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Information on EC 2.4.2.14 - amidophosphoribosyltransferase
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2.4.2.14 amidophosphoribosyltransferaseSpecify your search results
Word Map
- 2.4.2.14
- purine
-
phosphoribosylamine
-
glutamine-dependent
- glycinamide
- 6-diazo-5-oxo-l-norleucine
-
14cglycine
-
pp-ribose-p
- acivicin
- phosphoribosyltransferases
- ribotide
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p-rib-pp
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
amidophosphoribosyltransferase, glutamine phosphoribosylpyrophosphate amidotransferase, phosphoribosyl pyrophosphate amidotransferase, amido phosphoribosyltransferase, 5-phosphoribosyl-1-pyrophosphate amidotransferase, phosphoribosylamidotransferase, gpatase, glutamine phosphoribosyl pyrophosphate amidotransferase, phosphoribosyl amidotransferase, gprat, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-phosphoribosylpyrophosphate amidotransferase
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5-phosphoribosyl-1-pyrophosphate amidotransferase
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5-phosphoribosylpyrophosphate amidotransferase
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5-phosphororibosyl-1-pyrophosphate amidotransferase
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alpha-5-phosphoribosyl-1-pyrophosphate amidotransferase
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amidotransferase, phosphoribosyl pyrophosphate
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ATASE
Gln phosphoribosylpyrophosphate amidotransferase
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glutamine 5-phosphoribosylpyrophosphate amidotransferase
glutamine phosphoribosylpyrophosphate amidotransferase
glutamine ribosylpyrophosphate 5-phosphate amidotransferase
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GPAT
GPATase
phosphoribose pyrophosphate amidotransferase
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phosphoribosyl pyrophosphate amidotransferase
phosphoribosylamidotransferase
phosphoribosyldiphosphate 5-amidotransferase
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phosphoribosylpyrophosphate glutamyl amidotransferase
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PurF
ATASE
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glutamine 5-phosphoribosylpyrophosphate amidotransferase
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glutamine phosphoribosylpyrophosphate amidotransferase
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GPAT
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GPATase
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phosphoribosyl pyrophosphate amidotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
binding of 5-phospho-alpha-D-ribose 1-diphosphate activates the enzyme by a structural change that lowers the Km for glutamine 100fold and couples glutamine hydrolysis to synthesis of 5-phospho-beta-D-ribosylamine
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5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
mechanism of glutamine amide transfer
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5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
mechanism of glutamine amide transfer
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5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
amino group transfer
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amino group transfer
first step of de novo purine biosynthesis
amino group transfer
first step of de novo purine nucleotide biosynthesis
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
5-phospho-beta-D-ribosylamine:diphosphate phospho-alpha-D-ribosyltransferase (glutamate-amidating)
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CAS REGISTRY NUMBER
COMMENTARY
9031-82-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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)
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?
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
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-
-
?
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
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-
-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
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-
-
-
r
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
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-
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?
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
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-
?
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
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
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-
-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
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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
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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ir
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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reaction at 70% the rate of aminotransferase activity
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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ir
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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reaction at 50% the rate of aminotransferase activity
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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no activity with carbamoyl phosphate
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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glutamine binding site distinct from NH3-site
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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reaction at 33% the rate of amminotransferase activity
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
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-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
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first reaction in de-novo pathway of purine biosynthesis
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?
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
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?
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
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?
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
-
-
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?
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
rate-limiting enzyme of purine biosynthesis
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?
L-glutamine + H2O
L-glutamate + NH3
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enzyme exhibits glutaminase activity in the absence of other substrates or effectors
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?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
lower aminotransferase activity compared to amidotransferase activity
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?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
-
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?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
no activity with NH4+
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?
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
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?
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
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?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
3fold higher aminotransferase activity compared to amidotransferase activity
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?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
-
NH3-binding site is distinct from glutamine-site
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?
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
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-
?
