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Information on EC 2.1.2.2 - phosphoribosylglycinamide formyltransferase 1 and Organism(s) Homo sapiens and UniProt Accession P22102

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EC Tree
IUBMB 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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Homo sapiens
UNIPROT: P22102
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
glycinamide ribonucleotide formyltransferase, glycinamide ribonucleotide transformylase, garft, gar tfase, gar transformylase, garftase, phosphoribosylglycinamide formyltransferase, glycinamide ribonucleotide formyl transferase, gar formyltransferase, gartfase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycinamide ribonucleotide formyl transferase
-
glycinamide ribonucleotide formyltransferase
-
glycinamide ribonucleotide transformylase
-
trifunctional purine biosynthetic protein adenosine-3
-
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
-
-
-
-
glycinamide ribonucleotide formyltransferase
-
-
glycinamide ribonucleotide transformylase
glycinamide ribotide formyltransferase
-
-
phosphoribosylglycinamide formyltransferase
-
-
PurN
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formyl group transfer
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 hide
9032-02-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide
tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide
show the reaction diagram
10-formyl-5,8-dideazafolate + beta-glycinamide ribonucleotide
5,8-dideazafolate + N-formyl beta-glycinamide ribonucleotide
show the reaction diagram
-
-
-
-
?
10-formyl-5,8-dideazafolate + carbocyclic beta-glycinamide ribonucleotide
5,8-dideazafolate + N-formyl carbocyclic beta-glycinamide ribonucleotide
show the reaction diagram
-
-
-
-
?
10-formyl-5,8-dideazafolate + N1-(5-phospho-D-ribosyl)glycinamide
?
show the reaction diagram
-
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
show the reaction diagram
10-formyltetrahydrofolate + carbocyclic beta-glycinamide ribonucleotide
tetrahydrofolate + formyl glycinamide ribonucleotide
show the reaction diagram
-
-
-
-
?
10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide
tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide
show the reaction diagram
-
-
-
-
?
10-formyltetrahydrofolate + O-phosphonate carbocyclic glycinamide ribonucleotide
tetrahydrofolate + O-phosphonate-ribosyl-N-formylglycinamide
show the reaction diagram
-
-
-
-
?
beta-glycinamide ribonucleotide + 10-formyltetrahydrofolate
?
show the reaction diagram
-
-
-
-
?
beta-glycinamide ribonucleotide + ATP + formate
beta-formylglycinamide ribonucleotide + ADP
show the reaction diagram
-
assay at 25°C
-
-
?
additional information
?
-
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
10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide
tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide
show the reaction diagram
-
-
-
?
10-formyltetrahydrofolate + 5-phospho-D-ribosylglycinamide
tetrahydrofolate + 5'-phosphoribosyl-N-formylglycinamide
show the reaction diagram
10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide
tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10-formyltetrahydrofolate
binding structure and formyl transfer structure and mechanism analysis, overview
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lometrexol
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S)-2-(((5-(2-((6R)-2-amino-4-oxo-5,6,7,8-tetrahydro-1H-pyrido[2,3-d]-pyrimidin-6-yl)ethyl)thiophene-2-yl)carbonyl)amino)-pentanedioic acid
LY309887
(2S)-2-(((5-(2-((6S)-2-amino-4-oxo-1,6,7,8-tetrahydropyrimido[5,4-b]-[1,4]thiazin-6-yl)ethyl)thiophene-2-yl)carbonyl)amino)-pentanedioic acid
AG2034
(2S)-2-[[4-[(1RS)-1-[(2,4-diaminopteridin-6-yl)methyl]but-3-ynyl]benzoyl]amino]pentanedioic acid
-
(S)-2-(4-((2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)methyl)benzamido)pentanedioic acid
-
(S)-2-(4-(2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl)benzamido)pentanedioic acid
-
(S)-2-(4-(3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)propyl)benzamido)pentanedioic acid
-
(S)-2-(4-(4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)butyl)benzamido)pentanedioic acid
-
(S)-2-(4-(5-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)pentyl)benzamido)pentanedioic acid
-
(S)-2-(4-(6-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-5-yl)hexyl)benzamido)pentanedioic acid
-
