Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
additional information
?
-
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first step in histidine biosynthesis, enzyme is regulated in a complex allosterical manner, it is a key enzyme is control of the metabolic flux through the pathway
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first step in histidine biosynthesis
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first reaction of histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first step in histidine biosynthesis, mechanism of regulation, overview
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
additional information
?
-
-
the enzyme comprises 4 catalytic subunits HisGs and 4 regulatory subunits HisZ with histidine as a ligand, 8 histidine binding sites at the subunit interfaces
-
-
?
additional information
?
-
-
not: ribose 5-phosphate, AMP, ADP, UTP, CTP, GTP
-
-
?
additional information
?
-
-
not: ribose 5-phosphate, AMP, ADP, UTP, CTP, GTP
-
-
?
additional information
?
-
-
not: ribose 5-phosphate, AMP, ADP, UTP, CTP, GTP
-
-
?
additional information
?
-
-
the enzyme comprises 4 catalytic subunits HisGs and 4 regulatory subunits HisZ, only the complete hetero-octameric complex is catalytically active, the complex possesses 8 histidine binding sites at the subunit interfaces and histidine as a ligand
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
?
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first step in histidine biosynthesis, enzyme is regulated in a complex allosterical manner, it is a key enzyme is control of the metabolic flux through the pathway
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first step in histidine biosynthesis
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first reaction of histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first enzyme in histidine biosynthetic pathway. ATP-PRT expression plays a major role in regulating the pool of free His and contributes to the exceptional Ni tolerance of hyperaccumulator Alyssum species
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
-
first step in histidine biosynthesis, mechanism of regulation, overview
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
-
first step in histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
-
-
-
r
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
N1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
-
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(4E)-4-[(4-chlorophenyl)(hydroxy)methylidene]-1-(pyridin-3-ylmethyl)-5-(3,4,5-trimethoxyphenyl)pyrrolidine-2,3-dione
binds to the cavity between the domains I and II. The terminal chlorobenzoyl group of 1 makes hydrophobic interactions with the amphiphilic pocket near the phosphoribosyl pyrophosphate binding site
1,2,4-Triazole-3-alanine
-
1-(5-phospho-alpha-D-ribosyl)-ATP
-
product inhibition, competitive to both substrates
1-(5-phospho-beta-D-ribosyl)-ATP
product inhibition
1-[(5,6-diphenyl-1,2,4-triazin-3-yl)sulfanyl]-3-(1,3-thiazol-2-yl)propan-2-one
most potent inhibitor, spans the PR-ATP binding site, exhibits greater than 50% inhibition at 0.01 mM, 40% inhibition at 0.001 mM
2-([7-[(3-hydroxyphenyl)amino]-4-nitro-2,1,3-benzoxadiazol-5-yl]amino)-5-nitrophenol
2-[(2-bromo-3,5-dinitrophenyl)carbonyl]-N-phenylhydrazinecarboxamide
4-methoxybenzyl 2-methyl-5-oxo-4,7-dithiophen-2-yl-1,4,5,6,7,8-hexahydroquinoline-3-carboxylate
interacts with the phosphoribosyl diphosphate binding site but less strongly compared to compound 6 , exhibits greater than 50% inhibition at 0.01 mM
5-phospho-alpha-D-ribose 1-diphosphate
-
noncompetitive inhibitor with respect to both substrates in the reaction producing ATP and 5-phospho-alpha-D-ribose 1-diphosphate
adenine
-
competitive to ATP and 5-phospho-alpha-D-ribose 1-diphosphate
ATP
-
