melanoma cell line C32 and in the U-87 glioma cell line. Presence of hypoxanthine blocks the antiproliferative effects. Hypoxanthine phosphoribosyltransferase-negative cell line C32-TG cells completely has lost the inhibitory response to guanine treatment. Hypoxanthine phosphoribosyltransferase silencing by siRNA is able to partially block the guanine-induced antiproliferative effects in U-87 glioma cell lines
physiological function
6-oxopurine phosphoribosyltransferase (PRT) is an enzyme central to the purine salvage pathway, whose activity is critical for the production of nucleotides GMP and IMP that are required for DNA/RNA synthesis within the protozoan parasite
physiological function
having functional salvage pathway enzymes is important in the survival and functionality of mammalian cells. Salvage enzymes, such as HPRT, are known as common housekeeping genes, and are integral in several daily cellular functions regulating cell proliferation and cell cycle progression
physiological function
hypoxanthine is a key precursor salvaged for purine nucleotide synthesis in Plasmodium falciparum, and the most critical enzyme is hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRT) which catalyzes the freely reversible Mg2+-dependent conversion of 6-oxopurine bases to their respective nucleotides and diphosphate. The phosphoribosyl group is derived from 5-phospho-alpha-D-ribosyl 1-diphosphate (PRPP). The enzyme from malaria parasites (PfHGXPRT) is essential as hypoxanthine is the major precursor in purine metabolism
physiological function
hypoxanthine-guanine phosphoribosyltransferase (HGPRT) catalyzes the formation of guanosine-5'-monophosphate from guanine and inosine-5'-monophosphate from hypoxanthine. It is the key enzyme in the purine salvage pathway, catalyzes the synthesis of inosine- or guanosine-5'-monophosphate via replacement of the 1-diphosphate group in phosphoribosyl diphosphate with a corresponding free nucleobase. Deletion of the HGPRT gene (DELTAhgprt) in the model organism Mycobacterium smegmatis confirms that this enzyme is not essential for Mycobacterium smegmatis' growth
physiological function
hypoxanthine-guanine-(xanthine) phosphoribosyltransferases, HG(X)PRTs, catalyze the formation of the 6-oxopurine nucleoside monophosphates from a nucleobase and from 5'-phospho-alpha-D-ribosyl-1-diphosphate
physiological function
hypoxanthine-guanine-(xanthine) phosphoribosyltransferases, HG(X)PRTs, catalyze the formation of the 6-oxopurine nucleoside monophosphates from a nucleobase and from 5'-phospho-alpha-D-ribosyl-1-pyrophosphate
physiological function
hypoxanthine-guanine-xanthine phosphoribosyltransference (HGXPRT) is a key enzyme in the purine salvage pathway of the malarial parasite, Plasmodium falciparum (Pf). It catalyses the conversion of hypoxanthine, guanine, and xanthine to their corresponding mononucleotides; IMP, GMP, and XMP, respectively
physiological function
the activity of hypoxanthine-guanine-[xanthine]-phosphoribosyltransferase, HG[X]PRT is essential for the growth of Plasmodium parasites
physiological function
the hypoxanthine phosphoribosyl transferase (TcHPRT) is a critical enzyme in Trypanosoma cruzi for the survival of the parasite. TcHPRT catalyzes the transfer of a mono phosphorylated ribose from phosphoribosyl diphosphate (PRPP) to the purine ring
physiological function
the Zobellia galactanivorans enzyme contains both HGPRT (N-terminal part) and AMPK (C-terminal part) domains. The N-terminal HGPRT module is involved in the purine salvage and converts hypoxanthine to inosine-5'-monophosphate (IMP) and guanine to guanosine-5'-monophosphate (GMP)
physiological function
-
the Zobellia galactanivorans enzyme contains both HGPRT (N-terminal part) and AMPK (C-terminal part) domains. The N-terminal HGPRT module is involved in the purine salvage and converts hypoxanthine to inosine-5'-monophosphate (IMP) and guanine to guanosine-5'-monophosphate (GMP)
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physiological function
-
the Zobellia galactanivorans enzyme contains both HGPRT (N-terminal part) and AMPK (C-terminal part) domains. The N-terminal HGPRT module is involved in the purine salvage and converts hypoxanthine to inosine-5'-monophosphate (IMP) and guanine to guanosine-5'-monophosphate (GMP)
-
physiological function
-
hypoxanthine-guanine phosphoribosyltransferase (HGPRT) catalyzes the formation of guanosine-5'-monophosphate from guanine and inosine-5'-monophosphate from hypoxanthine. It is the key enzyme in the purine salvage pathway, catalyzes the synthesis of inosine- or guanosine-5'-monophosphate via replacement of the 1-diphosphate group in phosphoribosyl diphosphate with a corresponding free nucleobase. Deletion of the HGPRT gene (DELTAhgprt) in the model organism Mycobacterium smegmatis confirms that this enzyme is not essential for Mycobacterium smegmatis' growth
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physiological function
-
the Zobellia galactanivorans enzyme contains both HGPRT (N-terminal part) and AMPK (C-terminal part) domains. The N-terminal HGPRT module is involved in the purine salvage and converts hypoxanthine to inosine-5'-monophosphate (IMP) and guanine to guanosine-5'-monophosphate (GMP)
-
physiological function
-
hypoxanthine-guanine phosphoribosyltransferase (HGPRT) catalyzes the formation of guanosine-5'-monophosphate from guanine and inosine-5'-monophosphate from hypoxanthine. It is the key enzyme in the purine salvage pathway, catalyzes the synthesis of inosine- or guanosine-5'-monophosphate via replacement of the 1-diphosphate group in phosphoribosyl diphosphate with a corresponding free nucleobase. Deletion of the HGPRT gene (DELTAhgprt) in the model organism Mycobacterium smegmatis confirms that this enzyme is not essential for Mycobacterium smegmatis' growth
-
physiological function
-
the Zobellia galactanivorans enzyme contains both HGPRT (N-terminal part) and AMPK (C-terminal part) domains. The N-terminal HGPRT module is involved in the purine salvage and converts hypoxanthine to inosine-5'-monophosphate (IMP) and guanine to guanosine-5'-monophosphate (GMP)
-
physiological function
-
the Zobellia galactanivorans enzyme contains both HGPRT (N-terminal part) and AMPK (C-terminal part) domains. The N-terminal HGPRT module is involved in the purine salvage and converts hypoxanthine to inosine-5'-monophosphate (IMP) and guanine to guanosine-5'-monophosphate (GMP)
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additional information
crystal structures of the enzyme in complex with GMP and IMP and with three acyclic nucleoside phosphonate (ANP) inhibitors are determined. Structure comparisons, overview. One of the most important interactions between a 6-oxopurine PRT and the nucleoside monophosphate is the hydrogen bond between the 6-oxo group and a highly conserved lysine side-chain, K145 in TbrHGPRT. This bond is critical in discriminating the 6-oxopurine from a 6-aminopurine, such as adenine
additional information
crystals of enzyme-diphosphate-GMP complex are used for structure determination, detailed overview
additional information
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crystals of enzyme-diphosphate-GMP complex are used for structure determination, detailed overview
additional information