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Mg2+
additional information
Fe
-
low temperature magnetic circular dichroism, electron paramagnetic resonance and resonance Raman spectroscopy of oxidized and reduced [4Fe-4S] cluster, native enzyme contains an [4Fe-4S]2+ cluster
Fe
-
iron-sulfur center can be removed with 1,10-phenanthroline, resulting apoprotein is devoid of amino- and amidotransferase activity
Mg2+
-
5-phospho-alpha-D-ribose 1-diphosphate-Mg3- is the reactive molecular species
Mg2+
-
maximal activation at concentrations 2.5-5 times higher than that of the corresponding 5-phospho-alpha-D-ribose 1-diphosphate concentration
additional information
-
low temperature magnetic circular dichroism, electron paramagnetic resonance and resonance Raman spectroscopy
additional information
-
S2- is oxidized by O2 to a mixture of sulfur oxides bound as thiocysteine and yet unidentified products
additional information
-
prototype for a metal-free amidophosphoribosyltransferase
additional information
-
non-heme iron is not present in significant amounts
additional information
-
non-heme iron is not present in significant amounts
additional information
-
not activated by Ba2+, Cd2+, Cu2+, Fe2+, Hg2+, Ni2+, Zn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
-
approx. 60% inactivation of amidotransferase activity after 30 min, very weak inactivation of NH3-dependent activity
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
-
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
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
-
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
-
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
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
-
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
-
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
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)
-
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
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphoribosyl-5-phosphate
-
3-4fold activation of glutaminase activity in the presence of phosphate or diphosphate
Mg-phosphoribosyldiphosphate
-
no glutamine-binding site in the absence of Mg-phosphoribosyldiphosphate
Mg-phosphoribosyldiphosphate
-
requirement, phosphoribosyldiphosphate-Mg3- is the reactive molecular species of phosphoribosyldiphosphate, Km-value: 0.62 mM
additional information
-
complex allosteric enzyme whose activity is regulated by a series of conformational changes induced by a number of ligands
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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, 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
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
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.
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
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
193
glutamine
-
5-phospho-alpha-D-ribose 1-diphosphate-independent glutamine hydrolysis
0.35
5-phospho-alpha-D-ribose 1-diphosphate
at pH 7.8, temperature not specified in the publication
0.64
L-glutamine
-
N101G mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity
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
2.43
L-glutamine
-
G102A mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase 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
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
phosphoribosylanthranilate
mutant I198V, modestly higher rate than spontaneous substrate hydrolysis of <1/h
additional information
phosphoribosylanthranilate
variant 1-04, 25 to 30-fold more active than mutant I198V but 2.3*10(7)-fold less efficient than phosphoribosylanthranilate isomerase
additional information
phosphoribosylanthranilate
variant 1-04, conversion of 5.5% of available substrate, 22 turnovers per active site
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.053 - 0.058
1-alpha-diphosphoryl-2-alpha,3-alpha-dihydroxy-4-beta-cyclopentane-methanol-5-phosphate
0.02327
2,4-diamino-6-(3,4,5-trimethoxyanilino)-methylpyrido[3,2-d]pyrimidine
pH and temperature not specified in the publication
0.00331
2,4-diamino-6-(3,4,5-trimethoxybenzyl)-5,6,7,8-tetrahydro-quinazoline
pH and temperature not specified in the publication
0.1167
5-((4-carboxy-4-(4-(((2,4-diaminopyrido[3,2-d]pyrimidine-6-yl)methyl)amino)benzamido)butyl)carbamoyl)isophthalic acid
pH and temperature not specified in the publication
0.005293
DAS734
at pH 7.8, temperature not specified in the publication
0.053
1-alpha-diphosphoryl-2-alpha,3-alpha-dihydroxy-4-beta-cyclopentane-methanol-5-phosphate
-
P410W mutant enzyme
0.058
1-alpha-diphosphoryl-2-alpha,3-alpha-dihydroxy-4-beta-cyclopentane-methanol-5-phosphate
-
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
5',5'-P1,P4-diguanosine tetraphosphate
Artemia sp.
