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Information on EC 2.1.2.2 - phosphoribosylglycinamide formyltransferase 1 and Organism(s) Gallus gallus
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2.1.2.2 phosphoribosylglycinamide formyltransferase 1IUBMB Comments
Two enzymes are known to catalyse the third step in de novo purine biosynthesis. This enzyme utilizes 10-formyltetrahydrofolate as the formyl donor, while the other enzyme, EC 6.3.1.21, phosphoribosylglycinamide formyltransferase 2, utilizes formate. In vertebrates this activity is catalysed by a trifunctional enzyme that also catalyses the activities of EC 6.3.4.13, phosphoribosylamine---glycine ligase and EC 6.3.3.1, phosphoribosylformylglycinamidine cyclo-ligase.
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Word Map
- 2.1.2.2
- purine
- antifolate
- thymidylate
- dihydrofolate
- pemetrexed
-
formylation
-
polyglutamation
-
folate-dependent
-
multitargeted
-
ccrf-cem
- folylpolyglutamate
-
aminoimidazole
-
alimta
- lometrexol
- aicar
-
ddathf
- mta
- medicine
-
trifunctional
-
5,10-dideazatetrahydrofolic
-
6-substituted
- 5-aminoimidazole-4-carboxamide
-
pyrrolo2,3-dpyrimidine
-
aminoimidazolecarboxamide
-
folate-requiring
- trimetrexate
-
phosphoribosylaminoimidazole
- monoglutamate
- raltitrexed
- 5-formyltetrahydrofolate
-
igrov1
- diagnostics
-
formylglycinamide
-
antipurine
The taxonomic range for the selected organisms is: Gallus gallus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
glycinamide ribonucleotide formyltransferase, glycinamide ribonucleotide transformylase, garft, gar tfase, gar transformylase, garftase, phosphoribosylglycinamide formyltransferase, glycinamide ribonucleotide formyl transferase, gar formyltransferase, gartfase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-amino-N-ribosylacetamide 5'-phosphate (glycinamide ribotide) transformylase
-
-
2-amino-N-ribosylacetamide 5'-phosphate transformylase
-
-
-
-
5'-phosphoribosylglycinamide transformylase
-
-
-
-
5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide ribonucleotide transformylase
-
-
-
-
ADE8
-
-
-
-
GAR formyltransferase
-
-
-
-
GAR TFase
-
-
-
-
GAR transformylase
-
-
-
-
GART
-
-
-
-
glycinamide ribonucleotide transformylase
-
-
-
-
PurN
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
formyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
10-formyltetrahydrofolate:5'-phosphoribosylglycinamide N-formyltransferase
Two enzymes are known to catalyse the third step in de novo purine biosynthesis. This enzyme utilizes 10-formyltetrahydrofolate as the formyl donor, while the other enzyme, EC 6.3.1.21, phosphoribosylglycinamide formyltransferase 2, utilizes formate. In vertebrates this activity is catalysed by a trifunctional enzyme that also catalyses the activities of EC 6.3.4.13, phosphoribosylamine---glycine ligase and EC 6.3.3.1, phosphoribosylformylglycinamidine cyclo-ligase.
CAS REGISTRY NUMBER
COMMENTARY
9032-02-4
-
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
(6R)-N10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
(6R)-tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
10-formyltetrahydrofolate + (alpha,beta)-glycinamide ribonucleotide
tetrahydrofolate + formylglycinamide ribonucleotide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
10-formyltetrahydrofolate + carbocyclic beta-glycinamide ribonucleotide
tetrahydrofolate + formyl glycinamide ribonucleotide
-
-
-
-
?
5'-phosphoribosylglycinamide + 10-formyl-5,8-dideazafolate
5'-phosphoribosyl-N-formylglycinamide + 5,8-dideazafolate
-
-
-
-
r
inosinic acid + glycinamide ribotide + H2O
5-amino-4-imidazolecarboxamide ribotide + formylglycinamide ribotide
-
-
-
-
?
N5,N10-anhydroformyl-5,6,7,8tetrahydrofolic acid + 2-amino-N-ribosylacetamide 5'-phosphate + H2O
formylglycinamide ribotide + tetrahydrofolic acid + 2-formamido-N-ribosylacetamide 5'-phosphate
-
-
-
-
ir
N5,N10-anhydroformyltetrahydrofolic acid + glycinamide ribonucleotide
formylglycinamide ribonucleotide + ?
-
-
-
-
?