(S)-2-(5-(3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]-pyrimidin-5-yl)propyl)thiophene-2-carboxamido)pentanedioic acid
-
(S)-2-(5-(4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]-pyrimidin-5-yl)butyl)thiophene-2-carboxamido)pentanedioic acid
-
(S)-2-(5-(5-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]-pyrimidin-5-yl)pentyl)thiophene-2-carboxamido)pentanedioic acid
-
(S)-2-(5-(6-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]-pyrimidin-5-yl)hexyl)thiophene-2-carboxamido)pentanedioic acid
lometrexol, LMTX
1-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetyl]-piperidine-4-carboxylic acid (pyridin-3-ylmethyl)-amide
-
10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
specifically inhibits recombinant GAR Tfase, inactive against other folate-dependent enzymes, potent inhibitor of tumor cell proliferation
10-formyl-5,10-dideaza-5,6,7,8-tetrahydrofolic acid
-
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
2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-N-[[(pyridin-3-ylmethyl)-carbamoyl]-methyl]-acetamide
-
3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-N-pyridin-3-ylmethyl-propionamide
-
4-([2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-methyl)-N-pyridin-3-ylmethyl-benzamide
inhibition of thymidylate synthase, as well as glycinamide ribonucleotide formyltransferase and ribonucleotide formyltransferase. Growth inhibition of 4-([2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-methyl)-N-pyridin-3-ylmethyl-benzamide toward KB cells results in cytotoxicity and G1/G2-phase accumulation, and is partially protected by excess thymidine and adenosine, but is completely reversed in the combination of thymidine and adenosine
4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-cyclohexanecarboxylic acid (pyridin-3-ylmethyl)-amide
-
4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-N-pyridin-3-ylmethyl-benzamide
-
4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-N-pyridin-3-ylmethyl-butyramide
-
5-((4-carboxy-4-(4-(((2,4-diaminopyrido[3,2-d]pyrimidine-6-yl)methyl)amino)benzamido)butyl)carbamoyl)-isophthalic acid
iDIA
5-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-pentanoic acid (pyridin-3-ylmethyl)-amide
-
6-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)-acetylamino]-hexanoic acid (pyridin-3-ylmethyl)-amide
-
lometrexol
N-(4-[2-(2-amino-3,4-dihydro-4-oxo-7H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl]benzoyl)-L-glutamic acid
-
N-(5-[N-(3,4-dihydro-2-methyl-4-oxyquinazolin-6-ylmethyl)-N-methyl-amino]-2-thienoyl)-L-glutamic acid
-
N-([5-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]thiophen-2-yl]carbonyl)-L-glutamic acid
-
N-([5-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]thiophen-2-yl]carbonyl)-L-glutamic acid
-
N-[(5-[2-[(6R)-2-amino-4-oxo-3,4,5,6,7,8-hexahydropyrido[2,3-d]pyrimidin-6-yl]ethyl]-4-methylthiophen-2-yl)carbonyl]glutamic acid
modeling
N-[(5-[2-[(6R)-2-amino-4-oxo-3,4,5,6,7,8-hexahydropyrido[2,3-d]pyrimidin-6-yl]ethyl]thiophen-2-yl)carbonyl]glutamic acid
modeling
N-[(5-[2-[(6S)-2-amino-4-oxo-4,6,7,8-tetrahydro-3H-pyrimido[5,4-b][1,4]thiazin-6-yl]ethyl]thiophen-2-yl)carbonyl]glutamic acid
modeling
N-[4-[(1R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylsulfanyl)butyl]benzoyl]glutamic acid
binding structure analysis, modeling, overview
N-[4-[(1S)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylsulfanyl)butyl]benzoyl]glutamic acid
binding structure analysis, modeling, overview
N-[4-[3-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)propyl]benzoyl]-L-glutamic acid
N-[4-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]benzoyl]-L-glutamic acid
-
N-[4-[4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylsulfanyl)butyl]benzoyl]glutamic acid
-
N-[4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid
N-[4-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid
-
N-[4-[6-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1,1,1-trifluoro-2-oxohexan-3-yl]benzoyl]glutamic acid
-
N-[6-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)hexanoyl]-L-glutamic acid
N-[7-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)heptanoyl]-L-glutamic acid
permetrexed
-
(6R)-5,10-dideazatetrahydrofolate
-
lometrexol
(6R)-dideazatetrahydrofolate diglutamate
-
LY235340
(6R)-dideazatetrahydrofolate pentaglutamate
-
LY235542
(6R)-dideazatetrahydrofolate tetraglutamate
-
LY266978
(6R)-dideazatetrahydrofolate triglutamate
-
LY235337
(6S)-dideazatetrahydrofolate
-
LY243246