-
IC50: 0.4 mM, 2 mM, approx. 80% inhibition
0.0002
DAS734
Arabidopsis thaliana
10 min preincubation of recombinant enzyme with inhibitor leads to maximum inhibition, slow but reversible binding
0.0002
DAS734
Arabidopsis thaliana
cell extracts of recombinant AtGPRAT3 expressing Escherichia coli
additional information
DAS734
Arabidopsis thaliana
>500-fold higher for mutant R264K compared to wild-type
additional information
DAS734
Arabidopsis thaliana
>500-fold higher for mutant R264K compared to wild-type
additional information
DAS734
Arabidopsis thaliana
>500-fold higher for mutant R264K compared to wild-type
additional information
DAS734
Arabidopsis thaliana
20-35 microM leads to 50% inhibition of Arabidopsis root growth (RI50) at in presence of endogenous AtGPRAT2 harbouring R264K polymorphism
additional information
DAS734
Arabidopsis thaliana
20-35 microM leads to 50% inhibition of Arabidopsis root growth (RI50) at in presence of endogenous AtGPRAT2 harbouring R264K polymorphism
additional information
DAS734
Arabidopsis thaliana
20-35 microM leads to 50% inhibition of Arabidopsis root growth (RI50) at in presence of endogenous AtGPRAT2 harbouring R264K polymorphism
additional information
DAS734
Arabidopsis thaliana
200 nM leads to 50% inhibition of Arabidopsis root growth (RI50) in wild-type AtGPRAT2 expressing seedlings
additional information
DAS734
Arabidopsis thaliana
200 nM leads to 50% inhibition of Arabidopsis root growth (RI50) in wild-type AtGPRAT2 expressing seedlings
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
assay method to measure both amidotransferase and aminotransferase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.5
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
-
stable enzyme, approx. 65% and unstable enzyme approx. 70% of maximal activity at pH 7, stable enzyme, approx. 75% and unstable enzyme approx. 65% of maximal activity at pH 9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
brine shrimp, activity increases 7fold during early larval development in 2 d old Artemia
-
-
brenda
no activity in Salmonella sp.
Salmonella enterica strain DM1936, lacking purF gene product, purF2085
-
-
brenda
wild type strain 972h- and mutant strain ade 2h- devoid of adenylosuccinate synthase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
isoform PRAT3 is essential for the synthesis of ureides in Phaseolus vulgaris nodules
physiological function
physiological function
the enzyme is critical for lung cancer cell proliferation and invasion
Show AA Sequence and Transmembrane Helices (40826 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
133000
-
placenta small form, large form is converted to small form by incubation with phosphoribosyldiphosphate
172000
-
sedimentation equilibrium centrifugation in the presence of phosphoribosyldiphosphate, the sedimentation profile is influenced by phosphate, phosphoribosyldiphosphate or purine mononucleotides
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
200000
215000
270000
-
placenta, large form, small form is converted to large form by incubation with purine nucleotides, large form presumably catalytically inactive
54000
SDS-PAGE analysis of the recombinant AtGPRAT2 expressed in Escherichia coli
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
additional information
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
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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.1 M sodium citrate tribasic pH 5.6, 1.5 M ammonium phosphate monobasic, and 0.1 M citric acid pH 3.4
when mapped onto the structure from Bacillus subtilis GPRAT (PDB: 1AO0), the site of mutation R264K lies within 10 A of the glutaminase site
crystals of the ternary enzyme-ADP-GMP complex are grown in glass melting point capillaries by the microbath method, 20 mg/ml enzyme are incubated with 1 mM ADP, 1 mM GMP, and 5 mM MgCl2 and mixed with an equal volume of 24% polyethylene glycol 8000, 200 mM KCl, 50 mM N-(2-hydroxyethyl)piperazine-N'-3-propanesulfonic acid, pH 7.9, brown crystals emerge after 6-12 weeks
crystal structure in the absence of ligands at 2.0 A, and with bound AMP at 2.5 A
-
