Information on EC 2.4.2.17 - ATP phosphoribosyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.4.2.17
-
RECOMMENDED NAME
GeneOntology No.
ATP phosphoribosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
double displacement mechanism; sequential kinetic mechanism in biosynthetic direction, ordered bi-bi mechanism with ATP binding first to free enzyme and phosphoribosyl-ATP dissociating last from enzyme-product complexes
-
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
sequential kinetic mechanism in biosynthetic direction, ordered bi-bi mechanism with ATP binding first to free enzyme and phosphoribosyl-ATP dissociating last from enzyme-product complexes
-
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
substrate binding sites, active site structure, switch between active and inactive conformation
-
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
substrate binding sites, e.g. Cys104, Asn75, Ser154, Glu156, and Val155, reaction mechanism
P60757
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
histidine biosynthesis
-
Histidine metabolism
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
1-(5-phospho-D-ribosyl)-ATP:diphosphate phospho-alpha-D-ribosyl-transferase
Involved in histidine biosynthesis.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1-(5-phospho-D-ribosyl)-ATP:pyrophosphate phospho-alpha-D-ribosyltransferase
-
-
-
-
adenosine triphosphate phosphoribosyltransferase
-
-
-
-
ATP phosphoribosyl transferase
-
-
ATP phosphoribosyl transferase
-
-
ATP phosphoribosyl transferase
-
-
ATP phosphoribosyl transferase complex
-
-
ATP phosphoribosyltransferase
Q9Z472
-
ATP phosphoribosyltransferase
-
-
ATP-phosphoribosyltransferase
-
-
ATP-PRT
-
-
-
-
ATP-PRT
-
-
ATP-PRT1
Q56UT3
-
ATP-PRT1
Q56US5
-
ATP-PRT2
Q56UT2
-
ATP-PRTase
-
-
N-1-(5'-phosphoribosyl)-ATP transferase
-
-
phosphoribosyl ATP synthetase
-
-
-
-
phosphoribosyl ATP:pyrophosphate phosphoribosyltransferase
-
-
-
-
phosphoribosyl-ATP pyrophosphorylase
-
-
-
-
phosphoribosyl-ATP:pyrophosphate-phosphoribosyl phosphotransferase
-
-
-
-
phosphoribosyladenosine triphosphate pyrophosphorylase
-
-
-
-
phosphoribosyladenosine triphosphate synthetase
-
-
-
-
phosphoribosyltransferase, adenosine triphosphate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9031-46-3
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-, Q9Z472
essential for histidine biosynthesis
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
-
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
-
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
P60757
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-, Q9S762
-
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-, P60759
-
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
first step in histidine biosynthesis
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
P60757
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
show the reaction diagram
-
first step in histidine biosynthesis, mechanism of regulation, overview
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-, Q56UT2, Q56UT3
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
show the reaction diagram
Q56US5
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
show the reaction diagram
-
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
show the reaction diagram
-
first reaction of histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
show the reaction diagram
-
-
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
show the reaction diagram
-
first step in histidine biosynthesis
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
show the reaction diagram
-
first step in histidine biosynthesis
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
show the reaction diagram
-, Q9S762
first step in histidine biosynthesis
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
show the reaction diagram
-
first step in histidine biosynthesis
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
-
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-alpha-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-, Q9Z472
-
-
-
?
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 with histidine as a ligand, 8 histidine binding sites at the subunit interfaces
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-
first step in histidine biosynthesis
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
P60757
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
show the reaction diagram
-
first step in histidine biosynthesis, mechanism of regulation, overview
-
-
r
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
1-(5-phospho-D-ribosyl)-ATP + diphosphate
show the reaction diagram
-, Q56UT2, Q56UT3
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
show the reaction diagram
Q56US5
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
show the reaction diagram
-
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
show the reaction diagram
-
first reaction of histidine biosynthesis
-
-
?