inhibits the reaction at high concentrations
beta,gamma-methylene-ATP
-
competitive with respect to N-1-(5-phosphoribosyl)-ATP, noncompetitive with respect to diphosphate; inhibitor of the reaction producing ATP and 5-phospho-alpha-D-ribose 1-diphosphate
beta-(2-thiazolyl)-DL-alanine
-
Ca2+
moderate inhibitory effect
dicoumarol
-
competitive with respect to ATP, inhibitor in both directions, diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
dinitrophenol
-
diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
diphosphate
-
non competitive to both substrates
ethyl [(6-nitro-1,3-benzothiazol-2-yl)amino](oxo)acetate
exhibits 39% inhibition
Guanosine 5'-diphosphate-3'-diphosphate
-
in presence of partially inhibiting concentrations of histidine guanosine 5'-diphosphate-3'-diphosphate becomes a potent inhibitor of the residual activity of ATP phosphoribosyltransferase, no inhibition in absence of histidine, inhibition is slowly reversible
Methylmercuric bromide
-
-
Mg2+
-
at high concentrations, Ki = 23 mM
Mn2+
moderate inhibitory effect
N-[3-[(6-nitro-1,3-benzothiazol-2-yl)amino]-3-oxo-1-phenylpropyl]benzamide
occupies only the phosphoribosyl diphosphate binding site, exhibits greater than 50% inhibition at 0.01 mM, 35% inhibition at 0.001 mM
p-hydroxymercuribenzoate
-
-
Pentachlorophenol
-
competitive to ATP, inhibitor in both directions, diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
additional information
-
carbonylcyanide m-chlorophenylhydrazone, which is a potent inhibitor of several enzymes with adenine-containing substrates or coenzymes has no effect
-
2-([7-[(3-hydroxyphenyl)amino]-4-nitro-2,1,3-benzoxadiazol-5-yl]amino)-5-nitrophenol
exhibits 46% inhibition
2-([7-[(3-hydroxyphenyl)amino]-4-nitro-2,1,3-benzoxadiazol-5-yl]amino)-5-nitrophenol
-
has whole-cell activity at 0.012 mM
2-[(2-bromo-3,5-dinitrophenyl)carbonyl]-N-phenylhydrazinecarboxamide
exhibits 71% inhibition
2-[(2-bromo-3,5-dinitrophenyl)carbonyl]-N-phenylhydrazinecarboxamide
-
has whole-cell activity at 0.025 mM
ADP
competitive to ATP
ADP
orthosteric inhibition
ADP
-
competitive to ATP, in the presence of histidine inhibition by AMP and ADP becomes positively cooperative and much more potent
Ag+
-
AMP
competitive inhibition
AMP
competitive inhibition
AMP
about 10% inhibition at 0.25 mM
AMP
-
linear competitive inhibitor with respect to ATP, stabilizes the enzyme to thermal inactivation, protect the ordered enzymatic structure against thermodenaturation
AMP
binding structure and inhibition mode
AMP
-
inhibits the enzyme complex together with histidine to the T-state
AMP
competitive inhibition
AMP
AMP is an inhibitor of subunit HisGS
AMP
-
competitive inhibitor to 5-phospho-alpha-D-ribose 1-diphosphate, in the presence of histidine inhibition by AMP and ADP becomes positively cooperative and much more potent
Cu2+
-
EDTA
moderate inhibitory effect
Hg2+
moderate inhibitory effect
histidine
-
feedback inhibition, inhibits the enzyme complex together with ATP to the T-state, no inhibition of mutants E130A and Y268F/Y269F
histidine
-
noncompetitive
histidine
-
noncompetitive feedback inhibition
L-histidine
feed-back inhibition; feed-back inhibition
L-histidine
allosterical inhibition
L-histidine
allosterical inhibition
L-histidine
complete inhibition at 1 mM, about 10% inhibition at 0.25 mM
L-histidine
-
feed-back inhibition
L-histidine
noncompetitive, alkaline pH decreases the inhibitory effect
L-histidine
-
feed-back inhibition; stabilizes the enzyme to thermal inactivation, protects the ordered enzymatic structure against thermodenaturation, no interaction with binding sites
L-histidine
-
feed-back inhibition
L-histidine
-
feed-back inhibition; stabilizes the enzyme to thermal inactivation, protects the ordered enzymatic structure against thermodenaturation, no interaction with binding sites
L-histidine
-
feed-back inhibition