crystal structure of 6-diazo-5-oxonorleucine inactivated enzyme at 2.3 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48
-
wild-type, stable enzyme from cells of mid-exponential growth phase, t1/2: 34 min, from cells of stationary growth phase, t1/2: 2-5 min, mutant enzyme, t1/2: 2 min, in the presence of ADP or adenosine 3 min, and 4 min in the presence of IMP
60
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ADP or ADP and GMP, ratio 1/1, stabilize equilibrium between dimeric and tetrameric form
-
phosphoribosyldiphosphate and other nucleotides antagonize stabilizing effect of AMP
-
stability profile depends on growth rate and growth phase of cell culture, PMSF improves stability
-
stable during all stages of purification provided thiols and oxygen are avoided
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
anaerobic conditions stabilize
in vitro O2 oxidizes iron in the Fe-S cluster to the high spin ferric state and sulfur to a mixtur of S in thiocystine residues plus other unidentified products
-
489755
low concentrations of thiols e.g. dithiothreitol or 2-mercaptoethanol accelerate aerobic inactivation
-
489747
O2, rather than peroxide, superoxide, hydroxyl radical or singlet oxygen, inactivates, allosteric inhibitors, such as AMP, ADP, GMP or GDP modulate the rate of inactivation
-
489753
oxygen sensitive enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol and phosphoribosyldiphosphate stabilize during storage at 4°C
-
3°C, crude mutant enzyme extract, inactivation overnight, partially purified mutant enzyme: inactivation within 72 h, PMSF stabilizes
-
3°C, crude or partially purified wild-type enzyme, at least 72 h stable
-
4°C, 50 mM phosphate bufer, pH 7.4, 5 mM MgCl2, 60 mM 2-mercaptoethanol, at least 4 weeks, no loss of activity
-
4°C, in phosphate buffer, pH 7.4, 60 mM 2-mercaptoethanol and phosphoribosyldiphosphate, at least 10 days
-
4°C, partially purified preparation in 50 mM phosphate buffer, pH 7.4, 5 mM Mg2+ and 60 mM 2-mercaptoethanol, at least 4 weeks
-
storage in 25 mM Tris buffer inactivates with 26% or 4% residual activity after 6 or 10 days, respectively
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, heat treatment, DEAE-Sepharose, Blue Dextran-Sepharose, hydroxylapatite
-
from bacterial extracts by desalting on a Bio-Rad 10DG column in presence of 10 mM dithiothreitol, stored at -70°C
heat treatment, acid precipitation, ammonium sulfate, ethanol, Sephadex G-150, DE-52
-
hexa-His-tagged mutant I198V and its variant 1-04 by metal affinity chromatography in presence of 1 mM beta-mercaptoethanol and 10% (v/v) glycerol, elution with 250 mM imidazole followed by dialysis
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplified from seedling cDNA library to encode 11-amino acid autoprocessing propeptide, N-terminal cysteine for an active enzyme and deleted chloroplast transit peptide, in pCR2.1TOPO for sequencing, in pET26b for expression in Escherichia coli BL21(DE3)
expression in Escherichia coli
expression of wild-type and K338Q/P422W mutant enzyme in amidophosphoribosyltransferase deficient CHO ade -A cells and in transgenic mice
-
expression of wild-type, Y74A, Y258A, Y258F, K326Q, Y329A, G331I, N351A and Y465A mutant enzyme in Escherichia coli
-
wildtype, mutant I198V and variants 1-04 and 2-02 of mutant I198V in pCA24N for expression as N-terminal hexa-His-tagged, C-terminal GFP-tagged proteins in Escherichia coli JMB9 DELTA TrpF (auxotrophic for tryptophan) and/or Escherichia coli KK8(pDM), mutant I198V in pCDF-1b for error-prone PCR based mutagenesis yielding variant 1-04
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased enzyme expression correlates with aggressive lung cancer. L-glutamine induces enzyme expression
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
marginal secondary enzyme activities can dramatically improve the fitness of contemporary organisms
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
Regulation of purine metabolism in Schizosaccharomyces pombe. IV. Variations in the stability and kinetic parameters of amidophosphoribosyltransferase depending on growth phase and growth conditions
Biochim. Biophys. Acta
370
85-95
1974
Schizosaccharomyces pombe
brenda
Itoh, R.; Gorai, I.; Usami, C.; Tsushima, K.
