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5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
L-glutamine + H2O
L-glutamate + NH3
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
phosphoribosylanthranilate
indoleglycerol phosphate + CO2 + H2O
5 µM PurF mutant I198V or variant 1-04, in presence of 0.5 mM beta-mercaptoethanol, pH 8.6, 23 °C, 16 h
Amadori rearrangement of aminoaldose (phosphoribosylanthranilate) to aminoketose (indoleglycerol phosphate)
-
?
additional information
?
-
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
-
-
?
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
-
-
-
-
r
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
first step of de novo purine biosynthesis
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
40 mM glutamine, 5 mM PRPP, 10 mM dithiothreitol
glutamate dehydrogenase-coupled assay, glutamate-dependent reduction of 1.36 mM 3-acetylpyridine dinucleotide measurable as increase of absorbance at 363 nm
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
-
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
-
in Salmonella enterica, the biosynthetic pathways for the generation of purines and the essential cofactor thiamine pyrophosphate branch after sharing five enzymatic steps. Phosphoribosyl amine is the first intermediate in the common portion of the pathway and is generated from phosphoribosylpyrophosphate and glutamine by the PurF enzyme (phosphoribosylpyrophosphate amidotransferase). Tryptophan biosynthetic enzyme complex anthranilate synthase-phosphoribosyltransferase, composed of the TrpD and TrpE proteins, is essential for phosphoribosyl amine formation in strains lacking both yjgF and purF
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
ir
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
reaction at 70% the rate of aminotransferase activity
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
ir
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
reaction at 50% the rate of aminotransferase activity
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
no activity with carbamoyl phosphate
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
glutamine binding site distinct from NH3-site
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
reaction at 33% the rate of amminotransferase activity
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
enzyme of purine biosynthetic pathway, regulatory enzyme in the flow of recently fixed nitrogen from initial assimilation into amino acids via purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
regulating enzyme of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
rate-limiting enzyme of purine biosynthesis
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
-
-
?
L-glutamine + H2O
L-glutamate + NH3
-
enzyme exhibits glutaminase activity in the absence of other substrates or effectors
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
lower aminotransferase activity compared to amidotransferase activity
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
-
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
no activity with NH4+
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
-
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
-
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
-
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
no activity with NH4+
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
2.8fold higher aminotransferase activity compared to amidotransferase activity
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
-
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
2fold higher aminotransferase activity compared to amidotransferase activity
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
3fold higher aminotransferase activity compared to amidotransferase activity
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
NH3-binding site is distinct from glutamine-site
-
?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
-
-
?
additional information
?
-
no GPRAT activity detectable in cell extracts of recombinant AtGPRAT1 expressing Escherichia coli
-
-
?
additional information
?
-
no GPRAT activity detectable in cell extracts of recombinant AtGPRAT1 expressing Escherichia coli
-
-
?
additional information
?
-
no GPRAT activity detectable in cell extracts of recombinant AtGPRAT1 expressing Escherichia coli
-
-
?
additional information
?
-
GPATase-thioester-5'-phosphoribosylpyrophosphate complex model demonstrates the ammonia transfer between the active sites of GPATase in its active conformation. The ammonia channel in GPATase is a transient structural element, a pipe through which ammonia travels in the absence of an external driving potential. The ammonia tunnel in GPATase discriminates against ammonium ion
-
-
?
additional information
?
-
-
GPATase-thioester-5'-phosphoribosylpyrophosphate complex model demonstrates the ammonia transfer between the active sites of GPATase in its active conformation. The ammonia channel in GPATase is a transient structural element, a pipe through which ammonia travels in the absence of an external driving potential. The ammonia tunnel in GPATase discriminates against ammonium ion
-
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
-
-
?
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
first step of de novo purine biosynthesis
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
-
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
-
in Salmonella enterica, the biosynthetic pathways for the generation of purines and the essential cofactor thiamine pyrophosphate branch after sharing five enzymatic steps. Phosphoribosyl amine is the first intermediate in the common portion of the pathway and is generated from phosphoribosylpyrophosphate and glutamine by the PurF enzyme (phosphoribosylpyrophosphate amidotransferase). Tryptophan biosynthetic enzyme complex anthranilate synthase-phosphoribosyltransferase, composed of the TrpD and TrpE proteins, is essential for phosphoribosyl amine formation in strains lacking both yjgF and purF
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
enzyme of purine biosynthetic pathway, regulatory enzyme in the flow of recently fixed nitrogen from initial assimilation into amino acids via purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
regulating enzyme of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
first reaction in de-novo pathway of purine biosynthesis
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
-
-
?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
rate-limiting enzyme of purine biosynthesis
-
?