L-histidine
complete inhibition at 0.1 mM
L-histidine
-
allosteric inhibition, synergistically favored by AMP; feed-back inhibition
L-histidine
-
allosteric inhibitor, inhibition dependent on pH, uncompetitive versus ATP, noncompetitive versus 5-phospho-alpha-D-ribosyl diphosphate
L-histidine
in the presence of histidine, subunit HisZ mediates allosteric inhibition of the enzyme
L-histidine
-
feed-back inhibition; reversed by Hg2+, p-hydroxymercuribenzoate, methylmercuric bromide, Ni2+; the L-configuration is essential, substitution of alpha-amino group appreciably reduces inhibition, non competitive inhibitor with respect to both substrates
L-histidine
-
feed-back inhibition
L-histidine
-
feed-back inhibition; inhibits reverse reaction cooperatively and completely
Zn2+
moderate inhibitory effect
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0.015 - 37
5-phospho-alpha-D-ribose 1-diphosphate
additional information
additional information
-
steady-state kinetics
-
0.015
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 25°C
0.015
5-phospho-alpha-D-ribose 1-diphosphate
wild type long-form enzyme, at pH 8.5 and 25°C
0.0184
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, wild-type enzyme
0.028
5-phospho-alpha-D-ribose 1-diphosphate
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
0.049
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 8.5, 25°C
0.067
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.07
5-phospho-alpha-D-ribose 1-diphosphate
A270P mutant protein, pH 8.5, temperature not specified in the publication
0.0712
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme D155A
0.08
5-phospho-alpha-D-ribose 1-diphosphate
N215K mutant protein, pH 8.5, temperature not specified in the publication
0.08
5-phospho-alpha-D-ribose 1-diphosphate
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.08
5-phospho-alpha-D-ribose 1-diphosphate
wild type protein, pH 8.5, temperature not specified in the publication
0.09
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme K8A
0.09
5-phospho-alpha-D-ribose 1-diphosphate
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.13
5-phospho-alpha-D-ribose 1-diphosphate
recombinant At-ATP-PRT1
0.182
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.0 and 24°C
0.57
5-phospho-alpha-D-ribose 1-diphosphate
crude cell extracts
0.6
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 10°C
0.6
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 20°C
0.7
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 25°C
0.7
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 15°C
0.8
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 30°C
0.901
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme T162A
0.94
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme K50A
5.15
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme T159A
37
5-phospho-alpha-D-ribose 1-diphosphate
crude cell extracts
0.097
ATP
at pH 8.5 and 25°C
0.097
ATP
wild type long-form enzyme, at pH 8.5 and 25°C
0.117
ATP
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
0.22
ATP
N215K mutant protein, pH 8.5, temperature not specified in the publication
0.22
ATP
wild type protein, pH 8.5, temperature not specified in the publication
0.23
ATP
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.24
ATP
A270P mutant protein, pH 8.5, temperature not specified in the publication
0.35
ATP
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.47
ATP
at pH 8.0 and 24°C
0.51
ATP
crude cell extracts
0.6
ATP
recombinant enzyme
1.05
ATP
-
25°C, pH 8, mutant enzyme T162A
1.07
ATP
-
25°C, pH 8, mutant enzyme T159A
1.2
ATP
at pH 8.5 and 30°C
1.7
ATP
at pH 8.5 and 25°C
1.8
ATP
at pH 8.5 and 20°C
2.1
ATP
at pH 8.5 and 10°C
2.7
ATP
-
25°C, pH 8, wild-type enzyme
4.7
ATP
-
25°C, pH 8, mutant enzyme D155A
5
ATP
-
25°C, pH 8, mutant enzyme K50A
8.45
ATP
-