determination of primary (1-14C and 9-15N) and secondary (1-3H and 7-15N) intrinsic kinetic isotope effect (KIE) values for PfHGXPRT, mass spectrometry. Intrinsic isotope effects contain information for understanding enzymatic transition state properties. The transition state of PfHGXPRT is explored by matching KIE values predicted from quantum mechanical calculations to the intrinsic values determined experimentally. This approach provides information about PfHGXPRT transition state bond lengths, geometry, and atomic charge distribution. The transition state structure of PfHGXPRT is determined in the physiological direction of addition of ribose 5-phosphate to hypoxanthine by overcoming the chemical instability of PRPP. The transition state for PfHGXPRT forms nucleotides through a well-developed and near-symmetrical DN*AN, SN1-like transition state. Structure comparisons to the human enzyme, overview
additional information
identification of a putative dual-domain hypoxanthine-guanine phosphoribosyltransferase (HGPRT)/adenylate kinase (AMPK). ZgHGPRT/AMPK single domain, dual domain 3D structure homology modeling, HGPRT from Leptospira interrogans (PDB ID 4QRI) and AMPK structure from Geobacillus stearothermophilus (PDB ID 1ZIN) are used as templates. ZgHGPRT/AMPK model is complexed with Hyp, PRPP and Mg2+ in the active site of the HGPRT domain, and with AMP, ATP and Mg2+ in the active site of AMPK domain. Essential elements of type I PRTs architecture are found in ZgHGPRT/AMPK amino acid sequence such as diphosphate loop, the flexible loop and PRPP binding domain (including PRPP loop), as well as in the homology model
additional information
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identification of a putative dual-domain hypoxanthine-guanine phosphoribosyltransferase (HGPRT)/adenylate kinase (AMPK). ZgHGPRT/AMPK single domain, dual domain 3D structure homology modeling, HGPRT from Leptospira interrogans (PDB ID 4QRI) and AMPK structure from Geobacillus stearothermophilus (PDB ID 1ZIN) are used as templates. ZgHGPRT/AMPK model is complexed with Hyp, PRPP and Mg2+ in the active site of the HGPRT domain, and with AMP, ATP and Mg2+ in the active site of AMPK domain. Essential elements of type I PRTs architecture are found in ZgHGPRT/AMPK amino acid sequence such as diphosphate loop, the flexible loop and PRPP binding domain (including PRPP loop), as well as in the homology model
additional information
isozyme HPGRT-1 structure determination and analysis, active site structure, detailed overview
additional information
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isozyme HPGRT-1 structure determination and analysis, active site structure, detailed overview
additional information
out of the five active site loops (I, II, III, III', and IV) in PfHGXPRT, loop III' facilitates the closure of the hood over the core domain which is the penultimate step during enzymatic catalysis. Residue Trp181 is important. Molceluar dynamics and simulation, structure-activity analysis, overview
additional information
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out of the five active site loops (I, II, III, III', and IV) in PfHGXPRT, loop III' facilitates the closure of the hood over the core domain which is the penultimate step during enzymatic catalysis. Residue Trp181 is important. Molceluar dynamics and simulation, structure-activity analysis, overview
additional information
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identification of a putative dual-domain hypoxanthine-guanine phosphoribosyltransferase (HGPRT)/adenylate kinase (AMPK). ZgHGPRT/AMPK single domain, dual domain 3D structure homology modeling, HGPRT from Leptospira interrogans (PDB ID 4QRI) and AMPK structure from Geobacillus stearothermophilus (PDB ID 1ZIN) are used as templates. ZgHGPRT/AMPK model is complexed with Hyp, PRPP and Mg2+ in the active site of the HGPRT domain, and with AMP, ATP and Mg2+ in the active site of AMPK domain. Essential elements of type I PRTs architecture are found in ZgHGPRT/AMPK amino acid sequence such as diphosphate loop, the flexible loop and PRPP binding domain (including PRPP loop), as well as in the homology model
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additional information
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identification of a putative dual-domain hypoxanthine-guanine phosphoribosyltransferase (HGPRT)/adenylate kinase (AMPK). ZgHGPRT/AMPK single domain, dual domain 3D structure homology modeling, HGPRT from Leptospira interrogans (PDB ID 4QRI) and AMPK structure from Geobacillus stearothermophilus (PDB ID 1ZIN) are used as templates. ZgHGPRT/AMPK model is complexed with Hyp, PRPP and Mg2+ in the active site of the HGPRT domain, and with AMP, ATP and Mg2+ in the active site of AMPK domain. Essential elements of type I PRTs architecture are found in ZgHGPRT/AMPK amino acid sequence such as diphosphate loop, the flexible loop and PRPP binding domain (including PRPP loop), as well as in the homology model
-
additional information
-
crystals of enzyme-diphosphate-GMP complex are used for structure determination, detailed overview
-
additional information
-
crystals of enzyme-diphosphate-GMP complex are used for structure determination, detailed overview
-
additional information
-
identification of a putative dual-domain hypoxanthine-guanine phosphoribosyltransferase (HGPRT)/adenylate kinase (AMPK). ZgHGPRT/AMPK single domain, dual domain 3D structure homology modeling, HGPRT from Leptospira interrogans (PDB ID 4QRI) and AMPK structure from Geobacillus stearothermophilus (PDB ID 1ZIN) are used as templates. ZgHGPRT/AMPK model is complexed with Hyp, PRPP and Mg2+ in the active site of the HGPRT domain, and with AMP, ATP and Mg2+ in the active site of AMPK domain. Essential elements of type I PRTs architecture are found in ZgHGPRT/AMPK amino acid sequence such as diphosphate loop, the flexible loop and PRPP binding domain (including PRPP loop), as well as in the homology model
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additional information
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identification of a putative dual-domain hypoxanthine-guanine phosphoribosyltransferase (HGPRT)/adenylate kinase (AMPK). ZgHGPRT/AMPK single domain, dual domain 3D structure homology modeling, HGPRT from Leptospira interrogans (PDB ID 4QRI) and AMPK structure from Geobacillus stearothermophilus (PDB ID 1ZIN) are used as templates. ZgHGPRT/AMPK model is complexed with Hyp, PRPP and Mg2+ in the active site of the HGPRT domain, and with AMP, ATP and Mg2+ in the active site of AMPK domain. Essential elements of type I PRTs architecture are found in ZgHGPRT/AMPK amino acid sequence such as diphosphate loop, the flexible loop and PRPP binding domain (including PRPP loop), as well as in the homology model
-
additional information
-
identification of a putative dual-domain hypoxanthine-guanine phosphoribosyltransferase (HGPRT)/adenylate kinase (AMPK). ZgHGPRT/AMPK single domain, dual domain 3D structure homology modeling, HGPRT from Leptospira interrogans (PDB ID 4QRI) and AMPK structure from Geobacillus stearothermophilus (PDB ID 1ZIN) are used as templates. ZgHGPRT/AMPK model is complexed with Hyp, PRPP and Mg2+ in the active site of the HGPRT domain, and with AMP, ATP and Mg2+ in the active site of AMPK domain. Essential elements of type I PRTs architecture are found in ZgHGPRT/AMPK amino acid sequence such as diphosphate loop, the flexible loop and PRPP binding domain (including PRPP loop), as well as in the homology model
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homohexamer
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dynamic light scattering (pH 7.5, 25 °C) and gel filtration chromatography (HR 10/30 Superdex 200, FPLC, pH 7.5)
homotetramer
4 * 26000, calculated from amino acid sequence
monomer
-
1 * 51000, SDS-PAGE
octamer
-
8 * 18000, SDS-PAGE
?