(alpha,beta)-hydroxyacetamide ribonucleotide
-
-
(S)-2-(((4R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylthio)butyl)benzamido)pentanedioic acid
-
-
(S)-2-(4((S)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-hydroxybutyl)benzamido)pentanedioic acid
-
-
(S)-2-(4((S)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-methoxybutyl)benzamido)pentanedioic acid
-
-
(S)-2-(4-(2-(3-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)propyl)-1,3-dithian-2-yl)benzamido)pentanedioic acid
-
-
(S)-2-[2-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-acetylamino]-pentanedioic acid
-
-
(S)-2-[3-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-propionylamino]-pentanedioic acid
-
-
(S)-2-[4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-benzoylamino]-pentanedioic acid
-
-
(S)-2-[4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-butyrylamino]-pentanedioic acid
-
-
(S)-2-[5-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-pentanoylamino]-pentanedioic acid
-
-
(S)-2-[6-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo [2,3-d]pyrimidin-6-yl)-acetylamino]-hexanoylamino]-pentanedioic acid
-
-
10-Acetyl-5,8-dideazafolate
-
-
10-CF3CO-DDACTHF
-
-
10-formyl-DDACTHF
-
-
10-methanesulfonyl-5-DACTHF
-
-
10-methanesulfonyl-DDACTHF
-
-
10-methylthio-DDACTHF
-
-
10-trifluoroacetyl-DDACTHF
-
-
2',3'-dideoxy-2',3'-didehydro-carbocyclic glycinamide ribonucleotide
-
-
2',3'-dideoxy-carbocyclic glycinamide ribonucleotide
-
-
2',5'-furan-dideazatetrahydrofolate
-
LY222306
2',5'-thiophene dideazatetrahydrofolate
4-carbamoyl-2-[4-[4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(2,2,2-trifluoroacetyl)butyl]benzoylamino]butyric acid
-
-
4-carbamoyl-4-[4-[4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(2,2,2-trifluoroacetyl)butyl]benzoylamino]butyric acid
-
-
5'-phosphonate carbocyclic glycinamide ribonucleotide
-
-
5,10-dideaza-5,6,7,8-tetrahydrofolate
-
-
5,10-dideaza-5,6,7,8-tetrahydrofolic acid
-
-
5,10-dideazatetrahydrofolate
-
-
AG2034
-
-
AG2037
-
-
LY231514
-
antitumor activity may result from simultaneous and multiple inhibition of several key folate-requiring enzymes via its polyglutamated metabolites
LY231514 monoglutamate
-
-
LY231514 pentaglutamate
-
-
LY309887
-
-
methotrexate
-
-
N-(4-[3-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-propyl]benzoyl)-L-glutamic acid
-
dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-butyl]benzoyl)-L-glutamic acid
-
dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[5-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-pentyl]benzoyl)-L-glutamic acid
-
dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[6-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)-hexyl]benzoyl)-L-glutamic acid
-
dual inhibition of glycinamide ribonucleotide formyltransferase and, likely, 5-amino-4-imidazole carboxamide ribonucleotide formyltransferase, resulting in potent growth inhibition of human tumor cells KB and IGROV1 that express folate receptors
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)-gamma-glutamyl-gamma-glutamyl-gamma-glutamyl-gamma-glutamylglutamic acid
-
-
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)-gamma-glutamyl-gamma-glutamylglutamic acid
-
-
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)glutamic acid
-
-
N-([4-[(1R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-hydroxybutyl]phenyl]carbonyl)glutamic acid
-
-
N-([4-[(1R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-methoxybutyl]phenyl]carbonyl)glutamic acid
-
-
N-([4-[(1S)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylsulfanyl)butyl]phenyl]carbonyl)glutamic acid
-
-
N-([4-[(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)methyl]phenyl]carbonyl)glutamic acid
-
-
N-([4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)ethyl]phenyl]carbonyl)glutamic acid
-
-
N-([5-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2,3-dihydrothiophen-2-yl]carbonyl)-4-methylideneglutamic acid
-
-
N-[4-[2-(2,4-diamino-7H-pyrrolo[2,3-d]pyrimidin-5-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2,4-diaminopyrido[3,2-d]pyrimidin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]-2-fluorobenzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2,4-diaminoquinazolin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-(2-amino-4-methylquinazolin-6-yl)ethyl]benzoyl]-4-methylideneglutamic acid
-
-
N-[4-[2-[(6R)-2-amino-3,4,5,6,7,8-hexahydro-4-oxopyrido[2,3-d]pyrimidin-6-yl]ethyl]benzoyl]-L-glutamic acid
-
-