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
show the reaction diagram
-
-
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
show the reaction diagram
-
first step in histidine biosynthesis
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
show the reaction diagram
-
first step in histidine biosynthesis
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
show the reaction diagram
-, Q9S762
first step in histidine biosynthesis
-
-
-
ATP + 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate + N-1-(5'-phosphoribosyl)-ATP
show the reaction diagram
-
first step in histidine biosynthesis
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
magnesium could have an effect on the conformation of the enzyme and its activity which would be independent of the state of substrate complexation
Mg2+
-
dependent on
Mg2+
P60757
required for substrate binding
Mg2+
-
dependent on
Mg2+
-
Kact = 1.9 mM; Ki = 23 mM
additional information
-
maximal activity is achieved when the concentration of free magnesium reaches about 2 mM, concentrations higher than 5 mM lead to inhibition perhaps due to the formation of MgATP2- complex
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(4E)-4-[(4-chlorophenyl)(hydroxy)methylidene]-1-(pyridin-3-ylmethyl)-5-(3,4,5-trimethoxyphenyl)pyrrolidine-2,3-dione
-, P60759
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
-, Q9S762
;
1-(5-phospho-alpha-D-ribosyl)-ATP
-
product inhibition, competitive to both substrates
1-[(5,6-diphenyl-1,2,4-triazin-3-yl)sulfanyl]-3-(1,3-thiazol-2-yl)propan-2-one
-, P60759
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
-
has whole-cell activity at 0.012 mM
2-([7-[(3-hydroxyphenyl)amino]-4-nitro-2,1,3-benzoxadiazol-5-yl]amino)-5-nitrophenol
-, P60759
exhibits 46% inhibition
2-[(2-bromo-3,5-dinitrophenyl)carbonyl]-N-phenylhydrazinecarboxamide
-
has whole-cell activity at 0.025 mM
2-[(2-bromo-3,5-dinitrophenyl)carbonyl]-N-phenylhydrazinecarboxamide
-, P60759
exhibits 71% inhibition
4-methoxybenzyl 2-methyl-5-oxo-4,7-dithiophen-2-yl-1,4,5,6,7,8-hexahydroquinoline-3-carboxylate
-, P60759
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
ADP
-
competitive to ATP, in the presence of histidine inhibition by AMP and ADP becomes positively cooperative and much more potent
ADP
-, Q9Z472
competitive to ATP
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
AMP
-
linear competitive inhibitor with respect to ATP, stabilizes the enzyme to thermal inactivation, protect the ordered enzymatic structure against thermodenaturation
AMP
-
inhibits the enzyme complex together with histidine to the T-state
AMP
P60757
binding structure and inhibition mode
AMP
-
competitive
AMP
-, Q9Z472
competitive to ATP
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
Ca2+
-, Q9Z472
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
EDTA
-, Q9Z472
moderate inhibitory effect
ethyl [(6-nitro-1,3-benzothiazol-2-yl)amino](oxo)acetate
-, P60759
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
Hg2+
-, Q9Z472
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 feedback inhibition
histidine
-
noncompetitive
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; stabilizes the enzyme to thermal inactivation, protects the ordered enzymatic structure against thermodenaturation, no interaction with binding sites
L-histidine
-
feed-back inhibition; inhibits reverse reaction cooperatively and completely
L-histidine
-
feed-back inhibition
L-histidine
-, Q9S762
feed-back inhibition; feed-back inhibition
L-histidine
-
feed-back inhibition
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
-, Q9Z472
noncompetitive, alkaline pH decreases the inhibitory effect
Mg2+
-
at high concentrations, Ki = 23 mM
N-[3-[(6-nitro-1,3-benzothiazol-2-yl)amino]-3-oxo-1-phenylpropyl]benzamide
-, P60759
occupies only the phosphoribosyl diphosphate binding site, exhibits greater than 50% inhibition at 0.01 mM, 35% inhibition at 0.001 mM
Pentachlorophenol
-
competitive to ATP, inhibitor in both directions, diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
Zn2+
-, Q9Z472
moderate inhibitory effect
Mn2+
-, Q9Z472
moderate inhibitory effect
additional information
-