-
x * 26000, SDS-PAGE
?
-
x * 24352-24353, recombinant mutant enzymes, mass spectroscopy and DNA sequence determination
?
-
x * 41000-45000, sedimentation equilibrium in presence of guanidine-HCl
?
-
x * 25000-27000, SDS-PAGE
?
-
x * 25000-27000, SDS-PAGE
dimer
-
2 * 29000, SDS-PAGE
dimer
-
2 * 29000, SDS-PAGE
-
dimer
-
2 * 34000-34700, SDS-PAGE
dimer
residues 198-204 are involved in the largest dimer interface
dimer
2 * 23000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 26229-26232, in presence of KCl, SDS-PAGE, mass spectroscopy and DNA sequence determination
dimer
2 * 20600, SDS-PAGE
dimer
-
2 * 20600, SDS-PAGE
-
dimer
-
2 * 29500, SDS-PAGE
dimer
-
2 * 64000, SDS-PAGE
dimer
when the C-terminal region, which is predicted as a disordered stretch, is excised by proteolysis, TcHPRT adopts a dimeric state, suggesting that the C-terminal region acts as a main guide for the quaternary arrangement. The C-terminal region exhibits a modulatory role on the enzyme, as attested by the enhanced activity observed for the dimeric form
homodimer
2 * 22251, calculated from amino acid sequence
homodimer
2 * 41650, sedimentation velocity and SDS-PAGE, 2 * 43770, sequence caluclation
homodimer
-
2 * 41650, sedimentation velocity and SDS-PAGE, 2 * 43770, sequence caluclation
-
homodimer
-
2 * 41650, sedimentation velocity and SDS-PAGE, 2 * 43770, sequence caluclation
-
homodimer
-
2 * 41650, sedimentation velocity and SDS-PAGE, 2 * 43770, sequence caluclation
-
homodimer
-
2 * 41650, sedimentation velocity and SDS-PAGE, 2 * 43770, sequence caluclation
-
homodimer
-
2 * 41650, sedimentation velocity and SDS-PAGE, 2 * 43770, sequence caluclation
-
monomer or dimer
the recombinant chimeric enzyme exists as a mixture of monomeric and dimeric protein in solution, but shifts to a tetramer on addition of phosphoribosyl diphosphate
monomer or dimer
the recombinant chimeric enzyme exists as a mixture of monomeric and dimeric protein in solution, but shifts to a tetramer on addition of phosphoribosyl diphosphate
tetramer
-
4 * 19000, SDS-PAGE
tetramer
4 * 22800, SDS-PAGE
tetramer
-
active enzyme form, subunit A composition, overview
tetramer
-
4 * 26000, SDS-PAGE
tetramer
-
4 * 24000, SDS-PAGE
tetramer
the recombinant chimeric enzyme exists as a mixture of monomeric and dimeric protein in solution, but shifts to a tetramer on addition of phosphoribosyl diphosphate
tetramer
-
4 * 26229-26232, in absence of KCl, SDS-PAGE, mass spectroscopy and DNA sequence determination
tetramer
the recombinant chimeric enzyme exists as a mixture of monomeric and dimeric protein in solution, but shifts to a tetramer on addition of phosphoribosyl diphosphate
tetramer
4 * 28000, recombinant His-tagged enzyme, SDS-PAGE
tetramer
the tetrameric oligomerization state is required for enzyme activity, since residues that make up the active site are also involved in interactions in the dimeric interface, guiding the invariable residue Arg206 toward the active site
tetramer
the full-length enzyme form in solution adopts a stable and enzymatically active tetrameric form, exhibiting large intersubunit surfaces, two putative dimeric interfaces
trimer
-
3 * 25000, SDS-PAGE
trimer
-
3 * 26000, SDS-PAGE
trimer
-
3 * 27000, SDS-PAGE
additional information
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stereoview of the three-dimensional structure of subunit, subunit interaction
additional information
Pro93 and Tyr197 form part of crucial interactions holding together the AB interface in the unliganded or GMP-bound forms of HGPRT, while Pro93 and His26 interact at the interface after binding of phosphoribosyl diphosphate
additional information
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Pro93 and Tyr197 form part of crucial interactions holding together the AB interface in the unliganded or GMP-bound forms of HGPRT, while Pro93 and His26 interact at the interface after binding of phosphoribosyl diphosphate
additional information
dimer-tetramer equilibrium, the major peak is in a dimeric state. DTT is absent from the buffers containing MtHGPRT as there is only one cysteine residue per subunit and this enzyme does not undergo oxidation in the absence of reducing agents. MtHGPRT elutes as three different oligomeric species. MtHGPRT in the Tris-chloride-Mg2+ comprises a mixture of oligomeric states coexisting in a self-association equilibrium. Both tetrameric and dimeric forms of the enzyme are active after column chromatography. The specific activity of the tetramer appears higher than that of the dimer. Crystals of enzyme-diphosphate-GMP complex are used for structure determination, detailed overview
additional information
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dimer-tetramer equilibrium, the major peak is in a dimeric state. DTT is absent from the buffers containing MtHGPRT as there is only one cysteine residue per subunit and this enzyme does not undergo oxidation in the absence of reducing agents. MtHGPRT elutes as three different oligomeric species. MtHGPRT in the Tris-chloride-Mg2+ comprises a mixture of oligomeric states coexisting in a self-association equilibrium. Both tetrameric and dimeric forms of the enzyme are active after column chromatography. The specific activity of the tetramer appears higher than that of the dimer. Crystals of enzyme-diphosphate-GMP complex are used for structure determination, detailed overview
additional information
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dimer-tetramer equilibrium, the major peak is in a dimeric state. DTT is absent from the buffers containing MtHGPRT as there is only one cysteine residue per subunit and this enzyme does not undergo oxidation in the absence of reducing agents. MtHGPRT elutes as three different oligomeric species. MtHGPRT in the Tris-chloride-Mg2+ comprises a mixture of oligomeric states coexisting in a self-association equilibrium. Both tetrameric and dimeric forms of the enzyme are active after column chromatography. The specific activity of the tetramer appears higher than that of the dimer. Crystals of enzyme-diphosphate-GMP complex are used for structure determination, detailed overview
-
additional information
-
dimer-tetramer equilibrium, the major peak is in a dimeric state. DTT is absent from the buffers containing MtHGPRT as there is only one cysteine residue per subunit and this enzyme does not undergo oxidation in the absence of reducing agents. MtHGPRT elutes as three different oligomeric species. MtHGPRT in the Tris-chloride-Mg2+ comprises a mixture of oligomeric states coexisting in a self-association equilibrium. Both tetrameric and dimeric forms of the enzyme are active after column chromatography. The specific activity of the tetramer appears higher than that of the dimer. Crystals of enzyme-diphosphate-GMP complex are used for structure determination, detailed overview
-
additional information
Pro93 and Tyr197 form part of crucial interactions holding together the AB interface in the unliganded or GMP-bound forms of HGPRT, while Pro93 and His26 interact at the interface after binding of phosphoribosyl diphosphate
additional information