25°C, pH 8, mutant enzyme K8A
89
ATP
crude cell extracts
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0.024 - 6.16
5-phospho-alpha-D-ribose 1-diphosphate
additional information
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme K50A
0.024
5-phospho-alpha-D-ribose 1-diphosphate
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
0.45
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 10°C
0.57
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.0 and 24°C
0.64
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 15°C
0.84
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme T162A
0.94
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 30°C
0.94
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 20°C
1.07
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme K8A
1.16
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 25°C
1.2
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme T159A
1.29
5-phospho-alpha-D-ribose 1-diphosphate
A270P mutant protein, pH 8.5, temperature not specified in the publication
1.36
5-phospho-alpha-D-ribose 1-diphosphate
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
1.75
5-phospho-alpha-D-ribose 1-diphosphate
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
1.8
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 25°C
1.8
5-phospho-alpha-D-ribose 1-diphosphate
wild type long-form enzyme, at pH 8.5 and 25°C
1.91
5-phospho-alpha-D-ribose 1-diphosphate
wild type protein, pH 8.5, temperature not specified in the publication
2.22
5-phospho-alpha-D-ribose 1-diphosphate
N215K mutant protein, pH 8.5, temperature not specified in the publication
2.7
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, wild-type enzyme
2.83
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme D155A
6.16
5-phospho-alpha-D-ribose 1-diphosphate
-
25°C, pH 8, mutant enzyme K50A
0.024
ATP
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25°C
0.45
ATP
at pH 8.5 and 10°C
0.57
ATP
at pH 8.0 and 24°C
0.64
ATP
at pH 8.5 and 15°C
0.94
ATP
at pH 8.5 and 30°C
0.94
ATP
at pH 8.5 and 20°C
1.16
ATP
at pH 8.5 and 25°C
1.8
ATP
wild type long-form enzyme, at pH 8.5 and 25°C
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0.002
1-[(5,6-diphenyl-1,2,4-triazin-3-yl)sulfanyl]-3-(1,3-thiazol-2-yl)propan-2-one
-
0.88
ADP
wild type protein, pH 8.5, temperature not specified in the publication
0.0811
histidine
-
25°C, pH 8
0.0005 - 4.15
L-histidine
0.002
N-[3-[(6-nitro-1,3-benzothiazol-2-yl)amino]-3-oxo-1-phenylpropyl]benzamide
-
0.356
AMP
with respect to ATP, at pH 8.5 and 25°C
0.382
AMP
with respect to 5-phospho-alpha-D-ribose 1-diphosphate, at pH 8.5 and 25°C
1.29
AMP
wild type protein, pH 8.5, temperature not specified in the publication
0.0005
L-histidine
wild type enzyme, at pH 8.5 and 30°C
0.004
L-histidine
-
uncompetitive versus ATP, pH 8.0, 25°C
0.0079
L-histidine
-
uncompetitive versus ATP, pH 8.25, 25°C
0.011
L-histidine
mutant enzyme A270D, at pH 8.5 and 30°C
0.022
L-histidine
mutant enzyme S232Y, at pH 8.5 and 30°C
0.0235
L-histidine
-
Kii-value, non competitive versus 5-phospho-alpha-D-ribosyl diphosphate, pH 8.5, 25°C
0.0257
L-histidine
-
Kis-value, non competitive versus 5-phospho-alpha-D-ribosyl diphosphate, pH 8.5, 25°C
0.0269
L-histidine
-
uncompetitive versus ATP, pH 8.75, 25°C
0.0279
L-histidine
-
uncompetitive versus ATP, pH 8.5, 25°C
0.04
L-histidine
with respect to 5-phospho-alpha-D-ribose 1-diphosphate, at pH 8.5 and 25°C
0.044
L-histidine
mutant enzyme S143F, at pH 8.5 and 30°C
0.044
L-histidine
with respect to ATP, at pH 8.5 and 25°C
0.0504
L-histidine
-
uncompetitive versus ATP, pH 9.0, 25°C
0.1094
L-histidine
-
uncompetitive versus ATP, pH 9.25, 25°C
0.11
L-histidine
wild type protein, pH 8.5, temperature not specified in the publication
0.178
L-histidine
mutant enzyme S232Y/A270D, at pH 8.5 and 30°C
0.24
L-histidine