N-[4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid
-
-
N-[4-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid
-
-
N-[4-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]thiophene-2-carbonyl]-L-glutamic acid
-
-
N-[4-[5-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-2-(2,2,2-trifluoroacetyl)pentyl]benzoyl]-L-glutamic acid
-
effective inhibitor
N-[5-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]thiophene-2-carbonyl]-L-glutamic acid
-
-
N-[5-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]thiophene-2-carbonyl]-L-glutamic acid
-
-
N-[7-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)heptanoyl]-D-glutamic acid
-
-
N-[8-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)octanoyl]-D-glutamic acid
-
-
N-{4-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]benzoyl}-L-glutamic acid
-
-
N-{4-[5-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)pentyl]benzoyl}-L-glutamic acid
-
-
N-{4-[6-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)hexyl]benzoyl}-L-glutamic acid
-
-
pemetrexed
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 33
10-formyl-5,8-dideazafolate
0.0011 - 33
beta-glycinamide ribonucleotide
0.0036
carbocyclic beta-glycinamide ribonucleotide
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0019 - 0.102
10-formyl-5,8-dideazafolate
0.0034 - 14
beta-glycinamide ribonucleotide
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000015
10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
-
0.0067
2,4-diamino-6-(3,4,5-trimethoxyanilino)-methylpyrido[3,2-d]pyrimidine
pH and temperature not specified in the publication
0.02754
2,4-diamino-6-(3,4,5-trimethoxybenzyl)-5,6,7,8-tetrahydro-quinazoline
pH and temperature not specified in the publication
0.04218
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
0.000005 - 0.00005
N-[(5-[2-[(6R)-2-amino-4-oxo-3,4,5,6,7,8-hexahydropyrido[2,3-d]pyrimidin-6-yl]ethyl]-4-methylthiophen-2-yl)carbonyl]glutamic acid
pH and temperature not specified in the publication
0.000005 - 0.00005
N-[(5-[2-[(6R)-2-amino-4-oxo-3,4,5,6,7,8-hexahydropyrido[2,3-d]pyrimidin-6-yl]ethyl]thiophen-2-yl)carbonyl]glutamic acid
pH and temperature not specified in the publication
0.000005 - 0.00005
N-[(5-[2-[(6S)-2-amino-4-oxo-4,6,7,8-tetrahydro-3H-pyrimido[5,4-b][1,4]thiazin-6-yl]ethyl]thiophen-2-yl)carbonyl]glutamic acid
pH and temperature not specified in the publication
0.00021
N-[4-[(1R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylsulfanyl)butyl]benzoyl]glutamic acid
pH and temperature not specified in the publication
0.00018
N-[4-[(1S)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylsulfanyl)butyl]benzoyl]glutamic acid
pH and temperature not specified in the publication
0.00021
(S)-2-(((4R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylthio)butyl)benzamido)pentanedioic acid
-
-
0.0014
(S)-2-(4((S)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-hydroxybutyl)benzamido)pentanedioic acid
-
-
0.0012
(S)-2-(4((S)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-methoxybutyl)benzamido)pentanedioic acid
-
-
0.0011
(S)-2-(4-(2-(3-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)propyl)-1,3-dithian-2-yl)benzamido)pentanedioic acid
-
-
0.000015 - 0.00003
10-CF3CO-DDACTHF
0.000014
10-formyl-DDACTHF
0.00058
10-methanesulfonyl-5-DACTHF
-
26°C, pH 7.5
0.00023
10-methanesulfonyl-DDACTHF
-
26°C, pH 7.5
0.00025
10-methylthio-DDACTHF
0.000015
10-trifluoroacetyl-DDACTHF
-
26°C, pH 7.5
0.000056
4-carbamoyl-2-[4-[4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(2,2,2-trifluoroacetyl)butyl]benzoylamino]butyric acid
-
26°C, pH 7.5
0.0048
4-carbamoyl-4-[4-[4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(2,2,2-trifluoroacetyl)butyl]benzoylamino]butyric acid
-
26°C, pH 7.5
0.0017
DDACTHF
0.0093
LY231514 monoglutamate
-
-
0.000065
LY231514 pentaglutamate
-
-
0.0011
N-([4-[(1R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-hydroxybutyl]phenyl]carbonyl)glutamic acid
-
-
0.00085
N-([4-[(1R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-methoxybutyl]phenyl]carbonyl)glutamic acid
-
-
0.00018
N-([4-[(1S)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylsulfanyl)butyl]phenyl]carbonyl)glutamic acid
-
-
0.00006
N-[4-[2-[(6R)-2-amino-3,4,5,6,7,8-hexahydro-4-oxopyrido[2,3-d]pyrimidin-6-yl]ethyl]benzoyl]-L-glutamic acid
-
-
0.001067
N-[4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid
-
at pH 7.5 and 37°C
0.000017
N-[4-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid
-