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Pro93 and Tyr197 form part of crucial interactions holding together the AB interface in the unliganded or GMP-bound forms of HGPRT, while Pro93 and His26 interact at the interface after binding of phosphoribosyl diphosphate
additional information
structure comparison with the human enzyme
additional information
structure-function analysis, molecular dynamics, dynamic cross-correlation maps, and configurational entropy, overview
additional information
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structure-function analysis, molecular dynamics, dynamic cross-correlation maps, and configurational entropy, overview
additional information
the enzyme occurs as a mixture of monomer and dimer, and undergoes tetramerisation on the addition of phosphoribosyl diphosphate
additional information
transition state structure of PfHGXPRT, overview
additional information
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structure determination and analysis
additional information
structure determination and analysis
additional information
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structure determination and analysis
additional information
structure determination and analysis
additional information
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structure determination and analysis
additional information
analysis of the quaternary structure of enzyme TbrHGPRT in solution, overview
additional information
quaternary structure analysis
additional information
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quaternary structure analysis
additional information
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quaternary structure analysis
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additional information
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quaternary structure analysis
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additional information
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quaternary structure analysis
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additional information
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quaternary structure analysis
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additional information
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quaternary structure analysis
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free enzyme or enzyme complexed with IMP, hanging drop vapour diffusion method, 20°C, 10 mg/ml protein in 20 Tris-HCl, pH 7.4, mixed with a molar excess of IMP, 0.001 ml protein solution mixed with equal volume of reservoir solution containing 0.2 M magnesium acetate tetrahydrate, 0.1 M sodium cacodylate, pH 6.5, 12% w/v PEG 4000, or protein solution with 1 mM IMP mixed with reservoir solution containing 15% PEG 8000, 0.1 M sodium cacodylate, pH 6.5, 0.2 M magnesium acetate tetrahydrate, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution
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purified recombinant mutant L160I enzyme, hanging drop vapour diffusion method, 0.001 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 7.4, excess GMP in a molar ratio 4:1, is mixed with equal volume of crystallization solution containing 0.2 M CaCl2 dihydrate, 0.1 M HEPES, pH 7.5, 28% PEG 400, 20°C, 2 weeks, X-ray diffraction structure determination and analysis at 1.7 A resolution, purified recombinant wild-type enzyme, hanging drop vapour diffusion method, 0.001 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 7.4, excess IMP in a molar ratio 4:1, is mixed with equal volume of crystallization solution containing 0.2 M magnesium acetate tetrahydrate, 0.1 M sodium cacodylate, pH 6.5, 12% PEG 4000, 20°C, within 1 week, X-ray diffraction structure determination and analysis at 2.2 A resolution
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enzyme in complex with inhibitors (2-[(2,3-dihydroxypropyl)[2-(6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl]amino]ethyl)phosphonic acid, 9-[(N-phosphonoethyl-N-phosphonomethyl)-2-aminoethyl]-hypoxanthine, 9-[(N-phosphonoethyl-N-phosphonoethoxyethyl)-2-aminoethyl]-hypoxanthine, (2-[[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl][2-(2-phosphonoethoxy)ethyl]amino]ethyl)phosphonic acid, [[2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]propane-1,3-diyl]bis(oxymethylene)]bis(phosphonic acid), and [[[(4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]azanediyl]di(propane-3,1-diyl)]bis(phosphonic acid), X-ray diffraction structure determination and analysis at 2.55-2.9 A resolution
enzyme in complex with 2-(phosphonoethoxy)ethyl guanine, 2-(phosphonoethoxy)ethyl hypoxanthine, and (R,S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine, hanging drop vapor diffusion method, mixing of equal volumes of well solution, containing 0.1 M citrate pH 5.5, 10% isopropyl alcohol and 29% PEG 4000, and protein inhibitor complex with 17 mg/ml prtoein, and 3.3 mM for 2-(phosphonoethoxy)ethyl guanine, 3.9 mM (R,S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine, and 3.0 mM for 2-(phosphonoethoxy)ethyl hypoxanthine, X-ray diffraction structure determination and analysis at 2.6-2.78 A resolution
in complex with T-705-RMP, hanging drop vapor diffusion method, using 0.2 M NaCl, 1 M sodium/potassium tartrate, 0.1 M imidazole, pH 8.0
purified enzyme in complex with inhibitor [3-(guanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methylphosphonic acid and ([3-(guanine-9-yl)-2-((2-phosphonoethoxy)-methyl)propoxy]methyl)phosphonic acid, hanging drop method, mixing of 0.001 ml of 11.1 mg/ml protein in 0.1 M Tris-HCl, 0.01 M MgCl2, 1 mM DTT, and 0.3 mM 5-phospho-alpha-D-ribose 1-diphosphate, pH 7.4, and 4.8 mM inhibitor, with 0.001 ml of reservoir solution containing 20% PEG 3350, 0.2 M sodium bromide, 0.1 M Bis-Tris propane, pH 7.5, at 18°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement and modeling
purified recombinant mutant C22A/C105A/C205A enzyme 1. free or 2. in complex with inactive purine base analogue 7-hydroxy [4,3d] pyrazolo pyrimidine and 5-phospho-alpha-D-ribose 1-diphosphate, or 3. complexed with IMP or GMP, or 4. complexed with transition state analogue immuncillinHP-Mg2+-diphosphate, hanging drop vapour diffusion method, 18 mg/ml protein in 0.05 M Tris-HCl, pH 7.4, 1 mM MgCl2, 1 mM DTT, mixing of 0.002 ml of both protein and reservoir solution, the latter containing 0.2 M ammonium acetate, 0.1 m sodium acetate, pH 4.6, 30% w/v PEG 4000, 17°C, 2-7 days, cryoprotection by 30% glycerol in reservoir solution, X-ray diffraction structure determination and analysis at 1.9 A resolution
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recombinant chimeric mutant enzyme complex with the product GMP, 12 mg/ml protein and 5 mM GMP in 0.1 M Tris, pH 8.0, and 2.0 M ammonium sulfate, 2-5 days, X-ray diffraction structure determination and analysis at 2.8 A resolution, modeling
spectral analysis of the crystal structure of the HGPRT/immucillin-G 5'-phosphate/diphosphate complex
