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EC Tree
The taxonomic range for the selected organisms is: Arabidopsis thaliana The enzyme appears in selected viruses and cellular organisms
Synonyms
amidophosphoribosyltransferase, glutamine phosphoribosylpyrophosphate amidotransferase, phosphoribosyl pyrophosphate amidotransferase, amido phosphoribosyltransferase, phosphoribosylamidotransferase, 5-phosphoribosyl-1-pyrophosphate amidotransferase, gpatase, glutamine phosphoribosyl pyrophosphate amidotransferase, phosphoribosyl amidotransferase, gprat,
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Gln phosphoribosylpyrophosphate amidotransferase
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glutamine phosphoribosylpyrophosphate amidotransferase
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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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Gln phosphoribosylpyrophosphate amidotransferase
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glutamine 5-phosphoribosylpyrophosphate amidotransferase
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glutamine phosphoribosylpyrophosphate amidotransferase
glutamine ribosylpyrophosphate 5-phosphate amidotransferase
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phosphoribose pyrophosphate amidotransferase
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phosphoribosyl pyrophosphate amidotransferase
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phosphoribosyldiphosphate 5-amidotransferase
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phosphoribosylpyrophosphate glutamyl amidotransferase
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glutamine phosphoribosylpyrophosphate amidotransferase
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glutamine phosphoribosylpyrophosphate amidotransferase
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glutamine phosphoribosylpyrophosphate amidotransferase
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amino group transfer
first step of de novo purine biosynthesis
amino group transfer
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amino group transfer
first step of de novo purine biosynthesis
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5-phospho-beta-D-ribosylamine:diphosphate phospho-alpha-D-ribosyltransferase (glutamate-amidating)
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L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
additional information
?
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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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L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
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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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additional information
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no GPRAT activity detectable in cell extracts of recombinant AtGPRAT1 expressing Escherichia coli
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additional information
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no GPRAT activity detectable in cell extracts of recombinant AtGPRAT1 expressing Escherichia coli
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additional information
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no GPRAT activity detectable in cell extracts of recombinant AtGPRAT1 expressing Escherichia coli
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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
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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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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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Mg2+
5 mM used in assay conditions
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6-diazo-5-oxo-L-norleucine
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adenine nucleotide
maximal inhibition by combination of adenine nucleotides (in total 10 mM), inhibitory effect of single nucleotides (5 mM) increases in the order AMP, ATP, ADP
purine nucleotide
allosteric feedback inhibition by end products of the purine biosynthesis pathway, act on the PRPP domain
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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
DAS734
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
additional information
minimal inhibition by inosine monophosphate (IMP) and guanosine monophosphate (GMP)
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additional information
minimal inhibition by inosine monophosphate (IMP) and guanosine monophosphate (GMP)
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additional information
minimal inhibition by inosine monophosphate (IMP) and guanosine monophosphate (GMP)
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0.35
5-phospho-alpha-D-ribose 1-diphosphate
at pH 7.8, temperature not specified in the publication
1.34
L-glutamine
cell extracts of recombinant AtGPRAT2 expressing Escherichia coli
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0.005293
DAS734
at pH 7.8, temperature not specified in the publication
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additional information
DAS734
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
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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isoform AtGPRAT1
UniProt
brenda
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brenda
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ASE1_ARATH
566
0
61842
Swiss-Prot
Chloroplast (Reliability: 1 )
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54000
SDS-PAGE analysis of the recombinant AtGPRAT2 expressed in Escherichia coli
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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
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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
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from bacterial extracts by desalting on a Bio-Rad 10DG column in presence of 10 mM dithiothreitol, stored at -70°C
Ni-affinity column chromatography
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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)
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)
expressed in Escherichia coli BL21 cells
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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
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