2.4.2.14: amidophosphoribosyltransferase
This is an abbreviated version!
For detailed information about amidophosphoribosyltransferase, go to the full flat file.
Word Map on EC 2.4.2.14
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2.4.2.14
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purine
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phosphoribosylamine
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glutamine-dependent
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glycinamide
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6-diazo-5-oxo-l-norleucine
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14cglycine
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pp-ribose-p
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acivicin
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phosphoribosyltransferases
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ribotide
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p-rib-pp
- 2.4.2.14
- purine
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phosphoribosylamine
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glutamine-dependent
- glycinamide
- 6-diazo-5-oxo-l-norleucine
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14cglycine
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pp-ribose-p
- acivicin
- phosphoribosyltransferases
- ribotide
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p-rib-pp
Reaction
Synonyms
5'-phosphoribosylpyrophosphate amidotransferase, 5-phosphoribosyl-1-pyrophosphate amidotransferase, 5-phosphoribosylpyrophosphate amidotransferase, 5-phosphororibosyl-1-pyrophosphate amidotransferase, ADE4, alpha-5-phosphoribosyl-1-pyrophosphate amidotransferase, amido phosphoribosyltransferase, amidotransferase, phosphoribosyl pyrophosphate, APRT, ATASE, AtGPRT, Gln phosphoribosylpyrophosphate amidotransferase, glutamine 5-phosphoribosylpyrophosphate amidotransferase, glutamine phosphoribosyl pyrophosphate amidotransferase, glutamine phosphoribosylpyrophosphate amidotransferase, glutamine ribosylpyrophosphate 5-phosphate amidotransferase, GPAT, GPATase, GPRAT, GPRAT2, phosphoribose pyrophosphate amidotransferase, phosphoribosyl amidotransferase, phosphoribosyl pyrophosphate amidotransferase, phosphoribosylamidotransferase, phosphoribosyldiphosphate 5-amidotransferase, phosphoribosylpyrophosphate glutamyl amidotransferase, PPAT, PRAT, PurF
ECTree
2.4.2.14 amidophosphoribosyltransferaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 2.4.2.14 - amidophosphoribosyltransferase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1-alpha-diphosphoryl-2-alpha,3-alpha-dihydroxy-4-beta-cyclopentane-methanol-5-phosphate
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competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate in wild-type and P410W mutant, competition for the amidotransferase C site
2,4-diamino-6-(3,4,5-trimethoxyanilino)-methylpyrido[3,2-d]pyrimidine
PY873
2,4-diamino-6-(3,4,5-trimethoxybenzyl)-5,6,7,8-tetrahydro-quinazoline
PY899
2-amino-4-oxo-5-chloropentanoate
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approx. 80% inactivation of NH3-dependent activity after 30 min
5',5'-P1,P4-diguanosine tetraphosphate
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IC50: 0.4 mM, 2 mM, approx. 80% inhibition
5'-p-fluorosulfonylbenzoyladenosine
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inactivation follows pseudo-first order kinetic, AMP, GMP and 5-phospho-alpha-D-ribose 1-diphosphate protect
5-((4-carboxy-4-(4-(((2,4-diaminopyrido[3,2-d]pyrimidine-6-yl)methyl)amino)benzamido)butyl)carbamoyl)isophthalic acid
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adenine nucleotide
maximal inhibition by combination of adenine nucleotides (in total 10 mM), inhibitory effect of single nucleotides (5 mM) increases in the order AMP, ATP, ADP
iodoacetamide
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approx. 60% inactivation of amidotransferase activity after 30 min, very weak inactivation of NH3-dependent activity
piritrexim
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noncompetitive vs. 5-phospho-alpha-D-ribose 1-diphosphate, binds with positive cooperativity at 2 allosteric sites of an inactive dimer
purine nucleotide
allosteric feedback inhibition by end products of the purine biosynthesis pathway, act on the PRPP domain
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6-diazo-5-oxo-L-norleucine
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approx. 98% inactivation of amidotransferase activity after 30 min
6-diazo-5-oxo-L-norleucine
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competitive vs. glutamine, inactivation half-life: 11 min
ADP
50% inhibition of wild-type, S283A, K305Q, R307Q and S347A mutant enzyme at 4.7 mM, 24 mM, 31 mM, 28 mM and 8.1 mM respectively
AMP
50% inhibition of wild-type, S283A, K305Q, R307Q and S347A mutant enzyme at 0.9 mM, 6.1 mM, 2.5 mM, 2.6 mM and 1.5 mM respectively
AMP
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approx. 10 mM, complete inhibition, sigmoidal inhibition curve, competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate, GMP and AMP together have a synergistic effect on inhibition
AMP
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5 mM, 79% and 24% inhibition of aminotransferase and amidotransferase activity at 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
AMP
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competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate, noncompetitive vs. glutamine
AMP
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no inhibition in the presence of 5-phospho-alpha-D-ribose 1-diphosphate at high concentrations
AMP
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2.7 mM and 1.2 mM, 50% inhibition of stable and unstable enzyme preparation respectively
DAS734
phenyltriazole acetic acid herbicide, [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic acid, inhibits Arabidopsis root growth by 50% at 200 nM, phytotoxicity can be alleviated by addition of adenine, no inhibitory effect on Escherichia coli; phenyltriazole acetic acid herbicide, [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic acid, non-competitive with respect to L-glutamine with slow, tight-binding behavior, inhibits Arabidopsis root growth by 50% at 200 nM, phytotoxicity can be alleviated by addition of adenine, no inhibitory effect on Escherichia coli
DAS734
i.e. [5-(4-chlorophenyl)-1-isopropyl-1H-[1,2,4]triazol-3-yl]-acetic acid, direct and specific inhibition, competitive inhibitor for the substrate 5-phospho-alpha-D-ribose 1-diphosphate
GMP
50% inhibition of wild-type, S283A, K305Q, R307Q and S347A mutant enzyme at 9.4 mM, 6.6 mM, 50 mM, 50 mM and 145 mM respectively
GMP
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approx. 2.5 mM, complete inhibition, highly sigmoidal inhibition curve, competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate, GMP and AMP together have an synergistic effect on inhibition
GMP
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0.5 mM; 5 mM, 56% and 12% inhibition of aminotransferase and amidotransferase activity at 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
GMP
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no inhibition in the presence of 5-phospho-alpha-D-ribose 1-diphosphate at high concentrations
GMP
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0.44 mM and 0.25 mM, 50% inhibition of stable and unstable enzyme preparation respectively
IMP
50% inhibition of wild-type and S347A mutant enzyme at 26 mM and 41 mM respectively
additional information
minimal inhibition by inosine monophosphate (IMP) and guanosine monophosphate (GMP)
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additional information
minimal inhibition by inosine monophosphate (IMP) and guanosine monophosphate (GMP)
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additional information
minimal inhibition by inosine monophosphate (IMP) and guanosine monophosphate (GMP)
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additional information
strong synergistic inhibition with ADP and GMP
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additional information
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not inhibited by ribose 5-phosphate, purine ribonucleosides or bases, 2'- or 3'-phosphate or deoxyribose phosphate analogues or by pyrimidine ribonucleotides
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additional information
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synergistic inhibition of glutaminase activity by AMP plus GMP and N3-AMP plus GMP
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additional information
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synergistic inhibition by AMP and GMP, binding of GMP to an allosteric i.e. A site and AMP to a proximal catalytic i. e. C site are necessary for synergistic inhibition
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