Chicken liver amidophosphoribosyltransferase. Ligand-induced alterations in molecular properties
Biochim. Biophys. Acta
581
142-152
1979
Gallus gallus
brenda
Zhou, G.; Charbonneau, H.; Colman, R.F.; Zalkin, H.
Identification of sites for feedback regulation of glutamine 5-phosphoribosylpyrophosphate amidotransferase by nucleotides and relationship to residues important for catalysis
J. Biol. Chem.
268
10471-10481
1993
Escherichia coli
brenda
Taha, T.S.; Deits, T.L.
Detection of glycinamide ribonucleotide by HPLC with pulsed amperometry: application to the assay for glutamine: 5-phosphoribosyl-1-pyrophosphate amidotransferase (EC 2.4.2.14)
Anal. Biochem.
213
323-328
1993
Glycine max
brenda
Zhou, G.; Smith, J.L.; Zalkin, H.
Binding of purine nucleotides to two regulatory sites results in synergistic feedback inhibition of glutamine 5-phosphoribosylpyrophosphate amidotransferase
J. Biol. Chem.
269
6784-6789
1994
Escherichia coli
brenda
Kim, J.H.; Wolle, D.; Haridas, K.; Parry, R.J.; Smith, J.L.; Zalkin, H.
A stable carbocyclic analog of 5-phosphoribosyl-1-pyrophosphate to probe the mechanism of catalysis and regulation of glutamine phosphoribosylpyrophosphate amidotransferase
J. Biol. Chem.
270
17394-17399
1995
Escherichia coli
brenda
Kim, J.H.; Krahn, J.M.; Tomchick, D.R.; Smith, J.L.; Zalkin, H.
Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site
J. Biol. Chem.
271
15549-15557
1996
Escherichia coli
brenda
Schoettle, S.L.; Crisp, L.B.; Szabados, E.; Christopherson, R.I.
Mechanisms of inhibition of amido phosphoribosyltransferase from mouse L1210 leukemia cells
Biochemistry
36
6377-6383
1997
Mus musculus
brenda
Chen, S.; Tomchick, D.R.; Wolle, D.; Hu, P.; Smith, J.L.; Switzer, R.L.; Zalkin, H.
Mechanism of the synergistic end-product regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase by nucleotides
Biochemistry
36
10718-10726
1997
Bacillus subtilis (P00497), Bacillus subtilis
brenda
Muchmore, C.R.; Krahn, J.M.; Kim, J.H.; Zalkin, H.; Smith, J.L.
Crystal structure of glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli
Protein Sci.
7
39-51
1998
Bacillus subtilis, Escherichia coli
brenda
Kian, I.A.; Etingof, R.N.
Purine biosynthesis de novo in bovine retina: purification and characterization of amidophosphoribosyl transferase and phosphoribosyl pyrophosphate synthetase
Biochemistry
64
648-651
1999
Bos taurus
brenda
Bera, A.K.; Chen, S.; Smith, J.L.; Zalkin, H.
Temperature-dependent function of the glutamine phosphoribosylpyrophosphate amidotransferase ammonia channel and coupling with glycinamide ribonucleotide synthetase in a hyperthermophile
J. Bacteriol.
182
3734-3739
2000
Aquifex aeolicus
brenda
Yamaoka, T.; Yano, M.; Kondo, M.; Sasaki, H.; Hino, S.; Katashima, R.; Moritani, M.; Itakura, M.
Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses
J. Biol. Chem.
276
21285-21291
2001
Homo sapiens
brenda
Jimenez, A.; Santos, M.A.; Pompejus, M.; Revuelta, J.L.
Metabolic engineering of the purine pathway for riboflavin production in Ashbya gossypii
Appl. Environ. Microbiol.
71
5743-5751
2005
Eremothecium gossypii
brenda
Browne, B.A.; Ramos, A.I.; Downs, D.M.
PurF-independent phosphoribosyl amine formation in yjgF mutants of Salmonella enterica utilizes the tryptophan biosynthetic enzyme complex anthranilate synthase-phosphoribosyltransferase
J. Bacteriol.
188
6786-6792
2006
Salmonella enterica
brenda
Koenigsknecht, M.J.; Ramos, I.; Downs, D.M.
