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2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminopurine nucleoside-5'-monophosphate + diphosphate
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminopurine ribotide + diphosphate
2,6-diaminopurine 5-phosphoribosyl nucleotide + diphosphate
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminpurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminpurine 5'-phosphoribosyl nucleotide + diphosphate
2-aminobenzimidazole 5'-phosphoribosyl nucleotide + diphosphate
2-aminobenzimidazole + 5-phospho-alpha-D-ribose 1-diphosphate
very low activity
-
-
r
2-chloro-AMP + diphosphate
2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
best substrate
-
-
r
2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-chloro-AMP + diphosphate
2-fluoro-AMP + diphosphate
2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-fluoro-AMP + diphosphate
2-methoxyadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-methoxyadenosine 5'-monophosphate + diphosphate
-
-
-
r
2-methoxyadenosine 5'-phosphate + diphosphate
2-methoxyadenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
4-amino-5-imidazolecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
4-amino-5-imidazolecarboxamide ribotide + diphosphate
-
-
-
-
?
4-aminopyrazolo-(3,4-d)-pyrimidine + 5-phospho-alpha-D-ribose 1-diphosphate
4-aminopyrazolo-(3,4-d)-pyrimidine ribotide + diphosphate
-
-
-
-
?
4-carbamoylimidazolium 5-olate + 5-phospho-alpha-D-ribose 1-diphosphate
4-carbamoylimidazolium 5-olate 5'-phosphate + diphosphate
-
low activity
-
-
?
5-amino-4-imidazolecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
5-amino-4-imidazolecarboxamide ribotide + diphosphate
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
6-amino-2-hydroxypurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-amino-2-hydroxypurine ribotide + diphosphate
-
-
-
-
?
6-mercaptopurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-mercaptopurine ribotide + diphosphate
-
-
-
-
?
6-methoxyguanine + 5-phospho-alpha-D-ribose 1-diphosphate
6-methoxyguanosine 5'-monophosphate + diphosphate
-
-
-
r
6-methylpurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-methylpurine ribonucleoside-5'-monophosphate + diphosphate
-
-
-
r
6-methylpurine + 5-phospho-alpha-D-ribose 1-diphosphate
6-methylpurine ribotide + diphosphate
-
-
-
-
?
8-azaadenine + 5-phospho-alpha-D-ribose 1-diphosphate
8-azaadenosine 5'-phosphate + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
allopurinol + 5-phospho-alpha-D-ribose 1-diphosphate
?
-
-
-
r
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
benzyladenine + 5-phospho-alpha-D-ribose 1-diphosphate
benzyladenosine 5'-phosphate + diphosphate
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
-
at about 5.7% of the conversion rate for adenine
-
-
?
isopentenyladenine + 5-phospho-alpha-D-ribose 1-diphosphate
isopentenyladenosine 5'-phosphate + diphosphate
N1-methoxyadenine + 5-phospho-alpha-D-ribose 1-diphosphate
N1-methoxyadenosine 5'-monophosphate + diphosphate
-
-
-
r
N1-methyladenosine 5'-phosphate + diphosphate
N1-methyladenosine + 5-phospho-alpha-D-ribose 1-diphosphate
high activity
-
-
r
N6-benzyladenosine 5'-phosphate + diphosphate
N6-benzyladenine + 5-phospho-alpha-D-ribose 1-diphosphate
very low activity
-
-
r
N6-furfuryladenine + 5-phospho-alpha-D-ribose 1-diphosphate
N6-furfuryladenosine 5'-phosphate + diphosphate
-
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
xanthosine 5'-phosphate + diphosphate
-
-
-
-
?
zeatin + 5-phospho-alpha-D-ribose 1-diphosphate
zeatin riboside 5'-phosphate + diphosphate
additional information
?
-
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminopurine nucleoside-5'-monophosphate + diphosphate
-
-
-
r
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminopurine nucleoside-5'-monophosphate + diphosphate
-
-
-
r
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminopurine nucleoside-5'-monophosphate + diphosphate
-
-
-
r
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminopurine ribotide + diphosphate
-
specific for adenine or 2,6-diaminopurine
-
-
?
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminopurine ribotide + diphosphate
-
-
-
-
?
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminopurine ribotide + diphosphate
-
-
-
-
?
2,6-diaminopurine 5-phosphoribosyl nucleotide + diphosphate
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
2,6-diaminopurine 5-phosphoribosyl nucleotide + diphosphate
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
2,6-diaminopurine 5-phosphoribosyl nucleotide + diphosphate
2,6-diaminopurine + 5-phospho-alpha-D-ribose 1-diphosphate
low activity
-
-
r
2,6-diaminpurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminpurine 5'-phosphoribosyl nucleotide + diphosphate
-
-
-
r
2,6-diaminpurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminpurine 5'-phosphoribosyl nucleotide + diphosphate
-
-
-
r
2,6-diaminpurine + 5-phospho-alpha-D-ribose 1-diphosphate
2,6-diaminpurine 5'-phosphoribosyl nucleotide + diphosphate
-
-
-
r
2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-chloro-AMP + diphosphate
-
-
-
r
2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-chloro-AMP + diphosphate
-
-
-
r
2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-chloro-AMP + diphosphate
-
-
-
r
2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-chloro-AMP + diphosphate
-
-
-
r
2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-chloro-AMP + diphosphate
-
-
-
r
2-chloroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-chloro-AMP + diphosphate
-
-
-
r
2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-fluoro-AMP + diphosphate
-
-
-
r
2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-fluoro-AMP + diphosphate
-
-
-
r
2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-fluoro-AMP + diphosphate
-
-
-
r
2-fluoroadenine + 5-phospho-alpha-D-ribose 1-diphosphate
2-fluoro-AMP + diphosphate
-
-
-
r
5-amino-4-imidazolecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
5-amino-4-imidazolecarboxamide ribotide + diphosphate
-
-
-
-
?
5-amino-4-imidazolecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
5-amino-4-imidazolecarboxamide ribotide + diphosphate
-
-
-
?
5-amino-4-imidazolecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
5-amino-4-imidazolecarboxamide ribotide + diphosphate
-
no activity
-
-
?
5-amino-4-imidazolecarboxamide + 5-phospho-alpha-D-ribose 1-diphosphate
5-amino-4-imidazolecarboxamide ribotide + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
-
-
-
?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
-
-
-
?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
enzyme deficiency leads to severe renal failure, overview
-
-
?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
-
-
-
?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
-
-
-
?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
the enzyme is involved in the salvage of adenosine, overview
-
-
?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
-
the enzyme is involved in the salvage of adenosine, overview
-
-
?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribosyl-1-diphosphate + adenine
AMP + diphosphate
-
the enzyme is involved in the salvage of adenosine, overview
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
best acceptor substrate
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
isoform APT1 shows 100% activity with adenine
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
equilibrium lies far in the direction of nucleotide synthesis
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
adenine salvage enzyme
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
specific for adenine or 2,6-diamino-purine
5'-AMP
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
enzyme mediates the translocation of adenine into the cell as AMP
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
necessary for appropriate regulation of purine de novo biosynthesis
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
ordered substrate binding in the reverse reaction with AMP bound first followed by diphosphate
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
substrate binding structure
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
best acceptor substrate
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
highly specific for the donor substrate
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
human APRT deficiency results in serious kidney illness such as nephrolithiasis, interstitial nephritis, and chronic renal failure as a result of 2,8-dihydroxyadenine precipitation in the renal interstitium
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
binding to hAPRT is substrate shape-specific in the forward reaction, whereas it is base-specific in the reverse reaction
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
human APRT catalyzes the transformation of adenine into AMP and vice versa
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
substrate binding structure
AMP is bound in the low energy anti conformation with the ribose in the 2' endo conformation
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
strong preference for adenine as substrate over the 6-oxopurine bases, hypoxanthine and guanine
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
strong preference for adenine as substrate over the 6-oxopurine bases, hypoxanthine and guanine
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
diphosphate does not bind at the active site, but near the N-terminal side at Arg69
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
transfer to N9 of adenine
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?, r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
transfer to N9 of adenine
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?, r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
transfer to N9 of adenine
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
may play a role in maintaining the supply of adequate levels of active cytokinin
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
key enzyme that converts AMP in the purine salvage pathway. TaAPT2 gene may be related to the fertility alteration and abortion of pollen development
-
-
?
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
-
r
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
AMP + diphosphate
-
-
-
?
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
?
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
adenine binds to only one of the two subunits, leaving the adjacent adenine-free binding pockets occupied by a symmetry-related Tyr107 side chain, suggesting subunit-sequential catalytic site activity
-
-
?