ultraviolet resonance Raman spectroscopy study on the complexes of enzyme with products IMP, GMP, and XMP, both in Homo sapiens and Plasmodium falciparum, in resonance with the purine nucleobase electronic absorption. Human hypoxanthine guanine phosphoribosyltransferase catalyzes the phosphoribosylation of guanine and hypoxanthine, while the Plasmodium falciparum enzyme acts on xanthine as well. Spectra of bound nucleotides show that the enzyme distorts the structure of the nucleotides. The distorted structure resembles that of the deprotonated nucleotide. The two proteins assemble similar active sites for their common substrates. While the human enzyme does not bind XMP, Plasmodium falciparum hypoxanthine guanine phosphoribosyltransferase perturbs the pKa of bound XMP
apo-form and in complex with GMP, sitting drop vapor diffusion method, using 0.2 M trimethylamine N-oxide dehydrate, 0.1 M Tris pH 8.5, 20% (w/v) polyethylene glycol monomethyl ether 2000
recombinant enzyme, 7 mg/ml, hanging-drop vapour-diffusion method, TMD buffer, pH 7.5, + equal volume of reservoir solution: 18°C or 4°C, pH 5.6 , 19% isopropanol, 19% polyethylene glycol 4000, 5% glycerol, or 17% polyethylene glycol 4000, 5% glycerol
purified recombinant enzyme PvHGPRT in complex with inhibitor [3R,4R]-4-guanin-9-yl-3-((S)-2-hydroxy-2-phosphonoethyl)oxy-1-N-(phosphonopropionyl)pyrrolidine, 21 mg/ml protein is incubated with 6.4 mM inhibitor on ice for 5 min, hanging drop method, mixing of 0.001 ml of protein and inhibitor with 0.001 ml of reservoir solution containing 0.3 M potassium thiocyanate, 0.1 M Bis-tris propane, pH 8.5, 18°C, X-ray diffraction structure determination and analysis at 2.85 A resolution, molecular replacement using the protein coordinates of subunit A of human HGPRT in complex with [(2-[(guanin-9H-yl)methyl]-propane-1,3-diyl)bis(oxy)]bis-(methylene)diphosphonic acid as template (PDB ID 4IJQ), model building
recombinant chimeric mutant enzyme complex with the product GMP, 12 mg/ml protein and 5 mM GMP in 0.1 M Tris, pH 8.0, and 2.0 M ammonium sulfate, 2-5 days, X-ray diffraction structure determination and analysis at 2.8 A resolution, modeling
ultraviolet resonance Raman spectroscopy study on the complexes of enzyme with products IMP, GMP, and XMP, both in Homo sapiens and Plasmodium falciparum, in resonance with the purine nucleobase electronic absorption. Human hypoxanthine guanine phosphoribosyltransferase catalyzes the phosphoribosylation of guanine and hypoxanthine, while the Plasmodium falciparum enzyme acts on xanthine as well. Spectra of bound nucleotides show that the enzyme distorts the structure of the nucleotides. The distorted structure resembles that of the deprotonated nucleotide. The two proteins assemble similar active sites for their common substrates. While the human enzyme does not bind XMP, Plasmodium falciparum hypoxanthine guanine phosphoribosyltransferase perturbs the pKa of bound XMP
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purified isozyme HPGRT-1 in complex with IMP, 2,5 mg/ml enzyme and 2 mM of IMP are mixed with 12.5% PEG 1000, 12.5% PEG 3350, 12.5% MPD, 0.03 M divalent cations, and 0.1 M MES/imidazole, pH 6.5, at 18°C, X-ray diffraction structure determination and analysis at 2.8 A resolution, screening and method optimmization, HPGRT-1 crystallizes in an orthorhombic system, and the systematic absences indicates space group P212121 with four polypeptide chains in the asymmetric unit, respectively
structure in the unliganded form, in complex with IMP and in complex with GMP, to 2.1, 1.9 and 2.2 A resolution, respectively. The overall fold of the IMP complex is similar to that of the unliganded form, but the main-chain and side-chain atoms of the active site move to accommodate IMP. The overall folds of the IMP and GMP complexes are almost identical to each other. Enzyme belongs to group I
crystallization in complex with GMP and IMP, structure analysis
mutant enzyme D150A, crystallization complexed with xanthosine 5'-monophosphate, diphosphate and 2 Mg2+, post transition state structure analysis, active site structure
the recombinant enzyme is complexed with Mg2+, 5-phosphoribosyl 1-diphosphate and inactive substrate analogue 9-deazaguanine, hanging drop method, enzyme complex, 20 mg/ml, is precipitated by 0.1 M Tris-HCl, pH 8.0, 30% polyethylene glycol 4000, 0.2 M Li2SO4, 0.5% beta-octylglucoside at 4°C, X-ray diffraction structure analysis
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analysis of crystal structure
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crystallization and X-ray structure determination and analysis, 1 molecule of GMP bound per dimer
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purified recombinant TbrHGPRT in complex with GMP, IMP, and inhibitors [6-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)hexyl]phosphonic acid, [4-(6-oxo-1,6-dihydro-9H-purin-9-yl)butyl]phosphonic acid, and [5-(6-oxo-1,6-dihydro-9H-purin-9-yl)pentyl]phosphonic acid, hanging drop vapor diffusion method, mixing of 0.001 ml of protein ligand complex solution and 0.001 ml of well solution. The protein-ligand complexes are prepared using 36 mg/ml, 28 mg/ml, 60 mg/ml, and 28 mg/ml of enzyme in the presence of 3.2 mM GMP, 3.2 mM IMP, 4.6 mM [5-(6-oxo-1,6-dihydro-9H-purin-9-yl)pentyl]phosphonic acid, 4.6 mM [4-(6-oxo-1,6-dihydro-9H-purin-9-yl)butyl]phosphonic acid and 1.8 mM [6-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)hexyl]phosphonic acid, respectively, followed by incubation on ice for 10 min, the reservoir solution for the complexes with GMP, IMP, [4-(6-oxo-1,6-dihydro-9H-purin-9-yl)butyl]phosphonic acid, and [6-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)hexyl]phosphonic acid contains 25% PEG 3350, 0.2 M lithium sulfate, and 0.1 M Bis-Tris, pH 5.0-5.5. For [5-(6-oxo-1,6-dihydro-9H-purin-9-yl)pentyl]phosphonic acid the well solution is 25% PEG 3350, 0.2 M sodium iodide, 0.1 M Bis-Tris propane, pH 6.5, X-ray diffraction structure determination and analysis at 2.73, 2.51, 1.52, 2.89 and 2.81 A resolution, respectively. The structure of the complex with [6-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)hexyl]phosphonic acid is solved by molecular replacement using the structure of TcrHGPRT (PDB ID 1TC2) as the starting model. The starting models for the complexes with GMP, IMP, [4-(6-oxo-1,6-dihydro-9H-purin-9-yl)butyl]phosphonic acid, and [5-(6-oxo-1,6-dihydro-9H-purin-9-yl)pentyl]phosphonic acid are based upon the refined model of the complex with [6-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)hexyl]phosphonic acid, refinement and model building
purified recombinant His6-tagged enzyme, mixing of 5 mg/ml protein in 20 mM Tris-HCl, 100 mM NaCl, pH 8.0, with reservoir solution containing 0.1 M MES, pH 6.5, and 12% w/v PEG 20000 at 20°C, X-ray diffraction structure determination and analysis at 2.65 A resolution
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L160I
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site-directed mutagenesis, crystal structure determination
A72G
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site-directed mutagenesis, exchange in diphosphate binding site, decreased Km-value for diphosphate and guanine, increased Km-value for 5-phosphoribosyl 1-diphosphate, reduced activity