carbonylcyanide m-chlorophenylhydrazone, which is a potent inhibitor of several enzymes with adenine-containing substrates or coenzymes has no effect
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
potassium chloride
-
stimulates ATP-PRT activity in crude extracts, adding KCl to a final concentration of 0.13 M in reaction mixture increases the reaction rate by about 40%
ATP
-
binding activates the enzyme complex to the R-state
additional information
-
other salts like ammonium sulfate or ammonium chloride show the same effect as KCl
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0184
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, wild-type enzyme
0.049
-
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 8.5, 25C
0.067
-
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.07
-
5-phospho-alpha-D-ribose 1-diphosphate
-, Q9Z472
A270P mutant protein, pH 8.5, temperature not specified in the publication
0.0712
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, mutant enzyme D155A
0.08
-
5-phospho-alpha-D-ribose 1-diphosphate
-, Q9Z472
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication; N215K mutant protein, pH 8.5, temperature not specified in the publication; wild type protein, pH 8.5, temperature not specified in the publication
0.09
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, mutant enzyme K8A
0.09
-
5-phospho-alpha-D-ribose 1-diphosphate
-, Q9Z472
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.13
-
5-phospho-alpha-D-ribose 1-diphosphate
-, Q9S762
recombinant At-ATP-PRT1
0.57
-
5-phospho-alpha-D-ribose 1-diphosphate
-, Q9S762
crude cell extracts
0.901
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, mutant enzyme T162A
0.94
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, mutant enzyme K50A
5.15
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, mutant enzyme T159A
37
-
5-phospho-alpha-D-ribose 1-diphosphate
-, Q9S762
crude cell extracts
0.22
-
ATP
-, Q9Z472
N215K mutant protein, pH 8.5, temperature not specified in the publication; wild type protein, pH 8.5, temperature not specified in the publication
0.23
-
ATP
-, Q9Z472
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.24
-
ATP
-, Q9Z472
A270P mutant protein, pH 8.5, temperature not specified in the publication
0.263
-
ATP
-
pH 8.5, 25C
0.35
-
ATP
-, Q9Z472
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.51
-
ATP
-, Q9S762
crude cell extracts
0.6
-
ATP
-, Q9S762
recombinant enzyme
1.05
-
ATP
-
25C, pH 8, mutant enzyme T162A
1.07
-
ATP
-
25C, pH 8, mutant enzyme T159A
2.7
-
ATP
-
25C, pH 8, wild-type enzyme
4.7
-
ATP
-
25C, pH 8, mutant enzyme D155A
5
-
ATP
-
25C, pH 8, mutant enzyme K50A
8.45
-
ATP
-
25C, pH 8, mutant enzyme K8A
89
-
ATP
-, Q9S762
crude cell extracts
additional information
-
additional information
-
steady-state kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.84
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, mutant enzyme T162A
1.07
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, mutant enzyme K8A
1.2
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, mutant enzyme T159A
1.29
-
5-phospho-alpha-D-ribose 1-diphosphate
-, Q9Z472
A270P mutant protein, pH 8.5, temperature not specified in the publication
1.36
-
5-phospho-alpha-D-ribose 1-diphosphate
-, Q9Z472
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
1.75
-
5-phospho-alpha-D-ribose 1-diphosphate
-, Q9Z472
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
1.91
-
5-phospho-alpha-D-ribose 1-diphosphate
-, Q9Z472
wild type protein, pH 8.5, temperature not specified in the publication
2.22
-
5-phospho-alpha-D-ribose 1-diphosphate
-, Q9Z472
N215K mutant protein, pH 8.5, temperature not specified in the publication
2.7
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, wild-type enzyme
2.83
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, mutant enzyme D155A
6.16
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, mutant enzyme K50A
additional information
-
5-phospho-alpha-D-ribose 1-diphosphate
-
25C, pH 8, mutant enzyme K50A
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.002
-
1-[(5,6-diphenyl-1,2,4-triazin-3-yl)sulfanyl]-3-(1,3-thiazol-2-yl)propan-2-one
-, P60759
-
0.88
-
ADP
-, Q9Z472