at pH 7.5 and 37°C
0.000007 - 0.000009
N-[4-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]thiophene-2-carbonyl]-L-glutamic acid
0.0005
N-[4-[5-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-2-(2,2,2-trifluoroacetyl)pentyl]benzoyl]-L-glutamic acid
-
26°C, pH 7.5
0.000068
N-[5-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]thiophene-2-carbonyl]-L-glutamic acid
-
at pH 7.5 and 37°C
0.000022
N-[5-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]thiophene-2-carbonyl]-L-glutamic acid
-
at pH 7.5 and 37°C
0.000067
N-[7-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)heptanoyl]-D-glutamic acid
-
at pH 7.5 and 37°C
0.000099
N-[8-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)octanoyl]-D-glutamic acid
-
at pH 7.5 and 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00007 - 0.01
(S)-2-(((4R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylthio)butyl)benzamido)pentanedioic acid
0.0005 - 0.01
(S)-2-(4((S)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-hydroxybutyl)benzamido)pentanedioic acid
0.0007 - 0.01
(S)-2-(4((S)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-methoxybutyl)benzamido)pentanedioic acid
0.01 - 0.1
(S)-2-(4-(2-(3-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)propyl)-1,3-dithian-2-yl)benzamido)pentanedioic acid
0.000016 - 0.01
10-CF3CO-DDACTHF
0.0027 - 0.1
DDACTHF
0.0024 - 0.01
N-([4-[(1R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-hydroxybutyl]phenyl]carbonyl)glutamic acid
0.0005 - 0.01
N-([4-[(1R)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-methoxybutyl]phenyl]carbonyl)glutamic acid
0.00005 - 0.01
N-([4-[(1S)-4-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-1-(methylsulfanyl)butyl]phenyl]carbonyl)glutamic acid
0.001
N-([4-[(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)methyl]phenyl]carbonyl)glutamic acid
Homo sapiens
-
in situ
0.000018
N-([4-[2-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)ethyl]phenyl]carbonyl)glutamic acid
Homo sapiens
-
in situ
0.000014 - 0.1
N-[4-[2-[(6R)-2-amino-3,4,5,6,7,8-hexahydro-4-oxopyrido[2,3-d]pyrimidin-6-yl]ethyl]benzoyl]-L-glutamic acid
0.0000049
N-[4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid
Homo sapiens
-
at pH 7.5 and 37°C
0.0000019 - 0.0000068
N-[4-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]benzoyl]-L-glutamic acid
0.00000017 - 0.00000027
N-[4-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]thiophene-2-carbonyl]-L-glutamic acid
0.0000072
N-[4-[5-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)pentyl]benzoyl]-L-glutamic acid
Homo sapiens
-
in situ
0.0000086
N-[4-[6-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)hexyl]benzoyl]-L-glutamic acid
Homo sapiens
-
in situ
0.00000026
N-[5-[3-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)propyl]thiophene-2-carbonyl]-L-glutamic acid
Homo sapiens
-
at pH 7.5 and 37°C
0.00000055
N-[5-[4-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)butyl]thiophene-2-carbonyl]-L-glutamic acid
Homo sapiens
-
at pH 7.5 and 37°C
0.0000079
N-[7-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)heptanoyl]-D-glutamic acid
Homo sapiens
-
at pH 7.5 and 37°C
0.0000011
N-[8-(2-amino-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidin-6-yl)octanoyl]-D-glutamic acid
Homo sapiens
-
at pH 7.5 and 37°C
0.00003
pemetrexed
Homo sapiens
-
in situ
additional information
N-(4-[[(2,4-diaminopteridin-6-yl)methyl](methyl)amino]benzoyl)glutamic acid
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
37
-
in situ GARFT enzyme inhibition assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
enzyme immunohistochemic analysis in 70 cases of human gliomas and normal brain tissues, overview
Manually annotated by BRENDA team
the enzyme is frequently overexpressed in glioma, enzyme immunohistochemic analysis in 70 cases of human gliomas and normal brain tissues, overview
Manually annotated by BRENDA team
enzyme expression and functional significance in hepatocellular carcinoma cells from several patients, overview
Manually annotated by BRENDA team
-
O cell
Manually annotated by BRENDA team
-
xenograft, pancreatic carcinoma
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
glycinamide ribonucleotide transformylase is a folate-dependent enzyme in the de novo purine pathway
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PUR2_HUMAN
1010
0
107767
Swiss-Prot
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
108000
-
human GART comprises the C-terminal domain of a 108 kDa, trifunctional enzyme