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
adenine binds to only one of the two subunits, leaving the adjacent adenine-free binding pockets occupied by a symmetry-related Tyr107 side chain, suggesting subunit-sequential catalytic site activity
-
-
?
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
AMP + diphosphate
adenine + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
benzyladenine + 5-phospho-alpha-D-ribose 1-diphosphate
benzyladenosine 5'-phosphate + diphosphate
-
-
-
-
?
benzyladenine + 5-phospho-alpha-D-ribose 1-diphosphate
benzyladenosine 5'-phosphate + diphosphate
-
-
-
?
benzyladenine + 5-phospho-alpha-D-ribose 1-diphosphate
benzyladenosine 5'-phosphate + diphosphate
-
N6-benzyladenine
-
-
?
isopentenyladenine + 5-phospho-alpha-D-ribose 1-diphosphate
isopentenyladenosine 5'-phosphate + diphosphate
-
-
-
-
?
isopentenyladenine + 5-phospho-alpha-D-ribose 1-diphosphate
isopentenyladenosine 5'-phosphate + diphosphate
-
-
-
?
isopentenyladenine + 5-phospho-alpha-D-ribose 1-diphosphate
isopentenyladenosine 5'-phosphate + diphosphate
-
N6-(delta-isopentenyl)adenine
-
-
?
zeatin + 5-phospho-alpha-D-ribose 1-diphosphate
zeatin riboside 5'-phosphate + diphosphate
-
-
-
?
zeatin + 5-phospho-alpha-D-ribose 1-diphosphate
zeatin riboside 5'-phosphate + diphosphate
isoform APT4 shows about 38% activity with zeatin
-
-
?
zeatin + 5-phospho-alpha-D-ribose 1-diphosphate
zeatin riboside 5'-phosphate + diphosphate
isoform APT5 shows 100% activity with zeatin
-
-
?
zeatin + 5-phospho-alpha-D-ribose 1-diphosphate
zeatin riboside 5'-phosphate + diphosphate
isoforms APT1 shows 100% activity with zeatin
-
-
?
additional information
?
-
isoform APT2 is nearly inactive with adenine and zeatin
-
-
?
additional information
?
-
isoform APT2 is nearly inactive with adenine and zeatin
-
-
?
additional information
?
-
isoform APT2 is nearly inactive with adenine and zeatin
-
-
?
additional information
?
-
isoform APT2 is nearly inactive with adenine and zeatin
-
-
?
additional information
?
-
isoform APT4 is nearly inactive with adenine
-
-
?
additional information
?
-
isoform APT4 is nearly inactive with adenine
-
-
?
additional information
?
-
isoform APT4 is nearly inactive with adenine
-
-
?
additional information
?
-
isoform APT4 is nearly inactive with adenine
-
-
?
additional information
?
-
isoform APT5 is nearly inactive with adenine
-
-
?
additional information
?
-
isoform APT5 is nearly inactive with adenine
-
-
?
additional information
?
-
isoform APT5 is nearly inactive with adenine
-
-
?
additional information
?
-
isoform APT5 is nearly inactive with adenine
-
-
?
additional information
?
-
APRT differentiates adenine from other purines
-
-
-
additional information
?
-
APRT differentiates adenine from other purines
-
-
-
additional information
?
-
-
no activity with hypoxanthine, guanine, cytosine
-
-
?
additional information
?
-
-
no substrate: adenosine
-
-
?
additional information
?
-
-
no donor substrates: D-ribose 5-phosphate, ribose 1-phosphate
-
-
?
additional information
?
-
-
no substrate: hypoxanthine,guanine
-
-
?
additional information
?
-
-
at 0°C in the absence of Mg2+ but in presence of substrates the enzyme catalyzes a rapid and limited synthesis of AMP
-
-
?
additional information
?
-
although hypoxanthine and adenine have the same chemical skeleton, which differs only by a hydroxyl instead of an amine at the C6 position away from the reactive N9 nitrogen, adenine seems to be the only purine metabolized by hAPRT
-
-
-
additional information
?
-
-
although hypoxanthine and adenine have the same chemical skeleton, which differs only by a hydroxyl instead of an amine at the C6 position away from the reactive N9 nitrogen, adenine seems to be the only purine metabolized by hAPRT
-
-
-
additional information
?
-
both the PRPP and ADE substrates are well ordered in all four subunits of the enzyme's crystal asymmetric unit, substrates' binding structures, overview. Residue Tyr105 favors the forward reaction. Tyr105 is in contact with both adenine and PRPP substrates in the closed conformation of the flexible loop. It might therefore play a role in the enzyme catalytic processes
-
-
-
additional information
?
-
-
both the PRPP and ADE substrates are well ordered in all four subunits of the enzyme's crystal asymmetric unit, substrates' binding structures, overview. Residue Tyr105 favors the forward reaction. Tyr105 is in contact with both adenine and PRPP substrates in the closed conformation of the flexible loop. It might therefore play a role in the enzyme catalytic processes
-
-
-
additional information
?
-
induced change in the APT2 expression pattern in young panicles may mediate, at least in part, thermosensitive genic male sterility in the cultivar Annong S-1
-
-
?
additional information
?
-
-
induced change in the APT2 expression pattern in young panicles may mediate, at least in part, thermosensitive genic male sterility in the cultivar Annong S-1
-
-
?
additional information
?
-
APRT from Thermus thermophilus is known to have broad specificity in relation to adenine analogues, while it shows no significant catalytic activity if stereoisomers of PRPP are used as a substrate, narrow PRPP analogue specificity. One of the key factors determining the substrate specificity of an enzyme is its structure and the conformation of its active site in particular. Enzyme ligand interaction analysis
-
-
-
additional information
?
-
-
APRT from Thermus thermophilus is known to have broad specificity in relation to adenine analogues, while it shows no significant catalytic activity if stereoisomers of PRPP are used as a substrate, narrow PRPP analogue specificity. One of the key factors determining the substrate specificity of an enzyme is its structure and the conformation of its active site in particular. Enzyme ligand interaction analysis
-
-
-
additional information
?
-
no activity with 6-oxopurines (7-deazaxanthine and 7-deaza-6-hydroxypurine), 6-thiopurines (6-mercaptopurine), and 6-halopurines (6-chloropurine)
-
-
-
additional information
?
-
not only adenine but also a number of its derivatives, including 2-chloro- and 2-fluoroadenine, 2-methoxyadenine, N1-methoxyadenine, and 2,6-diaminpurine, are substrates of the enzyme
-
-
-
additional information
?
-
purine nucleotide synthesis using TthAPRT and TthHPRT (EC 2.4.2.8). No or poor activity with 8-azaguanine, thymine, 1,2,4-triazole-3-carboxamide, and 1,2,4-triazole-3-carboxy-N-methylamide
-
-
-
additional information
?
-
substrate specificity, overview. TtAPRT2 can use adenine as acceptor for NMP synthesis. But neither guanine nor hypoxanthine or xanthine are recognized as substrates by TtAPRT2
-
-
-
additional information
?
-
the enzyme APRT is specific for adenine, very poor activity with guanine, hypoxanthine, and xanthine
-
-
-
additional information
?
-
the enzyme APRT is specific for adenine, very poor activity with guanine, hypoxanthine, and xanthine
-
-
-
additional information
?
-
-
the enzyme APRT is specific for adenine, very poor activity with guanine, hypoxanthine, and xanthine
-
-
-
additional information
?
-
the enzyme encoded by gene TT_C1249 exhibits no detectable activity toward adenine, guanine, hypoxanthine, or xanthine. TTC1249 is a homologue of APRT (APRTh). Lack of activity of APRTh may be due to the replacement of the residues involved in binding the monophosphate of nucleotide
-
-
-
additional information
?
-
the enzyme encoded by gene TT_C1249 exhibits no detectable activity toward adenine, guanine, hypoxanthine, or xanthine. TTC1249 is a homologue of APRT (APRTh). Lack of activity of APRTh may be due to the replacement of the residues involved in binding the monophosphate of nucleotide
-
-
-
additional information
?
-
-
the enzyme encoded by gene TT_C1249 exhibits no detectable activity toward adenine, guanine, hypoxanthine, or xanthine. TTC1249 is a homologue of APRT (APRTh). Lack of activity of APRTh may be due to the replacement of the residues involved in binding the monophosphate of nucleotide
-
-
-
additional information
?