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-alpha-diphosphoryl-2-alpha,3-alpha-dihydroxy-4-beta-cyclopentane-methanol-5-phosphate
-
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
-
approx. 80% inactivation of NH3-dependent activity after 30 min
5',5'-P1,P4-diguanosine tetraphosphate
-
IC50: 0.4 mM, 2 mM, approx. 80% inhibition
5'-p-fluorosulfonylbenzoyladenosine
-
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
-
6-diazo-5-oxo-L-norleucine
6-iodopurine
-
5 mM, 39% inhibition
6-mercaptopurine ribonucleotide
-
5 mM, 64% inhibition
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
allopurinol ribonucleotide
-
5 mM, 68% inhibition
cAMP
competitive inhibitor
cGMP
competitive inhibitor
CMP
-
5 mM, 22% inhibition
dCMP
-
5 mM, 26% inhibition
diphosphate
-
uncompetitive vs. 5-phospho-alpha-D-ribose 1-diphosphate
glutamate
-
competitive vs. glutamate
IDP
-
5 mM, 29% inhibition
iodoacetamide
-
approx. 60% inactivation of amidotransferase activity after 30 min, very weak inactivation of NH3-dependent activity
methyl-dCMP
-
5 mM, 47% inhibition
N3-AMP
-
1.2-1.4 mM, 50% inhibition, AMP and GMP protect
NH3
-
inhibition of amidotransferase activity
NH4+
-
competitive vs. glutamine
OMP
-
5 mM, 25% inhibition
p-mercuribenzoate
-
0.001 mM, complete inhibition
piritrexim
-
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
-
TMP
-
5 mM, 42% inhibition
TTP
-
5 mM, 12% inhibition
UDP
-
5 mM, 19% inhibition
UMP
-
5 mM, 25% inhibition
UTP
-
5 mM, 16% inhibition
XDP
-
5 mM, 27% inhibition
XTP
-
5 mM, 44% inhibition
6-diazo-5-oxo-L-norleucine
-
6-diazo-5-oxo-L-norleucine
-
approx. 98% inactivation of amidotransferase activity after 30 min
6-diazo-5-oxo-L-norleucine
-
competitive vs. glutamine, inactivation half-life: 11 min
ADP
-
4.1 mM, 50% inhibition
ADP
-
1 mM, approx. 95% inhibition
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
ADP
-
5 mM, 40% inhibition
AMP
-
6.12 mM, 50% inhibition
AMP
-
1 mM, approx. 40% inhibition
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
-
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
-
4.7 mM, 50% inhibition
AMP
-
5 mM, 50% inhibition
AMP
-
competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate
AMP
-
1.8 mM, 50% inhibition
AMP
-
5 mM, 76% inhibition, noncompetive vs. glutamine
AMP
-
5 mM, 79% and 24% inhibition of aminotransferase and amidotransferase activity at 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
AMP
-
competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate, noncompetitive vs. glutamine
AMP
-
no inhibition in the presence of 5-phospho-alpha-D-ribose 1-diphosphate at high concentrations
AMP
-
2.7 mM and 1.2 mM, 50% inhibition of stable and unstable enzyme preparation respectively
ATP
-
-
ATP
-
10 mM, 10% residual activity
ATP
-
5 mM, 21% inhibition
azaserine
-
azaserine
-
competitive vs. glutamine, inactivation half-life: 12 min
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
GDP
-
8.5 mM, 50% inhibition
GDP
-
1 mM, approx. 75% inhibition
GDP
-
5 mM, 40% inhibition
GMP
-
IC50: 7.9 mM
GMP
-
1 mM, approx. 60% inhibition
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
-
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
-
1.2-1.4 mM, 50% inhibition
GMP
-
2 mM, 50% inhibition
GMP
-
0.5 mM; 50% inhibition
GMP
-
0.5 mM; 5 mM, 70% inhibition
GMP
-
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
-
no inhibition in the presence of 5-phospho-alpha-D-ribose 1-diphosphate at high concentrations
GMP
-
0.44 mM and 0.25 mM, 50% inhibition of stable and unstable enzyme preparation respectively