(6R)-N10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
(6R)-tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
(6R)-N10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
(6R)-tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
in uricotelic organisms such as birds, the major role of this active pathway is elimination of waste nitrogen
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
essential enzyme in DNA synthesis, third enzyme in de novo purine biosynthesis pathway
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
transformylation reaction of purine biosynthesis
-
-
?
additional information
?
-
-
reaction does not occur if glycine, glycinamide or glycinamide riboside is substituted for glycinamide ribotide
-
-
?
additional information
?
-
-
glycinamide ribonucleotide nucleoside is no substrate
-
-
?
additional information
?
-
-
trifunctional enzyme, GAR synthetase, aminoimidazole ribonucleotide synthetase and GAR transformylase
-
-
?
additional information
?
-
-
trifunctional enzyme, GAR synthetase, aminoimidazole ribonucleotide synthetase and GAR transformylase
-
-
?
additional information
?
-
-
trifunctional enzyme, GAR synthetase, aminoimidazole ribonucleotide synthetase and GAR transformylase
-
-
?
additional information
?
-
-
3 activities in a multifunctional protein, posessing glycinamide ribonucleotide synthetase, glycinamide ribonucleotidetransformylase and aminoimidazole ribonucleotide synthetase
-
-
?
additional information
?
-
-
3 activities in a multifunctional protein, posessing glycinamide ribonucleotide synthetase, glycinamide ribonucleotidetransformylase and aminoimidazole ribonucleotide synthetase
-
-
?
additional information
?
-
-
3 activities in a multifunctional protein, posessing glycinamide ribonucleotide synthetase, glycinamide ribonucleotidetransformylase and aminoimidazole ribonucleotide synthetase
-
-
?
additional information
?
-
-
GAR transformylase activity copurifies with 5,10-methylene-, 5,10-methenyl, and 10-formyl-H4folate sythetase (combined) trifunctional enzyme, EC 6.3.4.3, EC 1.5.1.5 and EC 3.5.4.9
-
-
?
additional information
?
-
-
purified along with 10-formyltetrahydrofolate synthetase
-
-
?
additional information
?
-
-
uses both diastereomers of 5,10-methenyltetrahydrofolate, (+)-L-diastereomer is used 120 times faster than the (-)-L-diastereomer
-
-
?
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
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
in uricotelic organisms such as birds, the major role of this active pathway is elimination of waste nitrogen
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
essential enzyme in DNA synthesis, third enzyme in de novo purine biosynthesis pathway
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
-
transformylation reaction of purine biosynthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PUR2_CHICK
1003
0
106544
Swiss-Prot
other Location (Reliability: 4)
A0A1D5NU16_CHICK
863
0
93387
TrEMBL
Mitochondrion (Reliability: 5)
C5J077_CHICK
266
0
28774
TrEMBL
other Location (Reliability: 2)
A0A547_CHICK
1003
0
106529
TrEMBL
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
-
protein possessing transformylase activity, sucrose density gradient ultracentrifugation
110000
110000 - 120000
-
gel filtration, sucrose density gradient ultracentrifugation, sedimentation velocity
55000
-
2 * 55000, SDS-PAGE, sucrose density ultracentrifugation, proteolytic cleavage
61000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
dimer
-
2 * 55000, SDS-PAGE, sucrose density ultracentrifugation, proteolytic cleavage
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of trifunctional 5,10-methenyl-, 5,10-methylene, and 10-formylH4folate synthetase, aminoimidazole carboxamide ribotide transformylase and serine transhydroxymethylase
-
purified in combination with formyl-methenyl-methylenetetrahydrofolate synthetase
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Daubner, S.C.; Schrimsher, J.L.; Schendel, F.J.; Young, M.; Henikoff, S.; Patterson, D.; Stubbe, J.; Benkovic, S.J.
A multifunctional protein possessing glycinamide ribonucleotide synthetase, glycinamide ribonucleotide transformylase, and aminoimidazole ribonucleotide synthetase activities in de novo purine biosynthesis
Biochemistry
24
7059-7062
1985
Drosophila melanogaster, Gallus gallus, Saccharomyces cerevisiae, Schizosaccharomyces pombe
Caperelli, C.A.; Benkovic, P.A.; Chettur, G.; Benkovic, S.J
Purification of a complex catalizing folate cofactor synthesis and transformylation in de novo purine biosynthesis
J. Biol. Chem.
255
1885-1890
1980
Saccharomyces cerevisiae, Gallus gallus, Columba sp., Oryctolagus cuniculus, Ovis aries, Sus scrofa
Caperelli, C.A.; Chettur, G.; Lin-Kosley, L.
