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Information on EC 2.4.2.14 - amidophosphoribosyltransferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SI61

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.14 amidophosphoribosyltransferase
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9SI61 not found.
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Word Map
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Gln phosphoribosylpyrophosphate amidotransferase
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glutamine phosphoribosylpyrophosphate amidotransferase
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5'-phosphoribosylpyrophosphate amidotransferase
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-
-
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5-phosphoribosyl-1-pyrophosphate amidotransferase
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-
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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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-
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ATASE
-
-
-
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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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GPAT
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GPATase
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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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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
first step of de novo purine biosynthesis
amino group transfer
SYSTEMATIC NAME
IUBMB Comments
5-phospho-beta-D-ribosylamine:diphosphate phospho-alpha-D-ribosyltransferase (glutamate-amidating)
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CAS REGISTRY NUMBER
COMMENTARY hide
9031-82-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[4Fe-4S]-center
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
5 mM used in assay conditions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
DAS734
purine nucleotide
allosteric feedback inhibition by end products of the purine biosynthesis pathway, act on the PRPP domain
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additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005293
DAS734
at pH 7.8, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0002
DAS734
additional information
DAS734
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform AtGPRAT1
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ASE1_ARATH
566
0
61842
Swiss-Prot
Chloroplast (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
SDS-PAGE analysis of the recombinant AtGPRAT2 expressed in Escherichia coli
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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)
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team