-
substrate specificity, overview. TtAPRT2 can use adenine as acceptor for NMP synthesis. But neither guanine nor hypoxanthine or xanthine are recognized as substrates by TtAPRT2
-
-
-
additional information
?
-
no activity with 6-oxopurines (7-deazaxanthine and 7-deaza-6-hydroxypurine), 6-thiopurines (6-mercaptopurine), and 6-halopurines (6-chloropurine)
-
-
-
additional information
?
-
not only adenine but also a number of its derivatives, including 2-chloro- and 2-fluoroadenine, 2-methoxyadenine, N1-methoxyadenine, and 2,6-diaminpurine, are substrates of the enzyme
-
-
-
additional information
?
-
the enzyme APRT is specific for adenine, very poor activity with guanine, hypoxanthine, and xanthine
-
-
-
additional information
?
-
the enzyme APRT is specific for adenine, very poor activity with guanine, hypoxanthine, and xanthine
-
-
-
additional information
?
-
APRT from Thermus thermophilus is known to have broad specificity in relation to adenine analogues, while it shows no significant catalytic activity if stereoisomers of PRPP are used as a substrate, narrow PRPP analogue specificity. One of the key factors determining the substrate specificity of an enzyme is its structure and the conformation of its active site in particular. Enzyme ligand interaction analysis
-
-
-
additional information
?
-
the enzyme encoded by gene TT_C1249 exhibits no detectable activity toward adenine, guanine, hypoxanthine, or xanthine. TTC1249 is a homologue of APRT (APRTh). Lack of activity of APRTh may be due to the replacement of the residues involved in binding the monophosphate of nucleotide
-
-
-
additional information
?
-
the enzyme encoded by gene TT_C1249 exhibits no detectable activity toward adenine, guanine, hypoxanthine, or xanthine. TTC1249 is a homologue of APRT (APRTh). Lack of activity of APRTh may be due to the replacement of the residues involved in binding the monophosphate of nucleotide
-
-
-
additional information
?
-
substrate specificity, overview. TtAPRT2 can use adenine as acceptor for NMP synthesis. But neither guanine nor hypoxanthine or xanthine are recognized as substrates by TtAPRT2
-
-
-
additional information
?
-
no activity with 6-oxopurines (7-deazaxanthine and 7-deaza-6-hydroxypurine), 6-thiopurines (6-mercaptopurine), and 6-halopurines (6-chloropurine)
-
-
-
additional information
?
-
not only adenine but also a number of its derivatives, including 2-chloro- and 2-fluoroadenine, 2-methoxyadenine, N1-methoxyadenine, and 2,6-diaminpurine, are substrates of the enzyme
-
-
-
additional information
?
-
the enzyme APRT is specific for adenine, very poor activity with guanine, hypoxanthine, and xanthine
-
-
-
additional information
?
-
the enzyme APRT is specific for adenine, very poor activity with guanine, hypoxanthine, and xanthine
-
-
-
additional information
?
-
APRT from Thermus thermophilus is known to have broad specificity in relation to adenine analogues, while it shows no significant catalytic activity if stereoisomers of PRPP are used as a substrate, narrow PRPP analogue specificity. One of the key factors determining the substrate specificity of an enzyme is its structure and the conformation of its active site in particular. Enzyme ligand interaction analysis
-
-
-
additional information
?
-
the enzyme encoded by gene TT_C1249 exhibits no detectable activity toward adenine, guanine, hypoxanthine, or xanthine. TTC1249 is a homologue of APRT (APRTh). Lack of activity of APRTh may be due to the replacement of the residues involved in binding the monophosphate of nucleotide
-
-
-
additional information
?
-
the enzyme encoded by gene TT_C1249 exhibits no detectable activity toward adenine, guanine, hypoxanthine, or xanthine. TTC1249 is a homologue of APRT (APRTh). Lack of activity of APRTh may be due to the replacement of the residues involved in binding the monophosphate of nucleotide
-
-
-
additional information
?
-
-
no substrate: hypoxanthine,guanine
-
-
?
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2,6-diaminopurine
-
competitive
4-aminopyrido(2,3-d)pyrimidine
-
-
4-aminopyrolo(2,3-d)pyrimidine
-
-
6-Mercaptopurine
-
competitive
alpha-D-5-phosphoribose 1-diphosphate
-
substrate inhibition
benznidazole
-
transcriptome and functional genomics reveal the participation of adenine phosphoribosyltransferase in Trypanosoma cruzi resistance to benznidazole
benzyladenine
-
competitive
D-2,5-dideoxy-2,5-imino-altritol 1,6-bisphosphate
D-DIAB, a iminoaltritol bis-phosphate, transition-state analogue inhibitor, enzyme interactions and binding structure analysis
EDTA
-
reversible by 2-mercaptoethanol and excess Mg2+
formycin AMP
-
competitive against adenine and diphosphate
immucillin AB
-
does not bind at the active site
isodutaduprine
-
alkaloid from Almeidea rubra, 21.6% inhibition at 0.0356 mM of the recombinant enzyme
isokokusagine
-
alkaloid from Almeidea rubra, 44.6% inhibition at 0.0412 mM of the recombinant enzyme
isoskimmianine
-
alkaloid from Almeidea rubra, 39.1% inhibition at 0.0386 mM of the recombinant enzyme
L-2,5-dideoxy-2,5-imino-altritol 1,6-bisphosphate
L-DIAB, a iminoaltritol bis-phosphate, enzyme binding structure analysis
adenine
-
-
adenine
-
substrate inhibition, 0.08 mM, 50% inhibition in Propositus (HPRT-) and 20% in control(HPRT+)
adenine
-
at high concentrations, at low 5-phospho-alpha-D-ribose 1-diphosphate concentration
ADP
-
-
ADP
-
is a much stronger inhibitor than ATP at pH 4.5, but has virtually no effect on activity at neutral pH
ADP
the inhibitor binds like the product AMP with both the alpha- and beta-phosphates occupying the 5'-phosphoribosyl binding site
AMP
-
-
AMP
-
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
AMP
-
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
AMP
-
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
AMP
competitive against 5-phospho-alpha-D-ribose 1-diphosphate; competitive against adenine
AMP
-
2 mM, 80% inhibition with Propositus (HPRT-) and 58% in control(HPRT+)
AMP
5-phospho-alpha-D-ribose 1-diphosphate and AMP compete for the same site where the latter also acts as a competitive inhibitor of the forward reaction. Tyr105 prevents strong inhibition of hAPRT by AMP
AMP
-
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
ATP
-
-
Ba2+
-
in presence of MnCl2
Ca2+
-
in presence of MnCl2
Ca2+
-
activation, competitive to Mg2+
Cd2+
-
in presence of MnCl2
diphosphate
-
-
diphosphate
noncompetitive against 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate
-
no inhibition
diphosphate
-
competitive against adenine and 5-phosphoribose 1-diphosphate
GMP
-
-
guanine
-
noncompetitive against 5-phosphoribose 1-diphosphate
Hg2+
-
in presence of MnCl2
Hg2+
-
reversed by 2-mercaptoethanol
Hg2+
-
complete inhibition at 5 mM
Mg2+
-
inhibition in presence of MnCl2, activation in absence
Mg2+
-
inhibition above 2 mM, activation below
Mg2+
required, high concentration of Mg2+ inhibited the reaction with a Ki = 5.4 mM
Mg2+
-
inhibitory effects are noncompetitive against 5-phosphoribose 1-diphosphate
N-ethylmaleimide
-
-
N-ethylmaleimide
-
strong, DTT or glutathione protect
N-ethylmaleimide
-
no inhibition
Na+
-
no inhibition
nucleotides
-
higher concentrations of all 5'-nucleotides are most inhibitory, 6-OH purine nucleotides are moderately inhibitory, pyrimidine nucleotides are least inhibitory
-
nucleotides
-
effect is strongly influenced by pH, inhibition at pH 7.1: ATP, GMP, activation at pH 7.1: GTP, UMP, UTP, CMP, CTP, IMP, no effect at pH 7.1: AMP, inhibition at pH 8.0: AMP, ATP, GMP, GTP, UTP, CTP, IMP, no effect at pH 8.0: UMP, CMP
-
nucleotides
-
nucleotide mono-, di- and triphosphates of adenine, guanine and hypoxanthine
-
nucleotides
-
effect is strongly influenced by pH, inhibition at pH 7.1: ATP, GMP, activation at pH 7.1: GTP, UMP, UTP, CMP, CTP, IMP, no effect at pH 7.1: AMP, inhibition at pH 8.0: AMP, ATP, GMP, GTP, UTP, CTP, IMP, no effect at pH 8.0: UMP, CMP
-
p-chloromercuribenzoate
-
complete inhibition at 1 mM, DTT or glutathione protect
p-chloromercuribenzoate
-
no inhibition
p-chloromercuribenzoate
-
no inhibition
p-chloromercuribenzoate
-
reversed by 2-mercaptoethanol and excess Mg2+
p-hydroxymercuribenzoate
-
DTT
p-hydroxymercuribenzoate
-
not enzyme from monkey liver
Pb2+
-
inhibits the enzyme in erythrocytes about 25% at 0.0005 mM and about 20% at 0.0001 mM, and participates in hemolysis, the intensity of which negatively correlates with the activity of phosphoribosyltransferases, APRT 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, APRT inhibition as one of the mechanisms of lead toxicity
SO42-
-
no inhibition
sulfhydryl reagents
-
-
Zn2+
-
-
additional information
-
no substrate inhibition by adenine
-
additional information
-
no effect of a variety of sugars, amino acids, organic acids and nucleotides tested, except for AMP, have any effect on the enzyme activity; not affected by PO43-
-
additional information
-
methanolic and hexanic extracts from roots and leaves of Cedrela fissilis and from fruits, branches and leaves of Cipadessa fruticosa show strong antileishmanicidal activities, the inhibitory activities of plant organ extracts with dichloromethane are lower, overview
-
additional information
not inhibited by Ocimum basilicum leaf essential oil
-
additional information
-
not affected by 2,6-diaminopurine, 4-carbamoylimidazolium 5-olate, 8-azaadenine, and 2-fluoro-6-aminopurine
-