wild type protein, pH 8.5, temperature not specified in the publication
1.29
-
AMP
-, Q9Z472
wild type protein, pH 8.5, temperature not specified in the publication
1.44
-
AMP
-
25C, pH 8
0.0811
-
histidine
-
25C, pH 8
0.004
-
L-histidine
-
uncompetitive versus ATP, pH 8.0, 25C
0.0079
-
L-histidine
-
uncompetitive versus ATP, pH 8.25, 25C
0.0235
-
L-histidine
-
Kii-value, non competitive versus 5-phospho-alpha-D-ribosyl diphosphate, pH 8.5, 25C
0.0257
-
L-histidine
-
Kis-value, non competitive versus 5-phospho-alpha-D-ribosyl diphosphate, pH 8.5, 25C
0.0269
-
L-histidine
-
uncompetitive versus ATP, pH 8.75, 25C
0.0279
-
L-histidine
-
uncompetitive versus ATP, pH 8.5, 25C
0.0504
-
L-histidine
-
uncompetitive versus ATP, pH 9.0, 25C
0.1094
-
L-histidine
-
uncompetitive versus ATP, pH 9.25, 25C
0.11
-
L-histidine
-, Q9Z472
wild type protein, pH 8.5, temperature not specified in the publication
0.24
-
L-histidine
-, Q9Z472
A270P mutant protein, pH 8.5, temperature not specified in the publication
0.28
-
L-histidine
-, Q9Z472
N215K mutant protein, pH 8.5, temperature not specified in the publication
0.52
-
L-histidine
-, Q9Z472
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
4.15
-
L-histidine
-, Q9Z472
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
0.002
-
N-[3-[(6-nitro-1,3-benzothiazol-2-yl)amino]-3-oxo-1-phenylpropyl]benzamide
-, P60759
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0119
-
(4E)-4-[(4-chlorophenyl)(hydroxy)methylidene]-1-(pyridin-3-ylmethyl)-5-(3,4,5-trimethoxyphenyl)pyrrolidine-2,3-dione
-, P60759
-
0.004
-
1-[(5,6-diphenyl-1,2,4-triazin-3-yl)sulfanyl]-3-(1,3-thiazol-2-yl)propan-2-one
-, P60759
-
0.0139
-
2-[(2-bromo-3,5-dinitrophenyl)carbonyl]-N-phenylhydrazinecarboxamide
-, P60759
-
0.0055
-
4-methoxybenzyl 2-methyl-5-oxo-4,7-dithiophen-2-yl-1,4,5,6,7,8-hexahydroquinoline-3-carboxylate
-, P60759
-
0.033
-
L-histidine
-
pH 8.5, 25C
0.006
-
N-[3-[(6-nitro-1,3-benzothiazol-2-yl)amino]-3-oxo-1-phenylpropyl]benzamide
-, P60759
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.39
-
-, Q9Z472
N215K/L231F/T235A/A270P mutant protein, pH 8.5, temperature not specified in the publication
1.96
-
-, Q9Z472
A270P mutant protein, pH 8.5, temperature not specified in the publication
2.01
-
-, Q9Z472
N215K mutant protein, pH 8.5, temperature not specified in the publication
2.04
-
-, Q9Z472
L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
2.1
-
-, Q9Z472
N215K/L231F/T235A mutant protein, pH 8.5, temperature not specified in the publication
2.19
-
-, Q9Z472
wild type protein, pH 8.5, temperature not specified in the publication
additional information
-
-
description of assay method
additional information
-
-
data for genetically-modified Corynebacterium glutamicum
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
-
-
assay at
8.5
-
-, Q9S762
assay at; assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
13
-, Q9Z472
>40% relative activity, rapid loss of activity below pH 7.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
assay at
30
-
-, Q9S762
assay at; assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-, Q56UT2, Q56UT3
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate; transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
Manually annotated by BRENDA team
Q56US5
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
Manually annotated by BRENDA team
-
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
Manually annotated by BRENDA team
-, Q56UT2, Q56UT3
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate; transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
Manually annotated by BRENDA team
Q56US5
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
Manually annotated by BRENDA team
-
transcript levels is constitutively higher in Alyssum lesbiacum (a plant that hyperaccumulates Ni and exhibits an exceptional degree of Ni tolerance) than in the congeneric nonaccumulator Alyssum montanum, transcript levels in the weak hyperaccumulator Alyssum serpyllifolium is intermediate
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Lactococcus lactis subsp. lactis (strain IL1403)
Lactococcus lactis subsp. lactis (strain IL1403)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