GTP
-
10 mM, 10% residual activity
GTP
-
5 mM, 79% inhibition
GTP
-
5 mM, 13% inhibition
IMP
50% inhibition of wild-type and S347A mutant enzyme at 26 mM and 41 mM respectively
IMP
-
5 mM, 86% inhibition
IMP
-
5 mM, 41% inhibition
phosphate
-
20 mM, 50% inhibition
phosphate
-
competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate
XMP
-
51% inhibition; 5 mM
XMP
-
competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate
XMP
-
5 mM, 41% inhibition
additional information
minimal inhibition by inosine monophosphate (IMP) and guanosine monophosphate (GMP)
-
additional information
minimal inhibition by inosine monophosphate (IMP) and guanosine monophosphate (GMP)
-
additional information
minimal inhibition by inosine monophosphate (IMP) and guanosine monophosphate (GMP)
-
additional information
strong synergistic inhibition with ADP and GMP
-
additional information
-
strong synergistic inhibition with ADP and GMP
-
additional information
-
not inhibited by ribose 5-phosphate, purine ribonucleosides or bases, 2'- or 3'-phosphate or deoxyribose phosphate analogues or by pyrimidine ribonucleotides
-
additional information
-
synergistic inhibition of glutaminase activity by AMP plus GMP and N3-AMP plus GMP
-
additional information
-
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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Adenocarcinoma of Lung
Role and regulation of coordinately expressed de novo purine biosynthetic enzymes PPAT and PAICS in lung cancer.
Carcinoma
Enzymic capacities of purine de Novo and salvage pathways for nucleotide synthesis in normal and neoplastic tissues.
Carcinoma
Increased amidophosphoribosyltransferase and decreased xanthine oxidase activity in human and rat renal cell carcinoma.
Carcinoma
Purine enzymology of human colon carcinomas.
Carcinoma, Hepatocellular
Enzymes of purine metabolism in cancer.
Carcinoma, Hepatocellular
Enzymic capacities of purine de Novo and salvage pathways for nucleotide synthesis in normal and neoplastic tissues.
Carcinoma, Hepatocellular
Glutamine phosphoribosylpyrophosphate amidotransferase: increased activity in hepatomas.
Carcinoma, Hepatocellular
Imbalance of purine metabolism in hepatomas of different growth rates as expressed in behavior of glutamine-phosphoribosylpyrophosphate amidotransferase (amidophosphoribosyltransferase, EC 2.4.2.14).
Carcinoma, Hepatocellular
Imbalance of purine metabolism in hepatomas of different growth rates as expressed in behavior of xanthine oxidase (EC 1.2.3.2).
Carcinoma, Hepatocellular
Molecular cloning of human amidophosphoribosyltransferase.
Carcinoma, Hepatocellular
Oncolytic activity and mechanism of action of a novel L-cysteine derivative, L-cysteine, ethyl ester, S-(N-methylcarbamate) monohydrochloride.
Carcinoma, Hepatocellular
Purification, properties, and immunotitration of hepatoma glutamine phosphoribosylpyrophosphate amidotransferase (amidophosphoribosyltransferase, EC 2.4.2.14).
Carcinoma, Hepatocellular
Rapid in vivo inactivation by acivicin of CTP synthetase, carbamoyl-phosphate synthetase II, and amidophosphoribosyltransferase in hepatoma.
Carcinoma, Lewis Lung
Enzymic capacities of purine de Novo and salvage pathways for nucleotide synthesis in normal and neoplastic tissues.
Carcinoma, Renal Cell
Enzymic capacities of purine de Novo and salvage pathways for nucleotide synthesis in normal and neoplastic tissues.
Carcinoma, Renal Cell
Increased amidophosphoribosyltransferase and decreased xanthine oxidase activity in human and rat renal cell carcinoma.
