Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.4.2.14 - amidophosphoribosyltransferase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC2.4.2.14
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.14 amidophosphoribosyltransferase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-phosphoribosylpyrophosphate amidotransferase
-
-
-
-
5-phosphoribosyl-1-pyrophosphate amidotransferase
-
-
-
-
5-phosphoribosylpyrophosphate amidotransferase
-
-
-
-
5-phosphororibosyl-1-pyrophosphate amidotransferase
-
-
-
-
alpha-5-phosphoribosyl-1-pyrophosphate amidotransferase
-
-
-
-
amido phosphoribosyltransferase
-
amidotransferase, phosphoribosyl pyrophosphate
-
-
-
-
ATASE
-
-
-
-
glutamine 5-phosphoribosylpyrophosphate amidotransferase
-
-
-
-
glutamine phosphoribosylpyrophosphate amidotransferase
glutamine ribosylpyrophosphate 5-phosphate amidotransferase
-
-
-
-
GPATase
-
-
-
-
phosphoribose pyrophosphate amidotransferase
-
-
-
-
phosphoribosyl amidotransferase
-
phosphoribosyl pyrophosphate amidotransferase
phosphoribosyldiphosphate 5-amidotransferase
-
-
-
-
phosphoribosylpyrophosphate glutamyl amidotransferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
5-phospho-beta-D-ribosylamine:diphosphate phospho-alpha-D-ribosyltransferase (glutamate-amidating)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9031-82-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
show the reaction diagram
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
show the reaction diagram
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
show the reaction diagram
NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
5-phospho-beta-D-ribosylamine + diphosphate
show the reaction diagram
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
5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
show the reaction diagram
L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activation, approx. 15% as effective as Mg2+ or Mn2+
Co2+
-
activation, approx. 40% as effective as Mg2+ or Mn2+
Fe
-
enzyme contains a [4Fe-4S] cluster
Mn2+
-
required, equally effective as Mg2+
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
6-diazo-5-oxo-L-norleucine
-
competitive vs. glutamine, inactivation half-life: 11 min
6-iodopurine
-
5 mM, 39% inhibition
6-mercaptopurine ribonucleotide
-
5 mM, 64% inhibition
ADP
-
5 mM, 40% inhibition
allopurinol ribonucleotide
-
5 mM, 68% inhibition
ATP
-
5 mM, 21% inhibition
azaserine
-
competitive vs. glutamine, inactivation half-life: 12 min
cAMP
competitive inhibitor
cGMP
competitive inhibitor
CMP
-
5 mM, 22% inhibition
dCMP
-
5 mM, 26% inhibition
GDP
-
5 mM, 40% inhibition
GTP
-
5 mM, 13% inhibition
IDP
-
5 mM, 29% inhibition
IMP
-
5 mM, 41% inhibition
lomexterol
-
methotrexate
-
methyl-dCMP
-
5 mM, 47% inhibition
NH3
-
inhibition of amidotransferase activity
OMP
-
5 mM, 25% inhibition
phosphate
-
competitive vs. 5-phospho-alpha-D-ribose 1-diphosphate
pipretixin
-
TMP
-
5 mM, 42% inhibition
TTP
-
5 mM, 12% inhibition
UDP
-
5 mM, 19% inhibition
UMP
-
5 mM, 25% inhibition
UTP
-
5 mM, 16% inhibition
XDP
-
5 mM, 27% inhibition
XMP
-
5 mM, 41% inhibition
XTP
-
5 mM, 44% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mg-phosphoribosyldiphosphate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14 - 0.48
5-phospho-alpha-D-ribose 1-diphosphate
1 - 4.5
L-glutamine
0.65
Mg2+
-
-
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
-
0.00131
AMP
pH and temperature not specified in the publication
4
azaserine
-
-
0.00174
lomexterol
pH and temperature not specified in the publication
0.01074
methotrexate
pH and temperature not specified in the publication
3.3
NH3
-
-
0.00528
pipretixin
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.001
-
L-glutamine
0.00125 - 0.0014
-
-
0.00297
-
NH3
0.0055
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
broad, phosphate buffer
6.5
-
imidazole/HCl buffer
6.8 - 7.4
-
Tris/HCl buffer preferred
7.5
-
Tris/HCl buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
adenocarcinoma 755
Manually annotated by BRENDA team
-
diploid wild 2 line, tissue culture
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
little or no activity in mitochondria or microsomes
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is critical for lung cancer cell proliferation and invasion
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
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)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
133000
-
placenta small form, large form is converted to small form by incubation with phosphoribosyldiphosphate
170000
-
placenta large form, in the presence of AMP or GMP
270000
-
placenta, large form, small form is converted to large form by incubation with purine nucleotides, large form presumably catalytically inactive
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
at least 15 min stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Mg2+ and phosphate are essential for stability
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen sensitive enzyme
-
489754
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 4°C, cell-free extract, overnight, more than 50% loss of activity
-
-20°C, crude, more than 50% loss of activity overnight
-
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, partially purified preparation in 50 mM phosphate buffer, pH 7.4, 5 mM Mg2+ and 60 mM 2-mercaptoethanol, at least 4 weeks
-
4°C, phosphate buffer, 10 d, 40% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose, partial purification
-
partial
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and K338Q/P422W mutant enzyme in amidophosphoribosyltransferase deficient CHO ade -A cells and in transgenic mice
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased enzyme expression correlates with aggressive lung cancer. L-glutamine induces enzyme expression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team