Purification of glycineamide ribonucleotide transformylase
Dev. Biochem.
4
371-376
1979
Gallus gallus
-
Warren, L.; Buchanan, J.M.
Biosynthesis of the purines. XIX. 2-Amino-N-ribosylacetamide 5'-phosphate(glycinamide ribotide) transformylase
J. Biol. Chem.
229
613-626
1957
Gallus gallus, Clostridium cylindrosporum, Columba sp.
Smith, G.K.; Benkovic, P.A.; Benkovic, S.J.
L(-)-10-formyltetrahydrofolate is the cofactor for glycinamide ribonucleotide transformylase from chicken liver
Biochemistry
20
4034-4036
1981
Gallus gallus, Escherichia coli
Caperelli, C.A.; Chettur, G.; Lin, L.Y.; Benkovic, S.J.
Purification of glycineamide ribonucleotide transformylase
Biochem. Biophys. Res. Commun.
82
403-410
1978
Saccharomyces cerevisiae, Gallus gallus, Ovis aries, Sus scrofa
Inglese, J.; Johnson, D.L.; Shiau, A.; Smith, J.M.; Benkovic, S.J.
Subcloning, characterization, and affinity labeling of Escherichia coli glycinamide ribonucleotide transformylase
Biochemistry
29
1436-1443
1990
Bacillus subtilis, Cricetulus griseus, Drosophila melanogaster, Escherichia coli, Gallus gallus, Homo sapiens, Mus musculus, Saccharomyces cerevisiae
Young, M.; Sammons, R.D.; Mueller, W.T.; Benkovic, S.J.
An antibody probe to determine the native species of glycinamide ribonucleotide transformylase in chicken liver
Biochemistry
23
3979-3986
1984
Gallus gallus, Mus musculus
Caperelli, C.A.
Mammalian glycinamide ribonucleotide transformylase: Purification and some properties
Biochemistry
24
1316-1320
1985
Gallus gallus, Mus musculus
Caperelli, C.A.
Mammalian glycinamide ribonucleotide transformylase. Kinetic mechanism and associated de novo purine biosynthesis activities
J. Biol. Chem.
264
5053-5057
1989
Gallus gallus, Drosophila melanogaster, Homo sapiens, Mus musculus
Dev, I.K.; Harvey, R.J.
N10-Formyltetrahydrofolate is the formyl donor for glycinamide ribonucleotide transformylase in Escherichia coli
J. Biol. Chem.
253
4242-4244
1978
Escherichia coli, Escherichia coli B / ATCC 11303, Gallus gallus, Salmonella enterica subsp. enterica serovar Typhimurium
Smith, G.K.; Mueller, W.T.; Wasserman, G.F.; Taylor, W.D.; Benkovic, S.J.
Characterization of the enzyme complex involving the folate-requiring enzymes of de novo purine biosynthesis
Biochemistry
19
4313-4321
1980
Gallus gallus, Escherichia coli
Warren, M.S.; Marolewski, A.E.; Benkovic, S.J.
A rapid screen of active site mutants in glycinamide ribonucleotide transformylase
Biochemistry
35
8855-8862
1996
Bacillus subtilis, Saccharomyces cerevisiae, Gallus gallus, Drosophila melanogaster, Escherichia coli, Homo sapiens
Sanghani, S.P.; Moran, R.G.
Tight binding of folate substrates and inhibitors to recombinant mouse glycinamide ribonucleotide formyltransferase
Biochemistry
36
10506-10516
1997
Gallus gallus, Escherichia coli, Homo sapiens, Mus musculus
Caperelli, C.A.; Giroux, E.L.
The human glycinamide ribonucleotide transformylase domain: purification, characterization, and kinetic mechanism
Arch. Biochem. Biophys.
341
98-103
1997
Bacillus subtilis, Escherichia coli, Gallus gallus, Homo sapiens, Saccharomyces cerevisiae
Antle, V.D.; Donat, N.; Hua, M.; Liao, P.L.; Vince, R.; Caperelli, C.A.
Substrate specificity of human glycinamide ribonucleotide transformylase
Arch. Biochem. Biophys.
370
231-235
1999
Gallus gallus, Escherichia coli, Homo sapiens
Antle, V.D.; Liu, D.; McKellar, B.R.; Caperelli, C.A.; Hua, M.; Vince, R.
Substrate specificity of glycinamide ribonucleotide transformylase from chicken liver
J. Biol. Chem.
271
6045-6049
1996
Gallus gallus, Escherichia coli
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