Gout
[Behavior of glutamine phosphoribosyl pyrophosphate amidotransferase in patients with primary gout]
Intellectual Disability
Identification of Clock Genes Related to Hypertension in Kidney From Spontaneously Hypertensive Rats.
Lesch-Nyhan Syndrome
Activities of amidophosphoribosyltransferase (EC2.4.2.14) and the purine phosphoribosyltransferases (EC2.4.2.7 and 2.4.2.8), and the phosphoribosylpyrophosphate content of rat central nervous system at different stages of development--their possible relationship to the neurological dysfunction in the Lesch-Nyhan syndrome.
Leukemia
Antifolates induce inhibition of amido phosphoribosyltransferase in leukemia cells.
Leukemia
Cytotoxic mechanisms of glutamine antagonists in mouse L1210 leukemia.
Leukemia
Mechanisms of inhibition of amido phosphoribosyltransferase from mouse L1210 leukemia cells.
Leukemia
Phosphoribosylamidotransferase: regulation of activity in virus-induced murine leukemia by purine nucleotides.
Leukemia
Properties of 5'-phosphoribosylpyrophosphate amidotransferase in virus induced murine leukemia.
Lung Neoplasms
Phosphoribosyl Pyrophosphate Amidotransferase Promotes the Progression of Thyroid Cancer via Regulating Pyruvate Kinase M2.
Neoplasm Metastasis
Exploring targeted therapy of osteosarcoma using proteomics data.
Neoplasms
Differential expression of six chicken genes associated with fatness traits in a divergently selected broiler population.
Neoplasms
Imbalance of purine metabolism in hepatomas of different growth rates as expressed in behavior of xanthine oxidase (EC 1.2.3.2).
Neoplasms
Kinetics of amidophosphoribosyltransferase in intact tumor cells.
Neoplasms
Oncolytic activity and mechanism of action of a novel L-cysteine derivative, L-cysteine, ethyl ester, S-(N-methylcarbamate) monohydrochloride.
Starvation
A study in molecular contingency: glutamine phosphoribosylpyrophosphate amidotransferase is a promiscuous and evolvable phosphoribosylanthranilate isomerase.
Starvation
Decreased phosphoribosylpyrophosphate as the basis for decreased purine synthesis during amino acid starvation of human lymphoblasts.
Starvation
Degradation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase in vivo.
Thyroid Neoplasms
Phosphoribosyl Pyrophosphate Amidotransferase Promotes the Progression of Thyroid Cancer via Regulating Pyruvate Kinase M2.
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0.031 - 0.87
5-phospho-alpha-D-ribose 1-diphosphate
193
glutamine
-
5-phospho-alpha-D-ribose 1-diphosphate-independent glutamine hydrolysis
additional information
additional information
-
0.031
5-phospho-alpha-D-ribose 1-diphosphate
-
P410W mutant enzyme
0.053
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.067
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.072
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.086
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.14 - 0.48
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.24
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.35
5-phospho-alpha-D-ribose 1-diphosphate
at pH 7.8, temperature not specified in the publication
0.4
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.4
5-phospho-alpha-D-ribose 1-diphosphate
-
cosubstrate NH3
0.47
5-phospho-alpha-D-ribose 1-diphosphate
-
adenocarcinoma 755
0.48
5-phospho-alpha-D-ribose 1-diphosphate
-
in Tris buffer
0.57
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.66
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.7
5-phospho-alpha-D-ribose 1-diphosphate
-
cosubstrate glutamine
0.87
5-phospho-alpha-D-ribose 1-diphosphate
-
at 90°C
0.1
L-glutamine
-
-
0.64
L-glutamine
-
N101G mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity
1.24 - 1.5
L-glutamine
-
-
1.34
L-glutamine
cell extracts of recombinant AtGPRAT2 expressing Escherichia coli
1.42
L-glutamine
-
N101D mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity
1.72
L-glutamine
-
5-phospho-alpha-D-ribose 1-diphosphate-dependent glutamine hydrolysis
1.72
L-glutamine
-
wild-type enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity
1.8
L-glutamine
-
adenocarcinoma 755
2.43
L-glutamine
-
G102A mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity
6.03
L-glutamine
-
N101G mutant enzyme, aminotransferase activity
6.08
L-glutamine
-
D127A mutant enzyme, aminotransferase activity
7.31
L-glutamine
-
R73L mutant enzyme, aminotransferase activity