additional information
expression of gene OsAPT2 is temperature-sensitive and is downregulated at 29°C
-
additional information
-
expression of gene OsAPT2 is temperature-sensitive and is downregulated at 29°C
-
additional information
-
no inhibition by iodoacetamide, DTNB
-
additional information
an enantiomeric pair of iminoaltritol bis-phosphates (L-DIAB and D-DIAB) is synthesized and shown to display inhibition of Saccharomyces cerevisiae adenine phosphoribosyltransferase (ScAPRT). Synthesis pathway, detailed overview. Crystallographic inhibitor binding analysis of L- and D-DIAB bound to the catalytic sites of ScAPRT demonstrates accommodation of both enantiomers by altered ring geometry and bis-phosphate catalytic site contacts
-
additional information
-
an enantiomeric pair of iminoaltritol bis-phosphates (L-DIAB and D-DIAB) is synthesized and shown to display inhibition of Saccharomyces cerevisiae adenine phosphoribosyltransferase (ScAPRT). Synthesis pathway, detailed overview. Crystallographic inhibitor binding analysis of L- and D-DIAB bound to the catalytic sites of ScAPRT demonstrates accommodation of both enantiomers by altered ring geometry and bis-phosphate catalytic site contacts
-
additional information
-
mechanism of product inhibition; no inhibition by GMP, XMP, UMP, CMP, and CDP
-
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evolution
adenine phosphoribosyltransferase (APRT) from the thermophilic eubacteria Thermus thermophilus belongs to the type I phosphorybosyltransferase protein family on the basis of its structure and catalytic activity
evolution
APRT refers to the type I phosphoribosyltransferase (PRT) family, which belongs to the large glycosyltransferase family
evolution
the TTC1250 gene encoding APRT, has 41% amino acid sequence identity to gene TTC1249 encoding APRTh, an catalytically inactve APRT homologue
evolution
the TTC1250 gene, which also encodes APRT, has 41% amino acid sequence identity to gene TTC1249 encoding APRTh
evolution
Thermus thermophilus strain HB27 enzyme TthHB27APRT belongs to the type I phosphoribosyltransferases. These share the alpha/beta type folding of the polypeptide chain and the presence of a specific sequence of 13 amino acid residues involved in binding of diphosphate (PRPP-binding motif), together with a structurally variable subdomain (the so-called, hood domain) involved in base recognition
evolution
three putative APRT isoforms are described in the genome of Schistosoma mansoni, namely, Smp_054360, Smp_054410, and Smp_151260, which are referred to as SmAPRT 1, 2 and 3, respectively. Phylogenetic analysis reveals that APRT exists in multiple copies originating from gene duplications at the base of the Schistosoma genus
evolution
-
the TTC1250 gene encoding APRT, has 41% amino acid sequence identity to gene TTC1249 encoding APRTh, an catalytically inactve APRT homologue
-
evolution
-
adenine phosphoribosyltransferase (APRT) from the thermophilic eubacteria Thermus thermophilus belongs to the type I phosphorybosyltransferase protein family on the basis of its structure and catalytic activity
-
evolution
-
Thermus thermophilus strain HB27 enzyme TthHB27APRT belongs to the type I phosphoribosyltransferases. These share the alpha/beta type folding of the polypeptide chain and the presence of a specific sequence of 13 amino acid residues involved in binding of diphosphate (PRPP-binding motif), together with a structurally variable subdomain (the so-called, hood domain) involved in base recognition
-
evolution
-
the TTC1250 gene, which also encodes APRT, has 41% amino acid sequence identity to gene TTC1249 encoding APRTh
-
evolution
-
the TTC1250 gene encoding APRT, has 41% amino acid sequence identity to gene TTC1249 encoding APRTh, an catalytically inactve APRT homologue
-
evolution
-
adenine phosphoribosyltransferase (APRT) from the thermophilic eubacteria Thermus thermophilus belongs to the type I phosphorybosyltransferase protein family on the basis of its structure and catalytic activity
-
evolution
-
Thermus thermophilus strain HB27 enzyme TthHB27APRT belongs to the type I phosphoribosyltransferases. These share the alpha/beta type folding of the polypeptide chain and the presence of a specific sequence of 13 amino acid residues involved in binding of diphosphate (PRPP-binding motif), together with a structurally variable subdomain (the so-called, hood domain) involved in base recognition
-
evolution
-
the TTC1250 gene, which also encodes APRT, has 41% amino acid sequence identity to gene TTC1249 encoding APRTh
-
malfunction
-
a congenital deficiency in the enzyme adenine phosphoribosyltransferase causes the disorder with 2,8-dihydroxyadenine crystalluria. In most cases, APRT deficiency is caused by autosomal recessive inheritance of a homozygote of the mutant gene APRT*Q0 or APRT*J, but there are also some cases in which the disorder is caused by the compound heterozygote APRT*Q0 and APRT*J
malfunction
loss of enzyme activity leads to excess accumulation of cytokinin bases, thus evoking myriad cytokinin-regulated responses, such as delayed leaf senescence, anthocyanin accumulation, and downstream gene expression
malfunction
APRT deficiencies in this enzyme lead to 2,8-dihydroxyadenine urolithiasis, and renal and allograft failures
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
-
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
adenine phosphoribosyl transferase 1 is a key metabolic enzyme participating in the cytokinin inactivation by phosphoribosylation
metabolism
APRT from Thermus thermophilus is a member of purine nucleotide processing methabolical pathways and can be used as a key component of an nucleotide synthesis enzymatic cascade that uses only pentose carbohydrates, nitrogenous bases and ATP as substrates
metabolism
APRT is an enzyme involved in the salvage of adenine (a 6-aminopurine), converting it to AMP. The purine salvage pathway relies on two essential and distinct enzymes to convert 6-aminopurine and 6-oxopurines into corresponding nucleotides
metabolism
enzyme APRT is a key enzyme in the purine salvage pathway in prokaryotes and eukaryotes
metabolism
the reversible adenine phosphoribosyltransferase enzyme (APRT) is essential for purine homeostasis in prokaryotes and eukaryotes. In humans, APRT (hAPRT) is the only enzyme known to produce AMP in cells from dietary adenine. APRT can also process adenine analogues, which are involved in plant development or neuronal homeostasis
metabolism
type I phosphoribosyltransferases play an important role in common and salvage pathways of purine, pyrimidine, and pyrimidine coenzyme synthesis, as well as biosynthesis of histidine and tryptophan in lower organisms
metabolism
-
APRT is an enzyme involved in the salvage of adenine (a 6-aminopurine), converting it to AMP. The purine salvage pathway relies on two essential and distinct enzymes to convert 6-aminopurine and 6-oxopurines into corresponding nucleotides
-
metabolism
-
APRT from Thermus thermophilus is a member of purine nucleotide processing methabolical pathways and can be used as a key component of an nucleotide synthesis enzymatic cascade that uses only pentose carbohydrates, nitrogenous bases and ATP as substrates
-
metabolism
-
type I phosphoribosyltransferases play an important role in common and salvage pathways of purine, pyrimidine, and pyrimidine coenzyme synthesis, as well as biosynthesis of histidine and tryptophan in lower organisms
-
metabolism
-
APRT from Thermus thermophilus is a member of purine nucleotide processing methabolical pathways and can be used as a key component of an nucleotide synthesis enzymatic cascade that uses only pentose carbohydrates, nitrogenous bases and ATP as substrates
-
metabolism
-
type I phosphoribosyltransferases play an important role in common and salvage pathways of purine, pyrimidine, and pyrimidine coenzyme synthesis, as well as biosynthesis of histidine and tryptophan in lower organisms
-
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 enables the reutilization of purine base adenine converting it to mononucleotide AMP, substrate for the synthesis of high-energy nucleotides
physiological function
-
amplification of adenine phosphoribosyltransferase suppresses the conditionally lethal growth and virulence phenotype of Leishmania donovani mutants lacking both hypoxanthine-guanine and xanthine phosphoribosyltransferases. Transfection of mutants lacking both hypoxanthine-guanine and xanthine phosphoribosyltransferases with an adenine phosphoribosyltransferase episome recapitulates the suppressor phenotype in vitro and enables growth on 6-oxypurines. Hypoxanthine is an inefficient substrate for adenine phosphoribosyltransferase
physiological function
adenine phosphoribosyltransferase (APRT) belongs to the type I phosphoribosyltransferases and catalyzes the formation of adenosine monophosphate via transfer of the 5-phosphoribosyl group from phosphoribosyl diphosphate to the nitrogen atom N9 of the adenine base
physiological function
adenine phosphoribosyltransferase, APRT catalyzes the transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl-1-diophosphate (PRPP) to N9 in 6-aminopurines, such as adenine or 6-aminopurine derivatives (e.g. 2,6-diaminopurine, 6-methylpurine, 2-fluoroadenine, among others), in presence of Mg2+ to obtain the corresponding NMPs
physiological function