Glutamine phosphoribosylpyrophosphate amidotransferase-independent phosphoribosyl amine synthesis from ribose 5-phosphate and glutamine or asparagine
J. Biol. Chem.
282
28379-28384
2007
no activity in Escherichia coli, no activity in Salmonella sp., no activity in Escherichia coli DM1293
brenda
Patrick, W.M.; Matsumura, I.
A study in molecular contingency: glutamine phosphoribosylpyrophosphate amidotransferase is a promiscuous and evolvable phosphoribosylanthranilate isomerase
J. Mol. Biol.
377
323-336
2008
Escherichia coli K-12 (P0AG16)
brenda
Walsh, T.A.; Bauer, T.; Neal, R.; Merlo, A.O.; Schmitzer, P.R.; Hicks, G.R.; Honma, M.; Matsumura, W.; Wolff, K.; Davies, J.P.
Chemical genetic identification of glutamine phosphoribosylpyrophosphate amidotransferase as the target for a novel bleaching herbicide in Arabidopsis
Plant Physiol.
144
1292-1304
2007
Arabidopsis thaliana (Q9SI61), Arabidopsis thaliana (Q9STG9), Arabidopsis thaliana (Q9T0J5)
brenda
Wang, X.S.; Roitberg, A.E.; Richards, N.G.
Computational studies of ammonia channel function in glutamine 5-phosphoribosylpyrophosphate amidotransferase
Biochemistry
48
12272-12282
2009
Escherichia coli (P0AG16), Escherichia coli
brenda
Qin, L.; Gong, X.; Xie, J.; Jiang, D.; Cheng, J.; Li, G.; Huang, J.; Fu, Y.
Phosphoribosylamidotransferase, the first enzyme for purine de novo synthesis, is required for conidiation in the sclerotial mycoparasite Coniothyrium minitans
Fungal Genet. Biol.
48
956-965
2011
Paraphaeosphaeria minitans (F2XMV3), Paraphaeosphaeria minitans, Paraphaeosphaeria minitans ZS-1 (F2XMV3)
brenda
Batool, S.; Nawaz, M.S.; Kamal, M.A.
In silico analysis of the amido phosphoribosyltransferase inhibition by PY873, PY899 and a derivative of isophthalic acid
Invest. New Drugs
31
1355-1363
2013
Homo sapiens (Q06203), Homo sapiens
brenda
Goswami, M.; Chen, G.; Chakravarthi, B.; Pathi, S.; Anand, S.; Carskadon, S.; Giordano, T.; Chinnaiyan, A.; Thomas, D.; Palanisamy, N.; Beer, D.; Varambally, S.
Role and regulation of coordinately expressed de novo purine biosynthetic enzymes PPAT and PAICS in lung cancer
Oncotarget
6
23445-23461
2015
Homo sapiens (Q06203)
brenda
Coleto, I.; Trenas, A.T.; Erban, A.; Kopka, J.; Alamillo, M.P.
Functional specialization of one copy of glutamine phosphoribosyl pyrophosphate amidotransferase in ureide production from symbiotically fixed nitrogen in Phaseolus vulgaris
Plant Cell Environ.
39
1767-1779
2016
Phaseolus vulgaris
brenda
Bibi, N.; Parveen, Z.; Nawaz, M.S.; Kamal, M.A.
In silico structure modeling and molecular docking analysis of phosphoribosyl pyrophosphate amidotransferase (PPAT) with antifolate inhibitors
Curr. Cancer Drug Targets
19
408-416
2019
Homo sapiens (Q06203), Homo sapiens
brenda
Cao, X.; Du, B.; Han, F.; Zhou, Y.; Ren, J.; Wang, W.; Chen, Z.; Zhang, Y.
Crystal structure of the chloroplastic glutamine phosphoribosylpyrophosphate amidotransferase GPRAT2 from Arabidopsis thaliana
Front. Plant Sci.
11
157
2020
Arabidopsis thaliana (Q9STG9), Arabidopsis thaliana
brenda
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