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Information on EC 2.1.2.3 - phosphoribosylaminoimidazolecarboxamide formyltransferase and Organism(s) Gallus gallus and UniProt Accession P31335

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Gallus gallus
UNIPROT: P31335 not found.
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The taxonomic range for the selected organisms is: Gallus gallus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
5-aminoimidazole-4-carboxamide ribonucleotide, aicar transformylase, aicar tfase, aicarft, 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase, aicarft/impchase, aminoimidazolecarboxamide ribonucleotide transformylase, aica ribonucleotide formyltransferase, aminoimidazole-4-carboxamide ribonucleotide transformylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AICAR transformylase/inosine monophosphate cyclohydrolase
bifunctional enzyme catalyzing the last two steps of the purine de novo synthesis pathway
10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
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5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
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5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase
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5-amino-4-imidazolecarboxamide ribonucleotide transformylase
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5-amino-4-imidazolecarboxamide ribotide transformylase
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AICAR formyltransferase
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AICAR transformylase
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aminoimidazolecarboxamide ribonucleotide transformylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazole-carboxamide N-formyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9032-03-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
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
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazole-4-carboxamide
tetrahydrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazole-4-carboxamide
show the reaction diagram
penultimate step of the purine de novo synthesis pathway
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10-formyltetrahydrofolate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfophenyl)-1H-pyrazo]-4-sulfobenzoic acid
Acid Yellow 54, 326203-A, competitive against 10-formyltetrahydrofolate, IC50: 0.012 mM, inhibitor partially blocks the cofactor binding site
Acid Yellow 17
IC50: 0.012 mM
beta-DADF
IC50 125 nM
NCI324571-C
IC50: 0.042 mM
NCI324572-F
IC50: 0.012 mM
NCI3262203-A
IC50: 0.012 mM
NCI47729-M
IC50: 0.003 mM
SALOR2
IC50: 0.0014 mM
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfophenyl)-1H-pyrazo]-4-sulfobenzoic acid
pH 7.5
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfophenyl)-1H-pyrazo]-4-sulfobenzoic acid
Gallus gallus
Acid Yellow 54, 326203-A, competitive against 10-formyltetrahydrofolate, IC50: 0.012 mM, inhibitor partially blocks the cofactor binding site
0.012
Acid Yellow 17
Gallus gallus
IC50: 0.012 mM
0.000125
beta-DADF
Gallus gallus
IC50 125 nM
0.042
NCI324571-C
Gallus gallus
IC50: 0.042 mM
0.012
NCI324572-F
Gallus gallus
IC50: 0.012 mM
0.012
NCI3262203-A
Gallus gallus
IC50: 0.012 mM
0.003
NCI47729-M
Gallus gallus
IC50: 0.003 mM
0.0014
SALOR2
Gallus gallus
IC50: 0.0014 mM
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PUR9_CHICK
593
0
64415
Swiss-Prot
other Location (Reliability: 3)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
crystal structure analysis, monomer contains two functionally independent domains transformylase and cyclohydrolase activities
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized in complex with its inhibitor 2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfophenyl)-1H-pyrazo]-4-sulfobenzoic acid
recombinant His-tag fusion protein crystallized by sitting drop vapor diffusion method in complex with its inhibitor beta-DADF
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein using His-tag
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as His-tag fusion protein
expressed in Escherichia coli BL21.DE3 as His-tag fusion protein
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
potential target for antineoplastic chemotherapy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wolan, D.W.; Greasley, S.E.; Wall, M.J.; Benkovic, S.J.; Wilson, I.A.
Structure of avian AICAR transformylase with a multisubstrate adduct inhibitor beta-DADF identifies the folate binding site
Biochemistry
42
10904-10914
2003
Gallus gallus (P31335)
Manually annotated by BRENDA team
Xu, L.; Li, C.; Olson, A.J.; Wilson, I.A.
Crystal structure of avian aminoimidazole-4-carboxamide ribonucleotide transformylase in complex with a novel non-folate inhibitor identified by virtual ligand screening
J. Biol. Chem.
279
50555-50565
2004
Gallus gallus (P31335), Homo sapiens (P31939)
Manually annotated by BRENDA team