G71A
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site-directed mutagenesis, no activity
G71E
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site-directed mutagenesis, no activity
G71R
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site-directed mutagenesis, no activity
T70K
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site-directed mutagenesis, exchange in diphosphate binding site, 6.7fold lower Km-value for diphosphate, lower Km for guanine, 2fold increase in Km-value for 5-phosphoribosyl 1-diphosphate, reduced activity
T70K/A72G
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site-directed mutagenesis, exchange in diphosphate binding site, decreased Km-value for diphosphate and guanine, increased Km-value for 5-phosphoribosyl 1-diphosphate, reduced activity
A192V
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naturally occuring mutation of HPRT1 gene, causes HPRT-related hyperuricemia
A64P
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
C105A
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prepared via splicing by overlap extension, reduced oxidation ofthe enzyme during storage
C205A
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prepared via splicing by overlap extension, reduced oxidation ofthe enzyme during storage
C22A
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prepared via splicing by overlap extension, reduced oxidation ofthe enzyme during storage
C23F
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naturally occuring mutation of HPRT1 gene, causes HPRT-related hyperuricemia
D185G
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naturally occuring mutation of HPRT1 gene, causes HPRT-related hyperuricemia
D31E
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identification of another genetic variation within the gout-affected population in Taiwan with mutation on exon 2 with T to G transition at cDNA base 93 resulting in a change from aspartic acid to glutamic acid at position 31
D44V
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
E196A
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
E196D
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
E196Q
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
E196R
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site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
E196V
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a naturally occuring mutation that leads to the Lesch-Nyhan syndrome
F199C
a naturally occuring mutation T596G, leads to 8% residual HPRT activity and causes juvenile-onset, severe gouty arthritis, nephrolithiasis, and mild neurologic symptoms. Adenine phosphoribosyltransferase, APRT, EC 2.4.2.7, in erythrocytes from subjects with HPRT deficiency is typically increased about 23fold compared with controls. Modeling of the mutated protein for prediction of the mechanisms of partial enzymatic activity
F36A
site-directed mutagenesis, unaltered substrate specificity compared to the wild-type enzyme
F36E
site-directed mutagenesis, unaltered substrate specificity compared to the wild-type enzyme
F36G
site-directed mutagenesis, inactive mutant
F36K
site-directed mutagenesis, unaltered substrate specificity compared to the wild-type enzyme
F36W
site-directed mutagenesis, unaltered substrate specificity compared to the wild-type enzyme
G140D
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
G70R
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
H204X
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
H60R
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naturally occuring mutation of HPRT1 gene, causes no altered phenotype compared to the wild-type enzyme
I137T
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DNA sequence determination and identification of the naturally occurring point mutation in the conserved 5-phosphoribosyl-1-diphosphate binding motif, causing a variant of Lesch-Nyhan syndrome, the mutation affects the affinity of the enzyme for 5-phosphoribosyl-1-diphosphate through structural alterations
I9S
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
K159E
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naturally occuring mutation of HPRT1 gene, causes HPRT-related hyperuricemia
K68A
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conformational changes, shifted catalytic loop closer to the active site
L147F
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natural occuring point mutation leading to enzyme deficiency, which is not correlated with a physiological syndrome
L147P
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naturally occuring mutation of HPRT1 gene, causes HPRT-related hyperuricemia
L65P
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
L68P
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naturally occuring mutation in an Argentine individual, the patient shows the LND phenotype, determination of the altered urine purine alkaloid metabolite contents
L68R
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naturally occuring mutation in an Argentine individual, the patient shows the LND phenotype, determination of the altered urine purine alkaloid metabolite contents
L78Q
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
M54L
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
P24R
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
P25T
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naturally occuring mutation of HPRT1 gene, causes HPRT-related hyperuricemia
Q144X
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naturally occuring nonsense mutation of HPRT1 gene, exchange of 430C-T, causes the Lesch-Nyhan syndrome
R48H
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naturally occuring mutation in an Argentine individual, the patient shows the HRND phenotype, determination of the altered urine purine alkaloid metabolite contents
R51X
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
S162R
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
T124P
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naturally occuring mutation of HPRT1 gene, causes HPRT-related hyperuricemia
T139P
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
V158G
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naturally occuring mutation of HPRT1 gene, causes HPRT-related hyperuricemia
V188A
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naturally occuring mutation of HPRT1 gene, causes HPRT-related hyperuricemia
Y195S
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naturally occuring mutation in an Argentine individual, the patient shows the HRND phenotype, determination of the altered urine purine alkaloid metabolite contents
Y72C
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naturally occuring mutation of HPRT1 gene, causes HPRT-related hyperuricemia
S103R
the mutation is associated with Gout arthritis and shows strongly reduced activity compared to the wild type enzyme
S95A
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site-directed mutagenesis, dramatic reduction of catalytic activity, weak complementation of bacterial enzyme deficient strain