112000
-
HeLa and L1210 cells
21800
-
recombinant enzyme, predicted from cDNA
21840
-
recombinant enzyme, MALDI-TOF mass spectral analysis
25700
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in apoform or in complex with inhibitors 10S methylthio-DDACTHF and 10R methylthio-DDACTHF, mixing of 0.002 ml of 15 mg/mL in 20 mM Tris, pH 8.0, 200 mM NaCl, 5 mM DTT, and inhibitors in a 5fold molar excess for complex crystals, with 0.002 ml of reservoir solution containing 0.1 M phosphate/citrate buffer, 1.5-2.0 M ammonium sulfate at pH 4.2, X-ray diffraction structure determination and analysis at 1.52-1.70 A resolution, molecular replacement
vapor diffusion sitting drop method, crystals of enzyme in complex with 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
sitting drop vapor diffusion method, using 0.1 M Tris-HCl (pH 7.5), 0.333 M NaCl, 18% (w/v) polyethylene glycol (PEG) 4000, and a 2% (w/v) PEG 400
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D144E
-
catalytically inactive mutant
D144H
-
catalytically inactive mutant
H108K
-
catalytically inactive mutant
H108R
-
catalytically inactive mutant
K170R
-
catalytically active mutant
N106D
-
catalytically inactive mutant
N106H
-
catalytically inactive mutant
N106Q
-
catalytically active mutant
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Ni-NTA resin column chromatography and Superdex 75 gel filtration
-
recombinant enzyme, expressed in E. coli
-
using a NiHisTrap HP column, the affinity tag is removed by cleavage with TEV protease
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme expression analysis in hepatocellular carcinoma cell lines, overview
gene purN, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
cloned and expressed in Escherichia coli BL21(DE3)pLysS
-
cloned and expressed in Escherichia coli HMS174(DE3)/pCC12
-
cloned by functional complementation in Escherichia coli
-
expressed in Escherichia coli Rosetta (DE3)pLysS cells
-
hybrid enzymes of human GART and PurN from Escherichia coli are expressed in Escherichia coli: PGX-B12 (PurN1-101/hGART102-202), GPX-M1 (hGART1-100/PurN101-212), GPX-M1 (hGART1129/PurN54-212), GPX-M24 (hGART1-54/PurN55-212), GPX-M36 (hGART1-89/PurN90-212), GPX-M55 (hGART1-56/PurN58-212), GPG-N11 (hGART1-56/PurN57-131/hGART132-202)
-
into the pET17b vector and into the pMC8HdeltaT vector for expression in Escherichia coli BL21Star(DE3)pRARE cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
medicine
high GART expression is observed in glioma and is related to the grade of malignancy. GART overexpression is significantly associated with overall survival. Transfecting cells with GART-siRNA suppresses proliferation and enhances temozolomide-induced apoptosis in glioma cells
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Caperelli, C.A.; Liu, D.
Carbocyclic substrates for de novo purine biosynthesis. Enantiospecific synthesis and enantiospecificity of enzymatic utilization
J. Biol. Chem.
267
9783-9787
1992
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Chen, P.; Schulze-Gahmen, U.; Stura, E.A.; Inglese, J.; Johnson, D.L.; Marolewski, A.; Benkovic, S.J.; Wilson, I.A.
Crystal structure of glycinamide ribonucleotide transformylase from Escherichia coli at 3.0 A resolution
J. Mol. Biol.
227
283-292
1992
Bacillus subtilis, Drosophila melanogaster, Escherichia coli, Homo sapiens, Mus musculus, Saccharomyces cerevisiae
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Habeck, L.L.; Leitner, T.A.; Shackelford, K.A.; Gossett, L.S.; Schultz, R.M.; Andis, S.L.; Shih, C.; Grindey, G.B.; Mendelsohn, L.G.
A novel class of monoglutamated antifolates exhibits tight-binding inhibition of human glycinamide ribonucleotide formyltransferase and potent activity against solid tumors
Cancer Res.
54
1021-1026
1994
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Shim, J.H.; Benkovic, S.J.
Evaluation of the kinetic mechanism of Escherichia coli glycinamide ribonucleotide transformylase
Biochemistry
37
8776-8782
1998
Escherichia coli, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Gooljarsingh, L.T.; Ramcharan, J.; Gilroy, S.; Benkovic, S.J.
Localization of GAR transformylase in Escherichia coli and mammalian cells
Proc. Natl. Acad. Sci. USA
98
6565-6570
2001
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Zhang, Y.; Desharnais, J.; Marsilje, T.H.; Li, C.; Hedrick, M.P.; Gooljarsingh, L.T.; Tavassoli, A.; Benkovic, S.J.; Olson, A.J.; Boger, D.L.; Wilson, I.A.
Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
Biochemistry
42
6043-6056
2003
Homo sapiens (P22102), Homo sapiens
Manually annotated by BRENDA team
Shi, C.; Chen, V.J.; et.al.
LY231514, a pyrrolo[2,3-d]pyrimidine-based antifolate that inhibits multiple folate-requiring enzymes
Cancer Res.
57
1116-1123
1997
Homo sapiens
Manually annotated by BRENDA team
Lee, S.G.; Lutz, S.; Benkovic, S.J.
On the structural and functional modularity of glycinamide ribonucleotide formyltransferases
Protein Sci.
12
2206-2214
2003
Homo sapiens
Manually annotated by BRENDA team
Cheng, H.; Chong, Y.; Hwang, I.; Tavassoli, A.; Zhang, Y.; Wilson, I.A.; Benkovic, S.J.; Boger, D.L.
Design, synthesis, and biological evaluation of 10-methanesulfonyl-DDACTHF, 10-methanesulfonyl-5-DACTHF, and 10-methylthio-DDACTHF as potent inhibitors of GAR Tfase and the de novo purine biosynthetic pathway
Bioorg. Med. Chem.
13
3577-3585
2005
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Chong, Y.; Hwang, I.; Tavassoli, A.; Zhang, Y.; Wilson, I.A.; Benkovic, S.J.; Boger, D.L.
Synthesis and biological evaluation of alpha- and gamma-carboxamide derivatives of 10-CF3CO-DDACTHF
Bioorg. Med. Chem.
13
3587-3592
2005
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Cheng, H.; Hwang, I.; Chong, Y.; Tavassoli, A.; Webb, M.E.; Zhang, Y.; Wilson, I.A.; Benkovic, S.J.; Boger, D.L.
Synthesis and biological evaluation of N-[4-[5-(2,4-diamino-6-oxo-1,6-dihydropyrimidin-5-yl)-2-(2,2,2-trifluoroacetyl)pentyl]benzoyl]-L-glutamic acid as a potential inhibitor of GAR Tfase and the de novo purine biosynthetic pathway
Bioorg. Med. Chem.
13
3593-3599
2005
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Manieri, W.; Moore, M.E.; Soellner, M.B.; Tsang, P.; Caperelli, C.A.
Human glycinamide ribonucleotide transformylase: active site mutants as mechanistic probes
Biochemistry
46
156-163
2007
Homo sapiens
Manually annotated by BRENDA team
Deng, Y.; Wang, Y.; Cherian, C.; Hou, Z.; Buck, S.A.; Matherly, L.H.; Gangjee, A.
Synthesis and discovery of high affinity folate receptor-specific glycinamide ribonucleotide formyltransferase inhibitors with antitumor activity
J. Med. Chem.
51
5052-5063
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
DeMartino, J.K.; Hwang, I.; Connelly, S.; Wilson, I.A.; Boger, D.L.
Asymmetric synthesis of inhibitors of glycinamide ribonucleotide transformylase
J. Med. Chem.
51
5441-5448
2008
Homo sapiens
Manually annotated by BRENDA team
McGuire, J.J.; Haile, W.H.
Metabolism-blocked antifolates as potential anti-rheumatoid arthritis agents: 4-amino-4-deoxy-5,8,10-trideazapteroyl-D,L-4-methyleneglutamic acid (CH-1504) and its analogs
Biochem. Pharmacol.
77
1161-1172
2009
Homo sapiens
Manually annotated by BRENDA team
Deng, Y.; Zhou, X.; Kugel Desmoulin, S.; Wu, J.; Cherian, C.; Hou, Z.; Matherly, L.H.; Gangjee, A.
Synthesis and biological activity of a novel series of 6-substituted thieno[2,3-d]pyrimidine antifolate inhibitors of purine biosynthesis with selectivity for high affinity folate receptors over the reduced folate carrier and proton-coupled folate transpo
J. Med. Chem.
52
2940-2951
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Connelly, S.; DeMartino, J.K.; Boger, D.L.; Wilson, I.A.
Biological and structural evaluation of 10R- and 10S-methylthio-DDACTHF reveals a new role for sulfur in inhibition of glycinamide ribonucleotide transformylase
Biochemistry
52
5133-5144
2013
Homo sapiens (P22102), Homo sapiens
Manually annotated by BRENDA team
Liu, Y.; Zhang, C.; Zhang, H.; Li, M.; Yuan, J.; Zhang, Y.; Zhou, J.; Guo, H.; Zhao, L.; Du, Y.; Wang, L.; Ren, L.