7.34
L-glutamine
-
wild-type enzyme, aminotransferase activity
7.67
L-glutamine
-
G102A mutant enzyme, aminotransferase activity
9.17
L-glutamine
-
N101D mutant enzyme, aminotransferase activity
9.76
L-glutamine
-
R73H mutant enzyme, aminotransferase activity
101
L-glutamine
-
R73H mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity
110
L-glutamine
-
R73L mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity
236
L-glutamine
-
D127A mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity
7.34
NH3
-
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic study
-
additional information
additional information
-
kinetic properties of amido- and aminotransferase activity
-
additional information
additional information
-
effect of AMP on kinetic parameters
-
additional information
additional information
-
kinetic constants of Arg73 and Tyr74 mutants for basal and total glutaminase activity
-
additional information
phosphoribosylanthranilate
variant 1-04, kcat/Km = 0.3 1/s*M, initial velocity measurements over time at substrate concentrations to up to 2 mM
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102000
-
sedimentation equilibrium centrifugation, phosphate, phosphoribosyldiphosphate or purine mononucleotides influence the sedimentation profile
110000
-
ligand-induced alteration of sedimentation coefficient and Stokes radius, gel filtration or sedimentation equilibrium centrifugation
127000
-
liver small form
133000
-
placenta small form, large form is converted to small form by incubation with phosphoribosyldiphosphate
170000
-
placenta large form, in the presence of AMP or GMP
172000
-
sedimentation equilibrium centrifugation in the presence of phosphoribosyldiphosphate, the sedimentation profile is influenced by phosphate, phosphoribosyldiphosphate or purine mononucleotides
180000
-
mutant unstable enzyme, gel filtration
181000
-
sedimentation equilibrium centrifugation in the presence of phosphate, the sedimentation profile is influenced by phosphate, phosphoribosyldiphosphate or purine mononucleotides
185000
-
highly concentrated enzyme solution, sucrose density gradient centrifugation, enzyme exists in equilibrium of tetramer, dimer and monomeric forms, conversion of dimer to tetramer within 10fold increase in protein concentration
194000
-
sedimentation equilibrium centrifugation
195000
-
sucrose density gradient centrifugation
270000
-
placenta, large form, small form is converted to large form by incubation with purine nucleotides, large form presumably catalytically inactive
292000
-
liver, large form
360000
-
wild-type stable enzyme, gel filtration
50000
-
2-4 * 50000, SDS-PAGE
54000
SDS-PAGE analysis of the recombinant AtGPRAT2 expressed in Escherichia coli
55000
-
x * 55000, isoform PRAT3, SDS-PAGE
56395
-
3-4 * 56395, calculated from nucleotide sequence
56700
-
x * 56700, calculated
57000
-
3-4 * 57000, SDS-PAGE
58000
-
x * 58000, SDS-PAGE
8000000
-
probably an aggregation of several purine synthetic activities, gel filtration
93000
-
sucrose density gradient centrifugation, enzyme exists in equilibrium of tetrameric, dimeric and monomeric forms
200000
-
native PAGE
200000
-
ligand-induced alteration of sedimentation coefficient and Stokes radius in the presence of phosphoribosyldiphosphate or phosphate, gel filtration and sedimentation equilibrium centrifugation
200000
-
highly concentrated enzyme solution, gel filtration, enzyme exists in equilibrium of tetrameric, dimeric and monomeric forms, conversion of dimer to tetramer within 10fold increase in protein concentration, AMP and GMP stabilize the dimeric form, GDP stabilizes the tetrameric form
215000
-
gel filtration
215000
-
only one enzyme form
additional information
-
-
additional information
-
the smaller molecular weight form of the liver enzyme is observed when incubated with purine nucleotides, the smaller one when incubated with phosphoribosyldiphosphate
additional information
-
the smaller molecular weight form of the liver enzyme is observed when incubated with purine nucleotides, the smaller one when incubated with phosphoribosyldiphosphate
additional information
-
2 molecular forms: homodimeric in the presence of 5-phospho-alpha-D-ribose 1-diphosphate, homotetrameric in the presence of purine ribonucleotides
additional information
-