A270P mutant protein, pH 8.5, temperature not specified in the publication
0.28
L-histidine
N215K mutant protein, pH 8.5, temperature not specified in the publication
0.52
L-histidine
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
4.15
L-histidine
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
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homodimer
2 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000
homohexamer or heterooctamer
heterooctamer
4 * 40000 + 4 * 23000, subunits HisZ and HisGS, SDS-PAGE
heterooctamer
short-form ATP phosphoribosyltransferase is a hetero-octameric allosteric enzyme comprising four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
heterooctamer
the enzyme consist of four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
heterooctamer
-
the enzyme consist of four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
-
heterooctamer
-
4 * 40000 + 4 * 23000, subunits HisZ and HisGS, SDS-PAGE
-
heterooctamer
-
short-form ATP phosphoribosyltransferase is a hetero-octameric allosteric enzyme comprising four catalytic subunits (HisGS) and four regulatory subunits (HisZ)
-
hexamer
-
hexamer
-
6 * 33367, dimers arranged in a hexamer, in the presence of AMP
hexamer
-
inactive form, in complex with histidine
hexamer
-
6 * 36000, viscometric methods, equilibrium centrifugation with meniscus depletion method after dialysis against 5.0 M guanidine-HCl and 0.143 M 2-mercaptoethanol
hexamer
-
6 * 33000, SDS-disc gel electrophoresis
homohexamer
long enzyme form
homohexamer
-
long enzyme form
-
homohexamer
6 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000
homohexamer
x-ray crystallography
homohexamer
-
6 * 31515.1, ESI-MS, gel filtration, His-tagged protein, not influenced by allosteric inhibitor L-histidine or ATP
homohexamer
-
6 * 31515.1, ESI-MS, gel filtration, His-tagged protein, not influenced by allosteric inhibitor L-histidine or ATP
-
homohexamer or heterooctamer
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
homohexamer or heterooctamer
-
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
-
homohexamer or heterooctamer
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
homohexamer or heterooctamer
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
homohexamer or heterooctamer
-
the long-form enzyme is a homohexamer with each chain comprised of the catalytic core, and a covalent C-terminal regulatory domain containing the allosteric binding site for histidine. The short-form is a hetero-octamer containing two catalytic dimers that associate with a second discrete domain (denoted HisZ) for allosteric regulation by the binding of histidine
-
octamer
-
4 * catalytic subunit HisGs + 4 * regulatory subunit HisZ, (alpha,beta)4
octamer
-
four HisGS catalytic subunits related to periplasmic binding proteins and four HisZ regulatory subunits that resemble histidyl-tRNA synthetases
octamer
-
4 * catalytic subunit HisGs + 4 * regulatory subunit HisZ, (alpha,beta)4
additional information
quarternary structure
additional information
-
quarternary structure
additional information
-
overall structure and monomer architecture, several motif 2 loops in both subunit types, switch structure between active and inactive conformation
additional information
-
subunit structures, structure evolution
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in complex with ATP, L-histidine, or L-histidine/AMP, hanging drop vapor diffusion method, using 0.1M sodium acetate, 0.1 M MgCl2, 13-15% (w/v) PEG 4000, pH 5.5 (ATP), or 0.1 M BTP, 0.2 M KSCN, 13-14% (w/v) PEG 3350, pH 6.5 (His), or 0.1 M Tris, 0.1 M MgCl2, 13-15% (w/v) PEG 4000, pH 7.5 (L-His/AMP)
truncated long-form enzyme devoid of its regulatory domain as apoenzyme and in complex with ATP, 5-phospho-alpha-D-ribose 1-diphosphate or 1-(5-phospho-beta-D-ribosyl)-ATP, hanging drop vapor diffusion method, using 1 M sodium acetate, 10 mM ZnCl2, and 7-10% (w/v) PEG 6000 (pH 5.0)
