2.4.2.17: ATP phosphoribosyltransferase
This is an abbreviated version!
For detailed information about ATP phosphoribosyltransferase, go to the full flat file.
Word Map on EC 2.4.2.17
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2.4.2.17
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hisgs
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l-histidine
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glutamicum
-
hexameric
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hetero-octameric
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histidyl-trna
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long-form
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short-form
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drug development
- 2.4.2.17
-
hisgs
- l-histidine
- glutamicum
-
hexameric
-
hetero-octameric
-
histidyl-trna
-
long-form
-
short-form
- drug development
Reaction
Synonyms
1-(5-phospho-D-ribosyl)-ATP:pyrophosphate phospho-alpha-D-ribosyltransferase, adenosine 5'-triphosphate phosphoribosyltransferase, adenosine triphosphate phosphoribosyltransferase, adenosine-triphosphate phosphoribosyltransferase, ATP phosphoribosyl transferase, ATP phosphoribosyl transferase complex, ATP phosphoribosyltransferase, ATP-phosphoribosyl transferase, ATP-phosphoribosyltransferase, ATP-PRT, ATP-PRT1, ATP-PRT2, ATP-PRTase, ATPPRT, HisG, HisGL, 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
ECTree
2.4.2.17 ATP phosphoribosyltransferaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 2.4.2.17 - ATP phosphoribosyltransferase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(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-(5-phospho-alpha-D-ribosyl)-ATP
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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
most potent inhibitor, spans the PR-ATP binding site, exhibits greater than 50% inhibition at 0.01 mM, 40% inhibition at 0.001 mM
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
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noncompetitive inhibitor with respect to both substrates in the reaction producing ATP and 5-phospho-alpha-D-ribose 1-diphosphate
adenine
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competitive to ATP and 5-phospho-alpha-D-ribose 1-diphosphate
beta,gamma-methylene-ATP
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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
dicoumarol
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competitive with respect to ATP, inhibitor in both directions, diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
dinitrophenol
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diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
diphosphate
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non competitive to both substrates
ethyl [(6-nitro-1,3-benzothiazol-2-yl)amino](oxo)acetate
exhibits 39% inhibition
Guanosine 5'-diphosphate-3'-diphosphate
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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
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
Pentachlorophenol
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competitive to ATP, inhibitor in both directions, diminishes yield of phosphoribosyladenosine triphosphate by acting as parasite substrate
additional information
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carbonylcyanide m-chlorophenylhydrazone, which is a potent inhibitor of several enzymes with adenine-containing substrates or coenzymes has no effect
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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
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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
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has whole-cell activity at 0.025 mM
ADP
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competitive to ATP, in the presence of histidine inhibition by AMP and ADP becomes positively cooperative and much more potent
AMP
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linear competitive inhibitor with respect to ATP, stabilizes the enzyme to thermal inactivation, protect the ordered enzymatic structure against thermodenaturation
AMP
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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
histidine
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feedback inhibition, inhibits the enzyme complex together with ATP to the T-state, no inhibition of mutants E130A and Y268F/Y269F
L-histidine
complete inhibition at 1 mM, about 10% inhibition at 0.25 mM
L-histidine
noncompetitive, alkaline pH decreases the inhibitory effect
L-histidine
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feed-back inhibition; stabilizes the enzyme to thermal inactivation, protects the ordered enzymatic structure against thermodenaturation, no interaction with binding sites
L-histidine
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feed-back inhibition; stabilizes the enzyme to thermal inactivation, protects the ordered enzymatic structure against thermodenaturation, no interaction with binding sites
L-histidine
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allosteric inhibition, synergistically favored by AMP; feed-back inhibition
L-histidine
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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
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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
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feed-back inhibition
L-histidine
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feed-back inhibition; inhibits reverse reaction cooperatively and completely