partially purified enzyme shows 3 molecular forms: an inactive tetramer formed in the presence of AMP, an active dimer formed with 5-phospho-alpha-D-ribose 1-diphosphate and an inactive dimer formed with piritrexim
additional information
-
enzymes from human placenta, Chinese hamster fibroblasts and mouse liver exist in two molecular weight forms, the larger one is observed when incubated with purine nucleotides, the smaller one when incubated with phosphoribosyldiphosphate
additional information
-
enzymes from human placenta, Chinese hamster fibroblasts and mouse liver exist in two molecular weight forms, the larger one is observed when incubated with purine nucleotides, the smaller one when incubated with phosphoribosyldiphosphate
additional information
-
enzymes from human placenta, Chinese hamster fibroblasts and mouse liver exist in two molecular weight forms, the larger one is observed when incubated with purine nucleotides, the smaller one when incubated with phosphoribosyldiphosphate
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C87A
the mutant shows strongly reduced activity compared to the wild type enzyme
D432A
the mutant shows strongly reduced activity compared to the wild type enzyme
D433A
the mutant shows strongly reduced activity compared to the wild type enzyme
R264K
increased resistance to DAS734 with >500-fold higher IC50 compared to wild-type: no inhibition by 100 microM DAS734 and no effect on reaction time course, the same allosteric inhibition by adenine nucleotides as the wild-type, Arg-264 conserved in almost every GPRAT sequence
S434A
the mutant shows strongly reduced activity compared to the wild type enzyme
Y329A
the mutant shows strongly reduced activity compared to the wild type enzyme
A417W
-
moderate resistance to inhibition by ATP or GPT
D310V
-
almost resistant to inhibition by ATP or GTP, low concentrations of ATP plus GTP activate
K333Q
-
almost resistant to inhibition by ATP or GTP, low concentrations of ATP plus GTP activate
G331I
-
50% of wild-type glutaminase activity, reduced inhibition by GMP, enhanced inhibition by AMP
K326Q/P410W
-
binding of GMP and AMP is abolished resulting in loss of inhibition
L415A
mutant has reduced transfer efficiency. The L415A GPATase mutant-thioester-5'-phosphoribosylpyrophosphate complex after 39 ps, shows the leakage of ammonia into bulk solution
N351A
-
approx. 50% of wild-type glutaminase activity, completely insensitive to inhibition by GMP, partially resistent to inhibition by AMP
P410W
-
reduced inhibition by AMP, strong synergistic inhibition by AMP and GMP
R26H
-
extremely labile enzyme
Y258A
-
complete loss of glutaminase and amidotransferase activity
Y258F
-
approx. 50% loss of glutaminase activity, very weak amidotransferase activity
Y329A
-
normal glutaminase activity, approx. 20% amidotransferase activity, less sensitive to GMP inhibition than wild-type
Y465A
-
100% of wild-type glutaminase activity, 28% of wild-type amidotransferase activity, inhibition by GMP and AMP is similar to wild-type
Y74A
-
complete loss of glutaminase activity, little loss of amidotransferase activity
I198V
by missense mutation A592G, purF(I198V) and variant purF(1-04) in pCA24N by two polymerase error prone PCR strategy (1. mutazyme, 2. Taq DNA polymerase in Thermopol reaction buffer) followed by second directed mutagenesis on purF(1-04) by passaging through Escherichia coli mutator strain XL1-Red leading to variant purF(2-02), mutant I198V and variants 1-04 and 2-02 improved growth of Escherichia coli JMB9 DELTA TrpF (auxotrophic for tryptophan) on medium lacking tryptophan by gained phosphoribosylanthranilate isomerase activity
N328S
recurring mutation after error-prone PCR, found in variant 1-04 of mutant I198V which also harbours mutations: I37M, A39T, E85G, P88S, N124S, I198V, K282R and one silent, Asn328 is implicated in PRPP binding and a critical residue for improving phosphoribosylanthranilate isomerase activity. Variant 2-02 has the same open reading frame as 1-04 but optimized transcription.
additional information
-
enzyme deletion mutant, auxotrophic for adenine, produces lower levels of riboflavin than wild-type
K326Q
-
similar glutaminase and amidotransferase activity as wild-type, not inhibited by GMP
K326Q
-
insensitive to inhibition by GMP, reduced synergistic inhibition
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Caskey, C.T.; Ashton, D.M.; Wyngaarden, J.B.