44600
-
-, Q9S762
calculated mass from amino acid sequence
44800
-
-, Q9S762
calculated mass from amino acid sequence
63000
-
-, Q9Z472
homodimer, gel filtration
180000
-
-
gel filtration
186000
-
-
dynamic light scattering in the presence of AMP or histidine
192000
-
-, Q9Z472
homohexamer, gel filtration
200000
220000
-
gel filtration
210000
221000
-
sedimentation, equilibrium centrifugation with meniscus depletion method
216000
-
-
ultracentrifugation analysis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
active form
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
hexamer
-
6 * 33367, dimers arranged in a hexamer, in the presence of AMP
hexamer
-
inactive form, in complex with histidine
homodimer
-, Q9Z472
2 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000
homohexamer
-
6 * 31515.1, ESI-MS, gel filtration, His-tagged protein, not influenced by allosteric inhibitor L-histidine or ATP
octamer
-
4 * catalytic subunit HisGs + 4 * regulatory subunit HisZ, (alpha,beta)4
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
homohexamer
-, Q9Z472
6 * 32191, MALDI-TOF MS, gel filtration, theoretical molecular mass 31000
additional information
-
overall structure and monomer architecture, several motif 2 loops in both subunit types, switch structure between active and inactive conformation
additional information
P60757
quarternary structure
additional information
-
subunit structures, structure evolution
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
P60757
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
-
hanging drop vapour diffusion method at 16C, 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
-, P60759
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
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
overview: stability at various pH-values
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
-
-
very sensitive to heat inactivation, 0.4 mM histidine stabilizes the enzyme to inactivation by heat
47.5
-
-
1.9 mg enzyme/ml, 80 min, 75% loss of activity without addition of AMP, with 0.05 mM AMP about 60% loss of activity, with 0.5 mM AMP about 40% loss of activity, with 5 mM AMP about 25% loss of activity
48
-
-
3 mg enzyme/ml, 10 min, 15% remaining activity without addition of histidine, with 0.000086 mM histidine about 15% remaining activity after 15 min, with 0.00069 mM histidine about 70% remaining activity after 80 min, with 0.00345 mM histidine about 80% remaining activity after 80 min, with 0.0069 mM histidine about 55% remaining activity after 50 min
additional information
-
-
heat inactivation depends on protein concentration and inhibitors
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
histidine or AMP stabilizes the enzyme with respect to thermal inactivation
-
L-histidine, 0.4 mM, stabilizes against heat inactivation, 0.04 mM does not stabilize against heat inactivation, at 1.33 mM and higher heat inactivation is greater than the control
-
NaCl and 2-mercaptoethanol stabilize the very labile enzyme
-
overview, stability of the enzyme at various pH-values, salt concentrations and histidine concentrations
-
slight stabilization by 10 mM MgCl2 or CaCl2 by 1 mM MnCl2 and by 1 mM histidine at pH-values above 7
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 50 mM Tris-HCl, pH 7.5, 0.4 mM DTT and one protease inhibitor per litre, 50% v/v glycerol, long term storage
-
4C, 0.01 M Tris, 0.10 M NaCl, 0.4 mM histidine, 2.8 mM 2-mercaptoethanol, 0.5 mM EDTA, pH 7.5, 50% loss of activity after several days
-
4C, HEPES buffer pH 7.5, final ammonium sulfate microcrystalline enzyme in 60% saturated ammonium sulfate, 0.1 M NaCl, 0.01 M Tris, 1.5 mM EDTA, 10 mM dithiothreitol, stable for 1 month, greater than 95% activity retained
-
storage in liquid nitrogen of quick-frozen enzyme in HEPES buffer pH 7.5, 0.1 M NaCl, 0.01 M Tris, 0.5 mM EDTA, 1 mM dithiothreitol, 1 mM histidine, indefinitely stable, preserves 100% activity. The critical factor for stability seems to be the maintenance of a sulfhydryl-reducing environment, high dithiothreitol concentrations has no adverse effect at either 0C or 37C