APRT is the sole enzyme with the crucial role of recycling (or salvaging) freely available adenine into AMP and exists in all phyla of life
physiological function
enzyme adenine phosphoribosyltransferase homologue occurs in complex with Thermus thermophilus glutamate dehydrogenase. APRTh mediates the allosteric activation of GDH by AMP, but shows no adenine phosphoribosyltransferase activity. Presence of complicated regulatory mechanisms of GDH mediated by multiple compounds to control the carbonnitrogen balance in bacterial cells. APRTh functions in the cell and supports the optimal growth of Thermus thermophilus in minimal medium
physiological function
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expression and role of adenine phosphoribosyltransferase (APRT) in Trypanosoma cruzi resistance to benznidazole (Bz), overview
physiological function
phosphoribosyltransferases catalyze the displacement of a PRPP alpha-1'-diphosphate to a nitrogen-containing nucleobase. Phosphoribosyltransferase APRT residue Tyr105 is essential for cell growth by facilitating the forward reaction, The APRT Tyr105 drives purine biosynthesis in vivo. Tyr105 is key for the fine-tuning of the kinetic activity efficiencies of forward and reverse reactions. In crystallo activity shows that the hydroxyl group of Tyr105 is essential to select the bioactive conformation of the dynamic flexible loop and to form the products
physiological function
purine phosphoribosyltransferases, purine PRTs, are essential enzymes in the purine salvage pathway of living organisms. They are involved in the formation of C-N glycosidic bonds in purine nucleosides-5'-monophosphate (NMPs) through the transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl-1-diphosphate (PRPP) to purine nucleobases in the presence of Mg2+
physiological function
Schistosoma mansoni depends upon the purine salvage pathway to obtain purine nucleotides. Therefore, enzymes from this pathway are essential for parasite survival, e.g. the adenine phosphoribosyltransferase (APRT) enzyme, which catalyzes the condensation reaction between adenine and PRPP (5-phosphoribosyldiphosphate) to produce AMP and PPi
physiological function
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expression and role of adenine phosphoribosyltransferase (APRT) in Trypanosoma cruzi resistance to benznidazole (Bz), overview
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physiological function
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APRT is the sole enzyme with the crucial role of recycling (or salvaging) freely available adenine into AMP and exists in all phyla of life
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physiological function
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adenine phosphoribosyltransferase (APRT) belongs to the type I phosphoribosyltransferases and catalyzes the formation of adenosine monophosphate via transfer of the 5-phosphoribosyl group from phosphoribosyl diphosphate to the nitrogen atom N9 of the adenine base
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physiological function
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enzyme adenine phosphoribosyltransferase homologue occurs in complex with Thermus thermophilus glutamate dehydrogenase. APRTh mediates the allosteric activation of GDH by AMP, but shows no adenine phosphoribosyltransferase activity. Presence of complicated regulatory mechanisms of GDH mediated by multiple compounds to control the carbonnitrogen balance in bacterial cells. APRTh functions in the cell and supports the optimal growth of Thermus thermophilus in minimal medium
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physiological function
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expression and role of adenine phosphoribosyltransferase (APRT) in Trypanosoma cruzi resistance to benznidazole (Bz), overview
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physiological function
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expression and role of adenine phosphoribosyltransferase (APRT) in Trypanosoma cruzi resistance to benznidazole (Bz), overview
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physiological function
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purine phosphoribosyltransferases, purine PRTs, are essential enzymes in the purine salvage pathway of living organisms. They are involved in the formation of C-N glycosidic bonds in purine nucleosides-5'-monophosphate (NMPs) through the transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl-1-diphosphate (PRPP) to purine nucleobases in the presence of Mg2+
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physiological function
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adenine phosphoribosyltransferase, APRT catalyzes the transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl-1-diophosphate (PRPP) to N9 in 6-aminopurines, such as adenine or 6-aminopurine derivatives (e.g. 2,6-diaminopurine, 6-methylpurine, 2-fluoroadenine, among others), in presence of Mg2+ to obtain the corresponding NMPs
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physiological function
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purine phosphoribosyltransferases, purine PRTs, are essential enzymes in the purine salvage pathway of living organisms. They are involved in the formation of C-N glycosidic bonds in purine nucleosides-5'-monophosphate (NMPs) through the transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl-1-diphosphate (PRPP) to purine nucleobases in the presence of Mg2+
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physiological function
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adenine phosphoribosyltransferase, APRT catalyzes the transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl-1-diophosphate (PRPP) to N9 in 6-aminopurines, such as adenine or 6-aminopurine derivatives (e.g. 2,6-diaminopurine, 6-methylpurine, 2-fluoroadenine, among others), in presence of Mg2+ to obtain the corresponding NMPs
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physiological function
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adenine phosphoribosyltransferase (APRT) belongs to the type I phosphoribosyltransferases and catalyzes the formation of adenosine monophosphate via transfer of the 5-phosphoribosyl group from phosphoribosyl diphosphate to the nitrogen atom N9 of the adenine base
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physiological function
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enzyme adenine phosphoribosyltransferase homologue occurs in complex with Thermus thermophilus glutamate dehydrogenase. APRTh mediates the allosteric activation of GDH by AMP, but shows no adenine phosphoribosyltransferase activity. Presence of complicated regulatory mechanisms of GDH mediated by multiple compounds to control the carbonnitrogen balance in bacterial cells. APRTh functions in the cell and supports the optimal growth of Thermus thermophilus in minimal medium
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additional information
analysis of the molecular mechanism underlying substrate specificity of APRT and catalysis in both directions of the reaction. Comparison of the crystal structures of hAPRT complexed to three cellular nucleotide analogues (hypoxanthine, IMP, and GMP) with the phosphate-bound enzyme. Substrate shape recognition in the forward reaction, purine base recognition in the reverse reaction. Binding to hAPRT is substrate shape-specific in the forward reaction, whereas it is base-specific in the reverse reaction. Quantum mechanics/molecular mechanics (QM/MM) analysis suggests that the forward reaction is mainly a nucleophilic substitution of type 2 (SN2) with a mix of SN1-type molecular mechanism. Based on our structural analysis, a magnesium-assisted SN2-type mechanism is involved in the reverse reaction. Structure-function analysis, overview
additional information
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analysis of the molecular mechanism underlying substrate specificity of APRT and catalysis in both directions of the reaction. Comparison of the crystal structures of hAPRT complexed to three cellular nucleotide analogues (hypoxanthine, IMP, and GMP) with the phosphate-bound enzyme. Substrate shape recognition in the forward reaction, purine base recognition in the reverse reaction. Binding to hAPRT is substrate shape-specific in the forward reaction, whereas it is base-specific in the reverse reaction. Quantum mechanics/molecular mechanics (QM/MM) analysis suggests that the forward reaction is mainly a nucleophilic substitution of type 2 (SN2) with a mix of SN1-type molecular mechanism. Based on our structural analysis, a magnesium-assisted SN2-type mechanism is involved in the reverse reaction. Structure-function analysis, overview
additional information
modeling of the model of the enzyme, substrate and magnesium cation co-factor complex and structure-function relationship analysis, X-ray crystallographic and NMR structure analysis, overview. In silico modeling of protein-ligand interaction by molecular docking via simulations of molecular dynamic, modeling of the APRT-PRPP-Mg2+ enzyme complex, homology modeling using the APRT structure from Homo sapiens (PDB code 1ZN7)
additional information