The enzymology of feedback inhibition of glutamine phosphoribosylpyrophosphate amidotransferase by purine ribonucleotides
J. Biol. Chem.
239
2570-2579
1964
Columba livia, Rattus norvegicus
brenda
Hartman, S.C.; Buchanan, J.M.
Biosynthesis of purines. XXI. 5-phosphoribosylpyrophosphate amidotransferase
J. Biol. Chem.
233
451-455
1958
Columba livia
brenda
Messenger, L.J.; Zalkin, H.
Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Purification and properties
J. Biol. Chem.
254
3382-3392
1979
Escherichia coli
brenda
Wong, J.Y.; Bernlohr, D.A.; Turnbough, C.L.; Switzer, R.L.
Purification and properties of glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis
Biochemistry
20
5669-5674
1981
Bacillus subtilis
brenda
Wong, J.Y.; Switzer, R.L.
Affinity chromatography of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase
Arch. Biochem. Biophys.
196
134-137
1979
Bacillus subtilis
brenda
Liras, A.; Argomaniz, L.; Llorente, P.
Presence, preliminary properties and partial purification of 5-phosphoribosylpyrophosphate amidotransferase from Artemia sp
Biochim. Biophys. Acta
1033
114-117
1990
Artemia sp.
brenda
Tsuda, M.; Katunuma, N.; Weber, G.
Rat liver glutamine 5-phosphoribosyl-1-pyrophosphate amidotransferase [EC 2.4.2.14]. Purification and properties
J. Biochem.
85
1347-1354
1979
Rattus norvegicus
brenda
Wood, A.W.; Seegmiller, J.E.
Properties of 5-phosphoribosyl-1-pyrophosphate amidotransferase from human lymphoblasts
J. Biol. Chem.
248
138-143
1973
Homo sapiens
brenda
Bernlohr, D.A.; Switzer, R.L.
Reaction of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase with oxygen: chemistry and regulation by ligands
Biochemistry
20
5675-5681
1981
Bacillus subtilis
brenda
Holmes, E.W.
Kinetic, physical, and regulatory properties of amidophosphoribosyltransferase
Adv. Enzyme Regul.
19
215-231
1981
Bacillus subtilis, Cricetulus griseus, Columba livia, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Zalkin, H.
Structure, function, and regulation of amidophosphoribosyltransferase from prokaryotes
Adv. Enzyme Regul.
21
225-237
1983
Bacillus subtilis, Gallus gallus, Escherichia coli
brenda
Itoh, R.; Holmes, E.W.; Wyngaarden, J.B.
Pigeon liver amidophosphoribosyltransferase. Ligand-induced alterations in molecular and kinetic properties
J. Biol. Chem.
251
2234-2240
1976
Columba livia
brenda
Holmes, E.W.; McDonald, J.A.; McCord, J.M.; Wyngaarden, J.B.; Kelley, W.N.
Human glutamine phosphoribosylpyrophosphate amidotransferase. Kinetic and regulatory properties
J. Biol. Chem.
248
144-150
1973
Homo sapiens
brenda
King, G.L.; Boounous, C.G.; Holmes, E.W.
Human placental amidophosphoribosyltransferase. Comparison of the kinetics of glutamine and ammonia utilization
J. Biol. Chem.
253
3933-3938
1978
Homo sapiens
brenda
Onate, Y.A.; Vollmer, S.J.; Switzer, R.L.; Johnson, M.K.
Spectroscopic characterization of the iron-sulfur cluster in Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase
J. Biol. Chem.
264
18386-18391
1989
Bacillus subtilis
brenda
Reynoldds, P.H.S.; Blevins, D.G.; Randall, D.D.
5-Phosphoribosylpyrophosphate amidotransferase from soybean root nodules: kinetic and regulatory properties
Arch. Biochem. Biophys.
229
623-631
1984
Glycine max
brenda
Nagy, M.; Reichert, U.; Ribet, A.M.
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