S95C
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site-directed mutagenesis, 2-3fold reduction of kcat, weak complementation of bacterial enzyme deficient strain
S95E
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site-directed mutagenesis, dramatic reduction of catalytic activity, no complementation of bacterial enzyme deficient strain
S95T
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site-directed mutagenesis, 2-3fold reduction of kcat, complementation of bacterial enzyme deficient strain
Y96F
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site-directed mutagenesis, dramatic reduction of catalytic activity, no complementation of bacterial enzyme deficient strain, 4-5fold decrease of Km value for 5-phosphoribosyl 1-diphosphate
Y96V
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site-directed mutagenesis, dramatic reduction of catalytic activity, no complementation of bacterial enzyme deficient strain, 4-5fold decrease of Km value for 5-phosphoribosyl 1-diphosphate
F197W
the mutant shows reduced activity compared tot he wild type enzyme
W181F
site-directed mutagenesis of residue Trp181 in loop III', the mutant shows an over 5fold decreased xanthine phosphoribosylation activity compared to wild-type and an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate (PRPP)
W181S
site-directed mutagenesis of residue Trp181 in loop III', the mutant shows an over 5fold decreased xanthine phosphoribosylation activity compared to wild-type and an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate (PRPP)
W181S/F197W
the mutant shows reduced activity compared tot he wild type enzyme
W181T
site-directed mutagenesis of residue Trp181 in loop III', the mutant shows an over 10fold decreased xanthine phosphoribosylation activity compared to wild-type and an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate (PRPP)
W181Y
site-directed mutagenesis of residue Trp181 in loop III', the mutant shows an over 5fold decreased xanthine phosphoribosylation activity compared to wild-type and an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate (PRPP)
D150A
reduced activity compared to wild-type, kcat for hypoxanthine, guanine, and xanthine are reduced by 11fold, 296fold, and 8.6fold, respectively, Km value for alpha-D-5-phosphoribosyl 1-diphosphate is reduced by 6.5fold
D163E
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site directed mutagenesis, slightly changed substrate affinities compared to wild-type
D163N
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site-directed mutagensis, exchange of xanthine binding residue, loss of the binding ability and activity against xanthine and XMP
F162L
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site directed mutagenesis, no effect on purine base specificity
I104G
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site directed mutagenesis, increased Km values for hypoxanthine, guanine, and xanthine
K134Q
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site directed mutagenesis, mutant recognizes adenine as substrate in addition, but less efficient than mutant K134S
K134S
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site directed mutagenesis, mutant recognizes adenine as substrate in addition, increased Km values for hypoxanthine, guanine, and xanthine
R155E
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site directed mutagenesis, reduced affinity to GMP and XMP, catalysation of the forward reaction with guanine and xanthine at accelerated rates, 15fold increased Km for xanthine
R155K
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site directed mutagenesis, reduced affinity to GMP and XMP, catalysation of the forward reaction with guanine and xanthine at accelerated rates, insensitive to phenylglyoxal
T47K
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site-directed mutagenesis, exchange of diphosphate binding site residue, 4-10fold decreased Km for diphosphate compared to the wild-type
Y156F
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site directed mutagenesis, weakened binding of GMP and XMP
Y156W
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site directed mutagenesis, slightly changed substrate affinities compared to wild-type
G69S
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reduced activity compared to the wild-type enzyme
L67M
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highly reduced activity with hypoxanthine compared to the wild-type enzyme, mutant is not active with guanine
C22A/C105A/C205A
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site-directed mutagenesis, kinetic and physical properties are similar to the wild-type enzyme, but the mutant enzyme is more resistant to oxidation
C22A/C105A/C205A
site-directed mutagenesis, the exchanges stabilize the enzyme protein, but kinetic and structural properties of the mutant enzyme are identical to wild-type human HGPRT
F36L
random mutagenesis, mutant phosphoribosylates xanthine, mutant does not bind the purine substrate directly, long-range modulation via loop IV influence the substrate specificity, altered enzyme stability
F36L
wild-type human enzyme does not accept xanthine as substrate, mutant F36L does catalyze the conversion of xanthine to XMP with a kcat much lower than those of hypoxanthine and guanine and fails to perturb the pKa of XMP
G70E
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naturally occuring mutation in an Argentine individual, the patient shows the HRND phenotype, determination of the altered urine purine alkaloid metabolite contents
G70E
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naturally occuring mutation of HPRT1 gene, causes the Lesch-Nyhan syndrome
Y195C
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naturally occuring mutation in an Argentine individual, the patient shows the HRND phenotype, determination of the altered urine purine alkaloid metabolite contents
Y195C
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naturally occuring mutation of HPRT1 gene, causes HPRT-related hyperuricemia
L44F
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site-directed mutagenesis, mutant does not phosphoribosylate guanine and xanthine, modulation via loop IV influence the substrate specificity, altered enzyme stability
L44F
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site-directed mutagenesis, temperature-sensitive mutant, no complementation of an enzyme-deficient Escherichia coli strain at 42°C, only at 20°C and 37°C
additional information
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random enzyme mutations induced by neutron irradiation of CHO cells, analysis of the molecular structure of the HPRT mutations and the types of point mutations using direct sequencing of PCR fragments , overview
additional information
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additional information
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construction of 4 chimeric enzymes with segments of human and Plasmodium falciparum enzymes, altered substrate specificities
additional information