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the recombinant enzymes are produced as fused proteins with a maltose-binding protein, and the purification is made by a two step amylose resin column followed by a digestion with Factor Xa
-, Q9S762
immobilized metal ion affinity chromatography, gel filtration
-, Q9Z472
centrifugation and DEAE-Sephacel anion-exchange column
-
recombinant selenomethionine-labeled enzyme from strain B834(DE3)
P60757
recombinant wild-type and selenomethionine-labeled enzyme complex comprising subunits HisGs and HisZ from Escherichia coli
-
immobilized metal ion affinity chromatography (Ni2+)
-
nickel-nitrilotriacetic acid column, Sephadex G-200 later on
-
ammonium sulfate precipitation and DEAE-cellulose chromatography
-
first purification by heating the crude extract, ammonium sulfate precipitation and selective histidine-dependent ammonium sulfate precipitation
-
Mn2+ precipitation, DEAE-cellulose and ammonium sulfate precipitation, later on Sephadex G-150
-
recombinant wild-type and selenomethionine-labeled subunits HisGs and HisZ from Escherichia coli in a multistep procedure
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
overexpression of an Alyssum lesbiacum ATP-PRT cDNA in transgenic Arabidopsis thaliana increases the pool of free His up to 15fold in shoot tissue, without affecting the concentration of any other amino acid. His-overproducing lines also display elevated tolerance to Ni but do not exhibit increased Ni concentrations in either xylem sap or shoot tissue, suggesting that additional factors are necessary to recapitulate the complete hyperaccumulator phenotype; overexpression of an Alyssum lesbiacum ATP-PRT cDNA in transgenic Arabidopsis thaliana increases the pool of free His up to 15fold in shoot tissue, without affecting the concentration of any other amino acid. His-overproducing lines also display elevated tolerance to Ni but do not exhibit increased Ni concentrations in either xylem sap or shoot tissue, suggesting that additional factors are necessary to recapitulate the complete hyperaccumulator phenotype
-, Q56UT2, Q56UT3
overexpression of an Alyssum lesbiacum ATP-PRT cDNA in transgenic Arabidopsis thaliana increases the pool of free His up to 15fold in shoot tissue, without affecting the concentration of any other amino acid. His-overproducing lines also display elevated tolerance to Ni but do not exhibit increased Ni concentrations in either xylem sap or shoot tissue, suggesting that additional factors are necessary to recapitulate the complete hyperaccumulator phenotype
Q56US5
overexpression of an Alyssum lesbiacum ATP-PRT cDNA in transgenic Arabidopsis thaliana increases the pool of free His up to 15fold in shoot tissue, without affecting the concentration of any other amino acid. His-overproducing lines also display elevated tolerance to Ni but do not exhibit increased Ni concentrations in either xylem sap or shoot tissue, suggesting that additional factors are necessary to recapitulate the complete hyperaccumulator phenotype
-
expression in Escherichia coli; expression in Escherichia coli
-, Q9S762
His-tagged protein expressed in Escherichia coli BL21(DE3)
-, Q9Z472
expression of selenomethionine-labeled enzyme in strain B834(DE3)
P60757
overexpression of subunits HisGs and HisZ comprising complex in Escherichia coli strain BL21(DE3) as wild-type, or in strain B834 as selenomethionine-labeled complex
-
codon adapted to Escherichia coli, synthetically prepared, His-tagged protein expressed in Escherichia coli BL21(DE3)pLysS
-
expressed in Escherichia coli
-
separate expression of subunits HisGs and HisZ in Escherichia coli strain BL21(DE3) as wild-type, or in strain B834 as selenomethionine-labeled proteins
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A270P
-, Q9Z472
conserved residue
L231F/T235A
-, Q9Z472
conserved residues
N215K
-, Q9Z472
conserved residue
N215K/L231F/T235A
-, Q9Z472
conserved residues, 37fold increase in Ki-value of histidine
N215K/L231F/T235A/A270P
-, Q9Z472
conserved residues
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-
HisG represents a potential drug target for tuberculosis
drug development
P60759
HisG represents a potential drug target for tuberculosis