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EC Tree
The taxonomic range for the selected organisms is: Homo sapiens 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
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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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amido phosphoribosyltransferase
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amidotransferase, phosphoribosyl pyrophosphate
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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 amidotransferase
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phosphoribosyl pyrophosphate amidotransferase
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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GPAT
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phosphoribosyl pyrophosphate amidotransferase
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phosphoribosyl pyrophosphate amidotransferase
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amino group transfer
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5-phospho-beta-D-ribosylamine:diphosphate phospho-alpha-D-ribosyltransferase (glutamate-amidating)
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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 + 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
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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?
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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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
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
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regulating enzyme of purine biosynthesis
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?
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
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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
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NH3-binding site is distinct from glutamine-site
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?
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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
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
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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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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
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regulating enzyme of purine biosynthesis
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?
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Ca2+
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activation, approx. 15% as effective as Mg2+ or Mn2+
Co2+
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activation, approx. 40% as effective as Mg2+ or Mn2+
Fe
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enzyme contains a [4Fe-4S] cluster
Mn2+
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required, equally effective as Mg2+
Mg2+
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required
Mg2+
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Km-value: 0.65 mM, inhibition above 10 mM
Mg2+
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maximal activation at concentrations 2.5-5 times higher than that of the corresponding 5-phospho-alpha-D-ribose 1-diphosphate concentration
additional information
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4Fe-4S-cluster
additional information
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not activated by Ba2+, Cd2+, Cu2+, Fe2+, Hg2+, Ni2+, Zn2+
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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
5-((4-carboxy-4-(4-(((2,4-diaminopyrido[3,2-d]pyrimidine-6-yl)methyl)amino)benzamido)butyl)carbamoyl)isophthalic acid
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6-diazo-5-oxo-L-norleucine
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competitive vs. glutamine, inactivation half-life: 11 min
6-iodopurine
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5 mM, 39% inhibition
6-mercaptopurine ribonucleotide
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5 mM, 64% inhibition
ADP
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5 mM, 40% inhibition
allopurinol ribonucleotide
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5 mM, 68% inhibition
ATP
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5 mM, 21% inhibition
azaserine
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competitive vs. glutamine, inactivation half-life: 12 min
cAMP
competitive inhibitor
cGMP
competitive inhibitor
CMP
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5 mM, 22% inhibition
dCMP
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5 mM, 26% inhibition
GDP
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5 mM, 40% inhibition
GTP
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5 mM, 13% inhibition
IDP
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5 mM, 29% inhibition
IMP
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5 mM, 41% inhibition
methyl-dCMP
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5 mM, 47% inhibition
NH3
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inhibition of amidotransferase activity
OMP
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5 mM, 25% inhibition
phosphate
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competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate
TMP
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5 mM, 42% inhibition
TTP
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5 mM, 12% inhibition
UDP
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5 mM, 19% inhibition
UMP
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5 mM, 25% inhibition
UTP
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5 mM, 16% inhibition
XDP
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5 mM, 27% inhibition
XMP
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5 mM, 41% inhibition
XTP
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5 mM, 44% inhibition
AMP
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1.8 mM, 50% inhibition
AMP
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5 mM, 76% inhibition, noncompetive vs. glutamine
AMP
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5 mM, 79% and 24% inhibition of aminotransferase and amidotransferase activity at 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
GMP
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0.5 mM; 50% inhibition
GMP
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0.5 mM; 5 mM, 70% inhibition
GMP
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0.5 mM; 5 mM, 56% and 12% inhibition of aminotransferase and amidotransferase activity at 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
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Mg-phosphoribosyldiphosphate
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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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0.14 - 0.48
5-phospho-alpha-D-ribose 1-diphosphate
additional information
additional information
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0.14 - 0.48
5-phospho-alpha-D-ribose 1-diphosphate
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0.47
5-phospho-alpha-D-ribose 1-diphosphate
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adenocarcinoma 755
0.48
5-phospho-alpha-D-ribose 1-diphosphate
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in Tris buffer
1 - 4.5
L-glutamine
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1.8
L-glutamine
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adenocarcinoma 755
additional information
additional information
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kinetic properties of amido- and aminotransferase activity
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additional information
additional information
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effect of AMP on kinetic parameters
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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
0.0034
6-diazo-5-oxo-L-norleucine
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0.00131
AMP
pH and temperature not specified in the publication
0.00174
lomexterol
pH and temperature not specified in the publication
0.01074
methotrexate
pH and temperature not specified in the publication
0.00528
pipretixin
pH and temperature not specified in the publication
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6 - 8
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broad, phosphate buffer
6.5
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imidazole/HCl buffer
6.8 - 7.4
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Tris/HCl buffer preferred
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brenda
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UniProt
brenda
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brenda
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adenocarcinoma 755
brenda
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brenda
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brenda
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diploid wild 2 line, tissue culture
brenda
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brenda
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little or no activity in mitochondria or microsomes
brenda
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brenda
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physiological function
the enzyme is critical for lung cancer cell proliferation and invasion
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PUR1_HUMAN
517
0
57399
Swiss-Prot
other Location (Reliability: 2 )
Q53H22_HUMAN
517
0
57385
TrEMBL
other Location (Reliability: 2 )
A8K4H7_HUMAN
517
0
57399
TrEMBL
other Location (Reliability: 2 )
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133000
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placenta small form, large form is converted to small form by incubation with phosphoribosyldiphosphate
170000
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placenta large form, in the presence of AMP or GMP
270000
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placenta, large form, small form is converted to large form by incubation with purine nucleotides, large form presumably catalytically inactive
additional information
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2 molecular forms: homodimeric in the presence of 5-phospho-alpha-D-ribose 1-diphosphate, homotetrameric in the presence of purine ribonucleotides
additional information
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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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60
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at least 15 min stable
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Mg2+ and phosphate are essential for stability
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oxygen sensitive enzyme
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489754
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-20°C or 4°C, cell-free extract, overnight, more than 50% loss of activity
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-20°C, crude, more than 50% loss of activity overnight
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4°C, 50 mM phosphate bufer, pH 7.4, 5 mM MgCl2, 60 mM 2-mercaptoethanol, at least 4 weeks, no loss of activity
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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
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4°C, phosphate buffer, 10 d, 40% loss of activity
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DEAE-cellulose, partial purification
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expression of wild-type and K338Q/P422W mutant enzyme in amidophosphoribosyltransferase deficient CHO ade -A cells and in transgenic mice
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increased enzyme expression correlates with aggressive lung cancer. L-glutamine induces enzyme expression
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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
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
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
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
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
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