Synthesis and antitumor activity of a novel series of 6-substituted pyrrolo[2,3-d]pyrimidines as potential nonclassical antifolates targeting both thymidylate and purine nucleotide biosynthesis
Eur. J. Med. Chem.
93
142-155
2015
Homo sapiens (P22102)
Manually annotated by BRENDA team
Cong, X.; Lu, C.; Huang, X.; Yang, D.; Cui, X.; Cai, J.; Lv, L.; He, S.; Zhang, Y.; Ni, R.
Increased expression of glycinamide ribonucleotide transformylase is associated with a poor prognosis in hepatocellular carcinoma, and it promotes liver cancer cell proliferation
Hum. Pathol.
45
1370-1378
2014
Homo sapiens (P22102), Homo sapiens
Manually annotated by BRENDA team
Mitchell-Ryan, S.; Wang, Y.; Raghavan, S.; Ravindra, M.P.; Hales, E.; Orr, S.; Cherian, C.; Hou, Z.; Matherly, L.H.; Gangjee, A.
Discovery of 5-substituted pyrrolo[2,3-d]pyrimidine antifolates as dual-acting inhibitors of glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase in de novo purine nucleotide biosynthesis: Implications of inhibiting 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase to AMPK activation and anti-tumor activity
J. Med. Chem.
56
10016-10032
2013
Homo sapiens (P22102), Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; Cherian, C.; Orr, S.; Mitchell-Ryan, S.; Hou, Z.; Raghavan, S.; Matherly, L.H.; Gangjee, A.
Tumor-targeting with novel non-benzoyl 6-substituted straight chain pyrrolo[2,3-d]pyrimidine antifolates via cellular uptake by folate receptor alpha and inhibition of de novo purine nucleotide biosynthesis
J. Med. Chem.
56
8684-8695
2013
Homo sapiens (P22102), Homo sapiens
Manually annotated by BRENDA team
Wang, Y.; Mitchell-Ryan, S.; Raghavan, S.; George, C.; Orr, S.; Hou, Z.; Matherly, L.H.; Gangjee, A.
Novel 5-substituted pyrrolo[2,3-d]pyrimidines as dual inhibitors of glycinamide ribonucleotide formyltransferase and 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase and as potential antitumor agents
J. Med. Chem.
58
1479-1493
2015
Homo sapiens (P22102), Homo sapiens
Manually annotated by BRENDA team
Liu, X.; Ding, Z.; Liu, Y.; Zhang, J.; Liu, F.; Wang, X.; He, X.; Cui, G.; Wang, D.
Glycinamide ribonucleotide formyl transferase is frequently overexpressed in glioma and critically regulates the proliferation of glioma cells
Pathol. Res. Pract.
210
256-263
2014
Homo sapiens (P22102)
Manually annotated by BRENDA team
Liu, X.; Ding, Z.; Liu, Y.; Zhang, J.; Liu, F.; Wang, X.; He, X.; Cui, G.; Wang, D.
Glycinamide ribonucleotide formyl transferase is frequently overexpressed in glioma and critically regulates the proliferation of glioma cells
Pathol. Res. Pract.
210
256-263
2014
Homo sapiens (P22102)
Manually annotated by BRENDA team
Deis, S.M.; Doshi, A.; Hou, Z.; Matherly, L.H.; Gangjee, A.; Dann, C.E.
Structural and enzymatic analysis of tumor-targeted antifolates that inhibit glycinamide ribonucleotide formyltransferase
Biochemistry
55
4574-4582
2016
Homo sapiens
Manually annotated by BRENDA team
Xing, R.; Zhang, H.; Yuan, J.; Zhang, K.; Li, L.; Guo, H.; Zhao, L.; Zhang, C.; Li, S.; Gao, T.; Liu, Y.; Wang, L.
Novel 6-substituted benzoyl and non-benzoyl straight chain pyrrolo[2,3-d]pyrimidines as potential antitumor agents with multitargeted inhibition of TS, GARFTase and AICARFTase
Eur. J. Med. Chem.
139
531-541
2017
Homo sapiens
Manually annotated by BRENDA team
Batool, S.; Nawaz, M.S.; Mushtaq, G.; Parvaiz, F.; Kamal, M.A.
In silico analysis of glycinamide ribonucleotide transformylase inhibition by PY873, PY899 and DIA
Saudi J. Biol. Sci.
24
1155-1161
2017
Homo sapiens (P22102), Homo sapiens
Manually annotated by BRENDA team