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modeling of the model of the enzyme, substrate and magnesium cation co-factor complex and structure-function relationship analysis, X-ray crystallographic and NMR structure analysis, overview. In silico modeling of protein-ligand interaction by molecular docking via simulations of molecular dynamic, modeling of the APRT-PRPP-Mg2+ enzyme complex, homology modeling using the APRT structure from Homo sapiens (PDB code 1ZN7)
additional information
structure analysis and comparisons, detailed overview
additional information
the base-binding loop is stabilized by a cluster of aromatic and conformation-restricting proline residues, and (b) an N-H-N hydrogen bond between the base-binding loop and the N1 atom of adenine is the key interaction that differentiates adenine from 6-oxopurines. The residues conferring rigidity to the base-binding loop are highly conserved. Comparison of structure and sequences of APRTs from the Trypanosomatidae family with a destabilizing insertion on the base-binding loop and propose the mechanism by which these evolutionarily divergent enzymes achieve base specificity. The base-binding loop not only confers appropriate affinity but also provides defined specificity for adenine. FtAPRT structure is divided into (a) the base-binding domain, (b) the core PRPP binding domain and (c) a flexible catalytic loop, which is proposed to sequester the active site from the solvent at the time of catalysis. Enzyme residue F23 is a key residue that stacks with the F16-P17 cis-peptide pair and stabilizes the base-binding loop. This residue also plays an important role by stacking against the substrate adenine
additional information
the hydroxyl group in conserved tyrosine 105 controls the protein dynamics and the catalytic efficiencies of the forward and reverse reactions. Determination of the key residues of the reaction and the catalytic flexible loop dynamics. Tyr105 is essential for cell growth by facilitating the forward reaction. The active site of APRT consists of a 13-amino-acid-long PRPP-binding motif, starting from Val123 in hAPRT, with a conserved A131TGGS/T core sequence which serves to anchor the 5'-monophosphate group of either PRPP or ribonucleotides. It also contains two adjacent aspartates (Asp127 and Asp128 in hAPRT), two arginines (Arg67 and Arg87), and a specific cis-peptide bond, between Asp65 and Ser66, which hold together the 2'- and 3'-OH of the ribose and the diphosphate moiety of PRPP. Analysis of the role of hAPRT flexible loop
additional information
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the hydroxyl group in conserved tyrosine 105 controls the protein dynamics and the catalytic efficiencies of the forward and reverse reactions. Determination of the key residues of the reaction and the catalytic flexible loop dynamics. Tyr105 is essential for cell growth by facilitating the forward reaction. The active site of APRT consists of a 13-amino-acid-long PRPP-binding motif, starting from Val123 in hAPRT, with a conserved A131TGGS/T core sequence which serves to anchor the 5'-monophosphate group of either PRPP or ribonucleotides. It also contains two adjacent aspartates (Asp127 and Asp128 in hAPRT), two arginines (Arg67 and Arg87), and a specific cis-peptide bond, between Asp65 and Ser66, which hold together the 2'- and 3'-OH of the ribose and the diphosphate moiety of PRPP. Analysis of the role of hAPRT flexible loop
additional information
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Trypanosoma cruzi regulation is mainly posttranscriptional
additional information
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Trypanosoma cruzi regulation is mainly posttranscriptional
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additional information
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the base-binding loop is stabilized by a cluster of aromatic and conformation-restricting proline residues, and (b) an N-H-N hydrogen bond between the base-binding loop and the N1 atom of adenine is the key interaction that differentiates adenine from 6-oxopurines. The residues conferring rigidity to the base-binding loop are highly conserved. Comparison of structure and sequences of APRTs from the Trypanosomatidae family with a destabilizing insertion on the base-binding loop and propose the mechanism by which these evolutionarily divergent enzymes achieve base specificity. The base-binding loop not only confers appropriate affinity but also provides defined specificity for adenine. FtAPRT structure is divided into (a) the base-binding domain, (b) the core PRPP binding domain and (c) a flexible catalytic loop, which is proposed to sequester the active site from the solvent at the time of catalysis. Enzyme residue F23 is a key residue that stacks with the F16-P17 cis-peptide pair and stabilizes the base-binding loop. This residue also plays an important role by stacking against the substrate adenine
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additional information
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modeling of the model of the enzyme, substrate and magnesium cation co-factor complex and structure-function relationship analysis, X-ray crystallographic and NMR structure analysis, overview. In silico modeling of protein-ligand interaction by molecular docking via simulations of molecular dynamic, modeling of the APRT-PRPP-Mg2+ enzyme complex, homology modeling using the APRT structure from Homo sapiens (PDB code 1ZN7)
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additional information
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structure analysis and comparisons, detailed overview
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additional information
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Trypanosoma cruzi regulation is mainly posttranscriptional
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additional information
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Trypanosoma cruzi regulation is mainly posttranscriptional
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additional information
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modeling of the model of the enzyme, substrate and magnesium cation co-factor complex and structure-function relationship analysis, X-ray crystallographic and NMR structure analysis, overview. In silico modeling of protein-ligand interaction by molecular docking via simulations of molecular dynamic, modeling of the APRT-PRPP-Mg2+ enzyme complex, homology modeling using the APRT structure from Homo sapiens (PDB code 1ZN7)
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additional information
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structure analysis and comparisons, detailed overview
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purified recombinant enzyme in apoform and in complex with substrate adenine, sitting drop vapor diffusion method, mixing of 10 mg/ml protein in 20 mM HEPES, pH 7.5, 150 mM NaCl, 1 mM DTT, and 10% glycerol, with crystallization solutions (a) 0.1 M Tris/HCl pH 8.5, 30% PEG 4000 and 0.2 M MgCl2 and (b) 0.2 M sodium acetate trihydrate, 0.1 M Tris-HCl, pH 8.5, 30% PEG 4000, X-ray diffraction structure determination and analysis at 1.9-2.28 A resolution
enzyme, 10 mg/ml, in complex with 9-deazaadenine and sulfate or Mg-phosphoribosyldiphosphate, 50 mM Hepes, pH 6.0, 8 mM MgCl2, 1 mM DTT, 1:2 molar ratio of 9-deazaadenine and iminoribitol, 1 mM sodium diphosphate, after 45 min incubation preparation of crystallization drops, crystals are obtained from mother liquid 0.1 M sodium acetate, pH 4.6, 24% polyethylene glycol 4000, 0.2 M ammonium sulfate, 0.05 M urea, 18°C, X-ray diffraction structure analysis, hydrogen bond network in the complexes
comparison of the crystal structure of PRPP-Mg2+-bound hAPRT to the ADE/PRPP-Mg2+ and AMP complex structures
enzyme complexes phosphate-hAPRT, hypoxanthine-PRPP-Mg2+-hAPRT, IMP-hAPRT, and GMP-hAPRT, mixing of 400 nl of 5 mg/ml protein complexes in 20 mM Tris-HCl, pH 7.4, 5 mM MgCl2, with 200 nl of crystallization solution made of 85 mM Tris-HCl, pH 8.5, 170 mM NaOAc, 19-21% PEG 4000, and 0-30% glycerol, overnight at 20°C, X-ray diffraction structrue determination and analysis at resolution 1.55-1.90 A, molecular replacement using the structure with PDB ID 6FCH as template, and modeling
hanging drop vapour diffusion method, with 15% (v/v) glycerol, 25.5% (w/v) PEG 4000, 0.17 M sodium acetate, and 0.085 M Tris-HCl, pH 8.5
recombinant human APRT is crystallized in complex with adenosine 5'-monophosphate, hanging-drop vapour-diffusion method
vapour diffusion method, hanging drops from solution: 10 mg/ml purified apo-enzyme in 10 mM MES, pH 6.0, 1 mM dithiothreitol, 5 mM MgCl2, 4°C, reservoir solution: 7-11% polyethylene glycol 5000 monomethyl ether, 0.2 M ammonium acetate, 0.1 M sodium citrate, pH 4.9, 10 mM MgCl2, 1.2-1.6 M ammonium sulfate, for AMP- or adenine-bound crystals addition of 10 mM AMP or 5 mM adenine in the reservoir solution, structure analysis
enzyme in complex with adenosine-5'-monophosphate and a phosphate ion, crystallization at 4°C by hanging-drop vapor-diffusion method