purified recombinant selenomethionine-labeled enzyme in complex with inhibitor AMP or with product 1-(5-phospho-D-ribosyl)-ATP, X-ray diffraction enzyme-inhibitor complex structure determination and analysis at 2.7 A resolution, X-ray diffraction enzyme-product complex structure determination and analysis at 2.9 A resolution, modeling
vapour diffusion method, trigonal prisms are obtained using 1.3 M sodium tartrate, 50-200 mM magnesium chloride, 100 mM citrate buffer pH 5.6 and enzyme in the presence of 2 mM AMP, round shaped crystals are obtained with 1.36-1.44 M ammonium sulfate, 0-0.3 M sodium chloride, 100 mM HEPES buffer pH 7.5 and enzyme in the presence of 2 mM AMP
-
purified recombinant wild-type and selenomethionine-labeled enzyme complex, the latter additionally by microseeding, hanging drop vapour diffusion method, 0.002 ml well solution containing 15-25% v/v PEG 400, 0.1 M Tris-HCl, pH 7.5, 0.2 M MgCl2, mixed with equal volume of protein solution containing 10-16 mg/ml protein, 10 mM ATP, or 10 mM N-1-methyl-ATP and 5 mM 5-phospho-alpha-D-ribose 1-diphosphate, crystal growth is dependent on ATP or N-1-methyl-ATP, derivatization with 2.5 mM sodium tungstate dihydrate, cryoprotection with 17-18% glycerol, X-ray diffraction structure determination and analysis at 2.9-3.2 A resolution
-
native and SeMet-labeled enzyme, hanging drop vapor diffusion method, using 2.53 M NaCl, 100 mM Bis-Tris propane pH 6.3, and 10% (v/v) glycerol
hanging drop vapor diffusion method
hanging drop vapour diffusion method at 16°C, the apocrystals are obtained using 0.1 M buffer MES pH 6.5 and magnesium sulfate as precipitant, crystals in the presence of AMP and histidine are obtained using 0.1 M sodium citrate pH 5.6, 0.5 M ammonium sulfate and 1 M lithium sulfate with 5 mM AMP and 0.1 mM histidine
-
HisG co-crystallized with compound 6, to 2.9 A resolution
hanging drop vapor diffusion method, using 11% (w/v) PEG 3350, 0.1 M bicine (pH 8.5), 0.15 M SrCl2, 0.15 M KBr, and 2% (v/v) 1,6-hexanediol
holoenzyme and catalytic subunit HisGS in complexes with substrates (5-phospho-alpha-D-ribose 1-diphosphate, 5-phospho-alpha-D-ribose 1-diphosphate-ATP, 5-phospho-alpha-D-ribose 1-diphosphate-ADP), product (N1-(5-phospho-beta-D-ribosyl)-ATP) and inhibitor (AMP), hanging drop vapor diffusion method, using 10% (w/v) polyethylene glycol 3350, 0.1 M bicine pH 8.5, 50 mM MgCl2, 0.1 M KBr, and 4% (v/v) 1,6-hexanediol
purified recombinant wild-type and selenomethionine-labeled subunits HisGs and HisZ separately, in a binary complex with histidine, sitting drop vapour diffusion method, 0.002 ml of 8 mg/ml protein mixed with 0.002 ml reservoir solution containing 22.5% w/v methyl-2,4-pentanediol, 0.2 M phosphate/citrate buffer, pH 4.2, 2 days, X-ray diffraction structure determination and analysis at 2.5 A resolution, modeling
-
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R216A
the mutant shows more than 50% inhibition at 0.25 mM AMP and complete loss of response to histidine while retaining its histidine-binding ability
R216Q
the mutant shows about 50% inhibition at 0.25 mM AMP, about 20% inhibition at 0.025 mM L-histidine, and about 45% inhibition at 0.25 mM ATP plus 0.025 mM L-histidine
R216A
-
the mutant shows more than 50% inhibition at 0.25 mM AMP and complete loss of response to histidine while retaining its histidine-binding ability
-
R216Q
-
the mutant shows about 50% inhibition at 0.25 mM AMP, about 20% inhibition at 0.025 mM L-histidine, and about 45% inhibition at 0.25 mM ATP plus 0.025 mM L-histidine
-
A249T
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
A270D
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
D213N
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
G230S