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determination of the frequency of HPRT deficiency within the gout-affected population in Taiwan, overview
additional information
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induction of HPRT mutations in G0 peripheral blood lymphocytes exposed in vitro to gamma rays at low, 0.0014 Gy/min, and high, 0.85 Gy/min, dose rates, the mutation increases at both high and low radiation rates, dose-rate effect on the induced HPRT mutant frequency correlating inversely with the cell curvival, overview
additional information
construction of a chimera of Plasmodium falciparum and human HGPRTs, which consists of the core of the protein from the human enzyme and the hood region from the parasite enzyme. Replacement of Tyr197 of human HGPRT by Ile207 in the chimera disrupts the interaction at the AB interface in the absence of PRPP. In the presence of PRPP, the interaction between Pro93 and His26 can restore the AB interface, shifting the chimeric enzyme to a tetrameric state, active site structure, overview
additional information
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construction of a chimera of Plasmodium falciparum and human HGPRTs, which consists of the core of the protein from the human enzyme and the hood region from the parasite enzyme. Replacement of Tyr197 of human HGPRT by Ile207 in the chimera disrupts the interaction at the AB interface in the absence of PRPP. In the presence of PRPP, the interaction between Pro93 and His26 can restore the AB interface, shifting the chimeric enzyme to a tetrameric state, active site structure, overview
additional information
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genotyping for mutations in the HPRT gene in healthy individuals and Lesch-Nyhan syndrome patients in Japanese population, diverse deletion mutations, detailed overview
additional information
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myosmine exhibits small, but significant, mutagenic potential and causes HPRT mutagenesis in nonsmoker lymphocytes, mutation frequency, overview
additional information
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shRNA knockdown of HPRT gene expression leading toloss of 94% activity, HPRT-deficient NT2 cells demonstrate aberrant expression of several transcription factors and dopaminergic markers
additional information
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wild-type enzyme complements enzyme deficiency of the bacterial enzyme in Escherichia coli
additional information
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construction of mutant lacking the Ser-Lys-Val C-terminal targeting signal, mutant enzyme is located throughout the parasite, including subcellular organelles such as nucleus and flagellum
additional information
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generation of HPRT gene knock-out mice, the mutant mice show 55% increased expression of the serotonin receptor 2C, HTR2C, semiquantitative realtime RT-PCR expression analysis
additional information
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construction of 4 chimeric enzymes with segments of human and Plasmodium falciparum enzymes, altered substrate specificities
additional information
construction of a chimera of Plasmodium falciparum and human HGPRTs, which consists of the core of the protein from the human enzyme and the hood region from the parasite enzyme. Replacement of Tyr197 of human HGPRT by Ile207 in the chimera disrupts the interaction at the AB interface in the absence of PRPP. In the presence of PRPP, the interaction between Pro93 and His26 can restore the AB interface, shifting the chimeric enzyme to a tetrameric state, active site structure, overview
additional information
-
construction of a chimera of Plasmodium falciparum and human HGPRTs, which consists of the core of the protein from the human enzyme and the hood region from the parasite enzyme. Replacement of Tyr197 of human HGPRT by Ile207 in the chimera disrupts the interaction at the AB interface in the absence of PRPP. In the presence of PRPP, the interaction between Pro93 and His26 can restore the AB interface, shifting the chimeric enzyme to a tetrameric state, active site structure, overview
additional information
molecular dynamics simulations of wild-type and in silico W181S, W181T, W181Y, and W181F PfHGXPRT mutants bound to IMP/PPi/Mg2+, overview. Escherichia coli strain Sphi609, (ara, DELTApro-gpt-lac, thi, hpt, pup, purH, J, strA) is a knockout strain for the genes encoding hypoxanthine phosphoribosyltransferase (HPRT) and xanthine-guanine phosphoribosyltransferase (XGPRT). Although activation of the enzyme mutants by IMP increases their catalytic efficiency by about 100fold, it is found that the kcat/Km values for the mutants drop by 5.7 to 75fold when compared with the wild-type enzyme
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molecular dynamics simulations of wild-type and in silico W181S, W181T, W181Y, and W181F PfHGXPRT mutants bound to IMP/PPi/Mg2+, overview. Escherichia coli strain Sphi609, (ara, DELTApro-gpt-lac, thi, hpt, pup, purH, J, strA) is a knockout strain for the genes encoding hypoxanthine phosphoribosyltransferase (HPRT) and xanthine-guanine phosphoribosyltransferase (XGPRT). Although activation of the enzyme mutants by IMP increases their catalytic efficiency by about 100fold, it is found that the kcat/Km values for the mutants drop by 5.7 to 75fold when compared with the wild-type enzyme
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chimeric constructs expressing N-terminal peptides of 11 amino acids from isoform I or of 60 amino acids from isoform II fused to a chloramphenicol acetyl transferase reporter show that the N-terminal domain of isoform II is both necessary and sufficient for membrane association
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construction of deletion mutant lacking 7 amino acid residues, Y82-S88, of the active site loop II, resulting in highly reduced kcat-values and in increased Km-values for the substrates
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saturation mutagenesis and complement selection for investigation of functional roles of residues Leu67 and Gly69, sequencing of 70 clones and identification of 30 different mutations, several mutants of L67 or G69 support bacterial growth on minimal medium, but only L67M and G69S can be expressed and purified from overexpressing bacteria, overview
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saturation mutagenesis for randomly exchange of amino acids of the active site loop II, construction of diverse mutants of the residues S102 to Q112, kinetic analysis and determination of catalytic efficiencies in the forward and reverse reaction, overview
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truncation of the C-terminal stretch of enzyme TcHPRTH6 enhances its catalytic efficiency
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truncation of the C-terminal stretch of enzyme TcHPRTH6 enhances its catalytic efficiency
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