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four crystal structures: (1) a structure (the enzyme/Pi complex) refined at 2.4 A with inorganic phosphate or sulfate bound in the 5-phosphoribosyl binding pocket, (2) an adenine bound structure (the enzyme/adenine complex) refined at 2.4 A, which shows adenine together with phosphates both at the 5'-phosphoryl and PPi positions of the presumed PRPP binding site, (3) an AMP bound structure (the enzyme/AMP complex) refined at 2.4 A, and (4) an ADP bound structure (the enzyme/ADP complex), refined at 2.8 A containing the inhibitor ADP bound like AMP with both the alpha- and beta-phosphates occupying the 5'-phosphoribosyl binding site. No crystals of the enzyme in complex with 5-phosphoribosyl-alpha-1-pyrophosphate are obtained, likely because the enzyme catalyzes a slow breakdown of 5-phosphoribosyl-alpha-1-pyrophosphate to ribose 5-phosphate and PPi. The crystal structure suggests that the enzyme evolves from a 6-oxopurine phosphoribosyltransferase. The individual subunit adopts an overall structure that resembles a 6-oxopurine phosphoribosyltransferase (PRTase) more than known adenine phosphoribosyltransferases implying that adenine phosphoribosyltransferase functionality in Crenarchaeotae has its evolutionary origin in this family of 6-oxopurine phosphoribosyltransferases. The N-terminal two-thirds of the polypeptide chain folds as a traditional type I PRTase with a five-stranded beta-sheet surrounded by helices. The C-terminal third adopts an unusual three-helix bundle structure that together with the nucleobase-binding loop undergoes a conformational change upon binding of adenine and phosphate resulting in a slight contraction of the active site
mixing of protein solution 13-15 mg/ml with an equal volume of mother liquid 0.1 M Hepes, pH 7.5, 1.5 M lithium sulfate, then equilibration against mother liquid at 18°C, crystals appear after 3 days, X-ray diffraction structure analysis, also crystallization of the enzyme in presence of diphosphate, Mg2+ or inhibitor immucillin, which do not bind at the active site
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purified His-tagged recombinant enzyme in complex with inhibitors D-DIAB and L-DIAB, and also with adenine, X-ray diffraction structure determination and analysis of enzyme-inhibitor complexes at 1.78 A and 1.98 A resolution, respectively, modeling, structure comparisons
purified recombinant enzyme APRT2, hanging-drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 200 mM NaCl and 20 mM Tris-HCl, pH 8.0, with 0.001 ml of precipitant solution containing 19% PEG 20000 and 0.1 M sodium citrate, pH 6.0, 30-50 days, 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using the structure of TthAPRT1 from Thermus thermophilus HB8 (PDB ID 1VCH) as a template
purified recombinant enzyme, crystals grow via capillary counter-diffusion technique, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement amd modeling
purified recombinant enzyme, hanging drop vapor diffusion technique, mixing of 12.5 mg/ml protein in 0.02 M Tris-HCl buffer, pH 8.0, 50 mM NaCl, 5% glycerol, 0.04% NaN3, and 5 mM AMP, with reservoir solution composed of 25% w/v PEG 3350, 0.1 M HEPES, pH 7.0, 0.5 M NaCl, and 0.04% NaN3, X-ray diffraction structure determination and analysis at 2.60 A resolution
purified recombinant native and selenomethionine-labeled enzymes, sitting drop vapour diffusion method, 0.001 ml of 20 mg/ml native protein in 20 mM Tris-HCl, 50 mM NaCl, pH 8.0, is mixed with an equal volume of reservoir solution containing 100 mM MES, pH 5.5, 100 mM calcium acetate, 3% w/v PEG 10000, and 3% v/v MeOH, 1 week, for the selenomethionine-labeled protein 40 mM calcium acetate, 1.5% w/v PEG 10000, and 3% v/v MeOH is used at a protein concentration of 29.4 mg/ml, X-ray diffraction structure determination and analysis at 1.9-2.6 A resolution, multiple wavelength anomalous dispersion method, asymmetric unit of two pairs of identical dimers, each related by noncrystallographic two-fold symmetry, a fifth monomer forms a similar dimer across a crystallographic two-fold axis, modeling
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G168E
the mutant of isoform APT1 shows reduced activity with zeatin (about 14%) and adenine (about 28%), respectively, compared to the wild type enzyme
G195D
the mutant of isoform APT1 shows nearly no activity with zeatin and adenine, respectively, compared to the wild type enzyme
G196R
the mutant of isoform APT1 shows nearly no activity with zeatin and adenine, respectively, compared to the wild type enzyme
L96F
the mutant of isoform APT1 shows reduced activity with zeatin (about 11%) and adenine (about 8%), respectively, compared to the wild type enzyme
P85T
the mutant of isoform APT1 shows nearly no activity with zeatin and adenine, respectively, compared to the wild type enzyme
R149K
the mutant of isoform APT1 shows no activity with zeatin and adenine, respectively, compared to the wild type enzyme
F25W
site-directed mutagenesis, tryptophan at the adenine binding site, kinetic constants similar to the wild-type
E104L
site-directed mutagenesis, the mutation decreases the catalytic efficiency of the enzyme in the forward reaction
G133D
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mutation in adenine phosphoribosyltransferase gene in patients with 2,8-dihydroxyadenine urolithiasis, Japanese patient
L110P
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mutation is associated with renal dysfunction
M136T
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10.3% loss of activity
R67Q
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mutation in adenine phosphoribosyltransferase gene in patients with 2,8-dihydroxyadenine urolithiasis, Japanese patient
V84W
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mutation in adenine phosphoribosyltransferase gene in patients with 2,8-dihydroxyadenine urolithiasis, Japanese patient
Y105F
site-directed mutagenesis, the mutation increases the inhibitory effect of AMP while decreasing the catalytic efficiency of the enzyme in the forward reaction
E106Q
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site-directed mutagenesis, decreased turnover and Km value for 5-phosphoribose 1-phosphate compared to the wild-type
G108A
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site-directed mutagenesis, increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
G108H
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site-directed mutagenesis, decreased turnover, slightly increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
K90A
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site-directed mutagenesis, decreased turnover compared to the wild-type
K93A
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site-directed mutagenesis, decreased turnover, increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
R69A
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site-directed mutagenesis, decreased turnover, increased Km value for adenine compared to the wild-type
R89A
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site-directed mutagenesis, decreased turnover, increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
Y103F
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site-directed mutagenesis, increased turnover, increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
Y107D
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site-directed mutagenesis, decreased turnover, increased Km value for adenine compared to the wild-type
Y107F
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site-directed mutagenesis, decreased turnover, increased Km value for adenine and 5-phosphoribose 1-phosphate compared to the wild-type
E106L
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site-directed mutagenesis, the mutant shows highly reduced kcat compared to wild-type
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F23A
site-directed mutagenesis, the mutation on the base-binding loop severely affects the activity and efficiency of the enzyme, the mutant enzyme is about 200fold less active as compared with wild-type
F23A
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site-directed mutagenesis, the mutation on the base-binding loop severely affects the activity and efficiency of the enzyme, the mutant enzyme is about 200fold less active as compared with wild-type
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D99N
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mutant enzyme has very low activity
D99N
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mutant enzyme has very low activity
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E106L
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site-directed mutagenesis, decreased turnover, increased Km value for adenine and decreased Km value for 5-phosphoribose 1-phosphate compared to the wild-type
E106L
site-directed mutagenesis, the mutant shows highly reduced kcat compared to wild-type
additional information
antisense expression of the enzyme for opression of the APT2 gene in Arabidopsis thaliana leads to lower AMP content, lower pollen germination rates, and some abnormalities in leaf phenotypes and flowering timing in the transgenic plants, overview
additional information
alignment of amino acid sequences, correlation between human clinical missense mutations and structure, structure taken from Leishmania donovani enzyme
additional information