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
L231F/T235A
conserved residues
N215K/L231F/T235A
conserved residues, 37fold increase in Ki-value of histidine
N215K/L231F/T235A/A270P
conserved residues
S143F
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
S232Y
the mutant with increased activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
S232Y/A270D
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
T228P
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
T235M
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
D213N
-
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
G230S
-
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
S143F
-
the mutant with reduced activity is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
T235M
-
the mutant is more resistant towards inhibition by L-histidine compared to the wild type enzyme
-
D155A
-
slight increase in kcat, 3.9fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 1.7fold increase in Km-value for ATP
E130A
-
site-directed mutagenesis, about 60% reduced activity compared to the wild-type enzyme, no inhibition by histidine
K50A
-
2.3fold increase in kcat, 51fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 1.8fold increase in Km-value for ATP
K8A
-
2.5fold decrease in kcat, 4.9fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 3.1fold increase in Km-value for ATP
S140A
-
mutant is unstable, kinetic parameters can not be determined
T159A
-
2.2fold decrease in kcat, 280fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 2.5fold decrease in Km-value for ATP
T162A
-
3.2fold decrease in kcat, 49fold increase in KM-value for 5-phospho-alpha-D-ribose 1-diphosphate, 2.6fold decrease in Km-value for ATP
Y268F/Y269F
-
site-directed mutagenesis, about 30% reduced activity compared to the wild-type enzyme, no inhibition by histidine
additional information
deletion of the entire C-terminal regulatory domain in combination with the gain of function mutation S143F in the catalytic domain results in an enzyme variant that is still highly active even at L-histidine concentrations close to the solubility limit
additional information
-
deletion of the entire C-terminal regulatory domain in combination with the gain of function mutation S143F in the catalytic domain results in an enzyme variant that is still highly active even at L-histidine concentrations close to the solubility limit
additional information
-
deletion of the entire C-terminal regulatory domain in combination with the gain of function mutation S143F in the catalytic domain results in an enzyme variant that is still highly active even at L-histidine concentrations close to the solubility limit
-
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Martin, R.G.
The first enzyme in histidine biosynthesis: the nature of feedback inhibition by histidine
J. Biol. Chem.
238
257-268
1963
Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Tebar, A.R.; Ballesteros, A.O.
Kinetic properties of ATP phosphoribosyltransferase of Escherichia coli
Mol. Cell. Biochem.
11
131-136
1976
Escherichia coli
brenda
Ames, B.N.; Martin, R.G.; Garry, B.J.
The first step in histidine biosynthesis
J. Biol. Chem.
236
2019-2026
1961
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Campylobacter jejuni (Q5HSJ4), Campylobacter jejuni RM 1221 (Q5HSJ4)
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Medicago truncatula (G7JFL4), Medicago truncatula
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2017
Psychrobacter arcticus (Q4FQF7), Psychrobacter arcticus DSM 17307 (Q4FQF7)
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Psychrobacter arcticus (Q4FQF7), Psychrobacter arcticus DSM 17307 (Q4FQF7)
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Campylobacter jejuni (Q5HSJ4), Campylobacter jejuni RM1221 (Q5HSJ4)
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