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 25ưC
0.015
5-phospho-alpha-D-ribose 1-diphosphate
wild type long-form enzyme, at pH 8.5 and 25ưC
0.0184
5-phospho-alpha-D-ribose 1-diphosphate
-
25ưC, 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 25ưC
0.049
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 8.5, 25ưC
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
-
25ưC, 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
-
25ưC, 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 24ưC
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 10ưC
0.6
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 20ưC
0.7
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 25ưC
0.7
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 15ưC
0.8
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 30ưC
0.901
5-phospho-alpha-D-ribose 1-diphosphate
-
25ưC, pH 8, mutant enzyme T162A
0.94
5-phospho-alpha-D-ribose 1-diphosphate
-
25ưC, pH 8, mutant enzyme K50A
5.15
5-phospho-alpha-D-ribose 1-diphosphate
-
25ưC, pH 8, mutant enzyme T159A
37
5-phospho-alpha-D-ribose 1-diphosphate
crude cell extracts
0.097
ATP

at pH 8.5 and 25ưC
0.097
ATP
wild type long-form enzyme, at pH 8.5 and 25ưC
0.117
ATP
truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25ưC
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
0.263
ATP
-
pH 8.5, 25ưC
0.35
ATP
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.47
ATP
at pH 8.0 and 24ưC
0.51
ATP
crude cell extracts
0.6
ATP
recombinant enzyme
1.05
ATP
-
25ưC, pH 8, mutant enzyme T162A
1.07
ATP
-
25ưC, pH 8, mutant enzyme T159A
1.2
ATP
at pH 8.5 and 30ưC
1.7
ATP
at pH 8.5 and 25ưC
1.8
ATP
at pH 8.5 and 20ưC
2
ATP
at pH 8.5 and 15ưC
2.1
ATP
at pH 8.5 and 10ưC
2.7
ATP
-
25ưC, pH 8, wild-type enzyme
4.7
ATP
-
25ưC, pH 8, mutant enzyme D155A
5
ATP
-
25ưC, pH 8, mutant enzyme K50A
8.45
ATP
-
25ưC, 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
-
25ưC, 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 25ưC
0.45
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 10ưC
0.57
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.0 and 24ưC
0.64
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 15ưC
0.84
5-phospho-alpha-D-ribose 1-diphosphate
-
25ưC, pH 8, mutant enzyme T162A
0.94
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 30ưC
0.94
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 20ưC
1.07
5-phospho-alpha-D-ribose 1-diphosphate
-
25ưC, pH 8, mutant enzyme K8A
1.16
5-phospho-alpha-D-ribose 1-diphosphate
at pH 8.5 and 25ưC
1.2
5-phospho-alpha-D-ribose 1-diphosphate
-
25ưC, 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 25ưC
1.8
5-phospho-alpha-D-ribose 1-diphosphate
wild type long-form enzyme, at pH 8.5 and 25ưC
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
-
25ưC, pH 8, wild-type enzyme
2.83
5-phospho-alpha-D-ribose 1-diphosphate
-
25ưC, pH 8, mutant enzyme D155A
6.16
5-phospho-alpha-D-ribose 1-diphosphate
-
25ưC, pH 8, mutant enzyme K50A
0.024
ATP

truncated long-form enzyme devoid of its regulatory domain, at pH 8.5 and 25ưC
0.45
ATP
at pH 8.5 and 10ưC
0.57
ATP
at pH 8.0 and 24ưC
0.64
ATP
at pH 8.5 and 15ưC
0.94
ATP
at pH 8.5 and 30ưC
0.94
ATP
at pH 8.5 and 20ưC
1.16
ATP
at pH 8.5 and 25ưC
1.8
ATP
wild type long-form enzyme, at pH 8.5 and 25ưC
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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
-
25ưC, 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 25ưC
0.382
AMP
with respect to 5-phospho-alpha-D-ribose 1-diphosphate, at pH 8.5 and 25ưC
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 30ưC
0.004
L-histidine
-
uncompetitive versus ATP, pH 8.0, 25ưC
0.0079
L-histidine
-
uncompetitive versus ATP, pH 8.25, 25ưC
0.011
L-histidine
mutant enzyme A270D, at pH 8.5 and 30ưC
0.022
L-histidine
mutant enzyme S232Y, at pH 8.5 and 30ưC
0.0235
L-histidine
-
Kii-value, non competitive versus 5-phospho-alpha-D-ribosyl diphosphate, pH 8.5, 25ưC
0.0257
L-histidine
-
Kis-value, non competitive versus 5-phospho-alpha-D-ribosyl diphosphate, pH 8.5, 25ưC
0.0269
L-histidine
-
uncompetitive versus ATP, pH 8.75, 25ưC
0.0279
L-histidine
-
uncompetitive versus ATP, pH 8.5, 25ưC
0.04
L-histidine
with respect to 5-phospho-alpha-D-ribose 1-diphosphate, at pH 8.5 and 25ưC
0.044
L-histidine
mutant enzyme S143F, at pH 8.5 and 30ưC
0.044
L-histidine
with respect to ATP, at pH 8.5 and 25ưC
0.0504
L-histidine
-
uncompetitive versus ATP, pH 9.0, 25ưC
0.1094
L-histidine
-
uncompetitive versus ATP, pH 9.25, 25ưC
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 30ưC
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 16ưC, 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
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