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alignment of amino acid sequences, correlation between human clinical missense mutations and structure, structure taken from Leishmania donovani enzyme
additional information
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determination and phenotype analysis of a naturally occuring mutation in the APRT gene by a homozygous 254 bp deletion-8 bp insertion mutation in exon 3, the patients shows sever renal failure, with pathological presence of adenine in both biological fluids, urinary stone excretion, and no enzyme activityin the hemolysate, overview
additional information
determination and phenotype analysis of a naturally occuring mutation in the APRT gene by a homozygous 254 bp deletion-8 bp insertion mutation in exon 3, the patients shows sever renal failure, with pathological presence of adenine in both biological fluids, urinary stone excretion, and no enzyme activityin the hemolysate, overview
additional information
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heterozygotes for the 254 bp deletion-8 bp insertion of the APRT gene show a 69% lower APRT enzymatic activity
additional information
heterozygotes for the 254 bp deletion-8 bp insertion of the APRT gene show a 69% lower APRT enzymatic activity
additional information
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a naturally occuring mutation T596G leading to amino acid exchange F199C in hypoxanthine guanine phosphoribosyltransferase, HPRT, EC 2.4.2.8, with 92% reduced activity and a severe gouty arthritis phenotype, while the mutation or HPRT deficiency typically lead to a 2-3fold increased APRT activity in erythrocytes. Modeling of the mutated protein for prediction of the mechanisms of partial enzymatic activity
additional information
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identification of three cases of APRT*Q0 /APRT*J compound heterozygote-type APRT deficiency, genotyping, overview
additional information
Saccharomyces cerevisiae strain DS1-2b expressing the Tyr105Phe variant of hAPRT displays a reduced growth rate in absence of exogenous adenine, similar to the Glu104Leu variant, compared with the wild-type
additional information
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Saccharomyces cerevisiae strain DS1-2b expressing the Tyr105Phe variant of hAPRT displays a reduced growth rate in absence of exogenous adenine, similar to the Glu104Leu variant, compared with the wild-type
additional information
alignment of amino acid sequences, correlation between human clinical missense mutations and structure, structure taken from Leishmania donovani enzyme
additional information
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alignment of amino acid sequences, correlation between human clinical missense mutations and structure, structure taken from Leishmania donovani enzyme
additional information
construction of an aprth knockout strain (Tt27DELTAAPRTh) and an aprth-overexpressing strain (Tt27NStHisAPRTh) of Thermus thermophilus in minimal medium. The Tt27DELTAAPRTh strain exhibits delayed growth and requires approximately 36 h to reach the early stationary phase, whereas the wild-type strain reached this phase after 21 h of cultivation. The Tt27NStHisAPRTh strain exhibits better growth than even the wild-type strain
additional information
construction of an aprth knockout strain (Tt27DELTAAPRTh) and an aprth-overexpressing strain (Tt27NStHisAPRTh) of Thermus thermophilus in minimal medium. The Tt27DELTAAPRTh strain exhibits delayed growth and requires approximately 36 h to reach the early stationary phase, whereas the wild-type strain reached this phase after 21 h of cultivation. The Tt27NStHisAPRTh strain exhibits better growth than even the wild-type strain
additional information
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construction of an aprth knockout strain (Tt27DELTAAPRTh) and an aprth-overexpressing strain (Tt27NStHisAPRTh) of Thermus thermophilus in minimal medium. The Tt27DELTAAPRTh strain exhibits delayed growth and requires approximately 36 h to reach the early stationary phase, whereas the wild-type strain reached this phase after 21 h of cultivation. The Tt27NStHisAPRTh strain exhibits better growth than even the wild-type strain
additional information
covalent immobilization of TtAPRT2 through surface exposed Lys residues promotes a multipoint covalent attachment which leads to higher degree of rigidification, thereby increasing the thermal stability of the protein. Dimeric TtAPRT2 is immobilized onto glutaraldehyde-activated magnetic iron oxide porous microparticles by two different strategies: (a) an enzyme immobilization at pH 8.5 to encourage the immobilization process by N-termini (MTtAPRT2A, MTtAPRT2B, MTtAPRT2C) or (b) an enzyme immobilization at pH 10.0 to encourage the immobilization process through surface exposed lysine residues (MTtAPRT2D, MTtAPRT2E, MTtAPRT2F). According to catalyst load experiments, MTtAPRT2B (activity: 480 IU/g biocatalyst, activity recovery 52%) and MTtAPRT2F (activity 507 IU/g biocatalyst, activity recovery 44%) are chosen as optimal derivatives. The potential reusability of MTtAPRT2B and MTtAPRT2F is also tested. Finally, MTtAPRT2F is employed in the synthesis of nucleoside-5'-monophosphate analogues. 0.025 ml of the bead suspension (0.020 mg/ml) are washed and equilibrated in corresponding binding buffer containing 50 mM potassium phosphate buffer, pH 8.5, 50 mM sodium borate buffer, pH 10.0, or 50 mM sodium borate buffer, pH 10.6, during 4 h at 25°C
additional information
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covalent immobilization of TtAPRT2 through surface exposed Lys residues promotes a multipoint covalent attachment which leads to higher degree of rigidification, thereby increasing the thermal stability of the protein. Dimeric TtAPRT2 is immobilized onto glutaraldehyde-activated magnetic iron oxide porous microparticles by two different strategies: (a) an enzyme immobilization at pH 8.5 to encourage the immobilization process by N-termini (MTtAPRT2A, MTtAPRT2B, MTtAPRT2C) or (b) an enzyme immobilization at pH 10.0 to encourage the immobilization process through surface exposed lysine residues (MTtAPRT2D, MTtAPRT2E, MTtAPRT2F). According to catalyst load experiments, MTtAPRT2B (activity: 480 IU/g biocatalyst, activity recovery 52%) and MTtAPRT2F (activity 507 IU/g biocatalyst, activity recovery 44%) are chosen as optimal derivatives. The potential reusability of MTtAPRT2B and MTtAPRT2F is also tested. Finally, MTtAPRT2F is employed in the synthesis of nucleoside-5'-monophosphate analogues. 0.025 ml of the bead suspension (0.020 mg/ml) are washed and equilibrated in corresponding binding buffer containing 50 mM potassium phosphate buffer, pH 8.5, 50 mM sodium borate buffer, pH 10.0, or 50 mM sodium borate buffer, pH 10.6, during 4 h at 25°C
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additional information
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construction of an aprth knockout strain (Tt27DELTAAPRTh) and an aprth-overexpressing strain (Tt27NStHisAPRTh) of Thermus thermophilus in minimal medium. The Tt27DELTAAPRTh strain exhibits delayed growth and requires approximately 36 h to reach the early stationary phase, whereas the wild-type strain reached this phase after 21 h of cultivation. The Tt27NStHisAPRTh strain exhibits better growth than even the wild-type strain
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additional information
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covalent immobilization of TtAPRT2 through surface exposed Lys residues promotes a multipoint covalent attachment which leads to higher degree of rigidification, thereby increasing the thermal stability of the protein. Dimeric TtAPRT2 is immobilized onto glutaraldehyde-activated magnetic iron oxide porous microparticles by two different strategies: (a) an enzyme immobilization at pH 8.5 to encourage the immobilization process by N-termini (MTtAPRT2A, MTtAPRT2B, MTtAPRT2C) or (b) an enzyme immobilization at pH 10.0 to encourage the immobilization process through surface exposed lysine residues (MTtAPRT2D, MTtAPRT2E, MTtAPRT2F). According to catalyst load experiments, MTtAPRT2B (activity: 480 IU/g biocatalyst, activity recovery 52%) and MTtAPRT2F (activity 507 IU/g biocatalyst, activity recovery 44%) are chosen as optimal derivatives. The potential reusability of MTtAPRT2B and MTtAPRT2F is also tested. Finally, MTtAPRT2F is employed in the synthesis of nucleoside-5'-monophosphate analogues. 0.025 ml of the bead suspension (0.020 mg/ml) are washed and equilibrated in corresponding binding buffer containing 50 mM potassium phosphate buffer, pH 8.5, 50 mM sodium borate buffer, pH 10.0, or 50 mM sodium borate buffer, pH 10.6, during 4 h at 25°C
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additional information
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construction of an aprth knockout strain (Tt27DELTAAPRTh) and an aprth-overexpressing strain (Tt27NStHisAPRTh) of Thermus thermophilus in minimal medium. The Tt27DELTAAPRTh strain exhibits delayed growth and requires approximately 36 h to reach the early stationary phase, whereas the wild-type strain reached this phase after 21 h of cultivation. The Tt27NStHisAPRTh strain exhibits better growth than even the wild-type strain
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