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Information on EC 2.1.2.3 - phosphoribosylaminoimidazolecarboxamide formyltransferase and Organism(s) Escherichia coli and UniProt Accession P15639

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The taxonomic range for the selected organisms is: Escherichia coli
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, aica ribonucleotide formyltransferase, aminoimidazolecarboxamide ribonucleotide transformylase, aicarftase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-aminoimidazole-4-carboxamide ribonucleotide tranformylase/IMP cyclohydrolase
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AICAR tranformylase/IMP cyclohydrolase
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10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
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-
-
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5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase
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-
-
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5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase
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-
-
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5-amino-4-imidazolecarboxamide ribonucleotide transformylase
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-
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5-amino-4-imidazolecarboxamide ribotide transformylase
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-
-
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5-aminoimidazole-4-carboxamide ribonucleotide tranformylase
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AICAR formyltransferase
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-
-
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AICAR TFase
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AICAR tranformylase
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AICAR transformylase
aminoimidazole-4-carboxamide ribonucleotide transformylase
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aminoimidazolecarboxamide ribonucleotide transformylase
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-
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PurH
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bifunctional enzyme with tranformylase and IMP cyclohydrolase activities
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formyl group transfer
-
-
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
10-formyldihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
dihydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
-
-
-
?
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
-
-
-
?
10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
show the reaction diagram
-
-
-
-
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
-
-
-
?
N10-formyltetrahydrofolic acid + 5-amino-4-imidazole carboxamide ribonucleotide
tetrahydrofolic acid + 5-formamido-4-imidazole carboxamide ribonucleotide
show the reaction diagram
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 + 5'-phosphoribosyl-5-amino-imidazolecarboxamide
tetrahdrofolic acid + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide
show the reaction diagram
-
-
-
-
r
10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N10-formyltetrahydrofolate
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-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N10-formyltetrahydropteroylglutamate
-
-
additional information
-
specific antifolate reagents and nonfolate inhibitors are analogues of cofactor N10-formyltetrahydrofolate and can completely inhibit AICAR Tfase activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.245
10-formyldihydrofolate
pH 7.5, temperature not specified in the publication
0.111
10-formyltetrahydrofolate
pH 7.5, temperature not specified in the publication
0.0346
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
at pH 7.5 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.18
10-formyldihydrofolate
pH 7.5, temperature not specified in the publication
4.97
10-formyltetrahydrofolate
pH 7.5, temperature not specified in the publication
3.63
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
at pH 7.5 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29.3
10-formyldihydrofolate
pH 7.5, temperature not specified in the publication
44.77
10-formyltetrahydrofolate
pH 7.5, temperature not specified in the publication
4150
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
at pH 7.5 and 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
growth deficiency phenotypes (in un-supplemented M9 minimal medium containing thymidine) are direct consequences of the gene deletions
metabolism
the enzyme is involved in the folate recycling pathway
additional information
-
the enzyme is located at the C-terminus of the bifunctional purine-biosynthesis protein, PurH, whose N-terminus possesses IMP cyclohydrolase activity. Coupling of the two domains is essential for the catalytic process, as the AICAR Tfase reaction favours the reverse direction by itself and the irreversible cyclization of 5-formyl-aminoimidazole-4-carboxamide ribonucleotide to IMP drives formyl transfer in the forward direction
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 22000, SDS-PAGE
additional information
-
PurH is composed of two domains linked by a flexible region. The N-terminal domain possesses IMPCH activity and the C-terminal domain possesses AICAR Tfase activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged PurH, without methylation of the 28 lysine residues, sitting drop vapour diffusion method, mixing of 0.001 ml of 56 mg/ml protein in 0.8 M sodium/potassium hydrogen phosphate, pH 7.5, with 0.001 ml of reservoir solution containing 0.1 M sodium acetate, pH 5.0, 1 M ammonium sulfate, 1 week to 1 month, X-ray diffraction structure determination and analysis at 3.05 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
recombinant N-terminally His6-tagged PurH from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and expressed
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expressed in Escherichia coli Rosetta (DE3) pLysS cells
gene purH, expression of N-terminally His6-tagged PurH in Escherichia coli strain Rosetta (DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Szabados, E.; Hindmarsh, E.J.; Phillips, L.; Duggleby, R.G.; Christopherson, R.I.
5-Aminoimidazole-4-carboxamide ribotide transformylase-IMP cyclohydrolase from human CCRF-CEM leukemia cells: purification, pH dependence and inhibitors
Biochemistry
33
14237-14245
1994
Bacillus subtilis, Escherichia coli, Gallus sp., Homo sapiens
Manually annotated by BRENDA team
Rayl, E.A.; Moroson, B.A.; Beardsley, G.P.
The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping
J. Biol. Chem.
271
2225-2233
1996
Bacillus subtilis, Escherichia coli, Gallus sp., Homo sapiens (P31939), Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Patrick, T.W.; Crosbie, G.W.
Specificity of 4-aminoimidazole-5-carboxamide ribotide transformylase of Escherichia coli
Biochem. J.
124
31-32
1971
Escherichia coli
Manually annotated by BRENDA team
Iwai, K.; Fujisawa, Y.; Suzuki, N.
The accumulation of 5'-phosphoribosyl-5amino-4-imidazolecarboxamide in folate-deficient pea seedlings and the enzymatic reaction in which the compound is involved
Agric. Biol. Chem.
36
398-408
1972
Allium cepa, Columba sp., Daucus carota, Escherichia coli, Gallus sp., Petroselinum crispum, Pisum sativum, Spinacia oleracea, Trifolium sp.
-
Manually annotated by BRENDA team
Wall, M.; Shim, J.H.; Benkovic, S.J.
Human AICAR transformylase: Role of the 4-Carboxamide of AICAR in binding and catalysis
Biochemistry
39
11303-11311
2000
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Shim, J.H.; Wall, M.; Benkovic, S.J.; Diaz, N.; Suarez, D.; Merz, K.M., Jr.
Evaluation of the catalytic mechanism of AICAR transformylase by pH-dependent kinetics, mutagenesis, and quantum chemical calculations
J. Am. Chem. Soc.
123
4687-4696
2001
Bacillus subtilis, Escherichia coli, Gallus sp., Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Qiu, X.; Yuan, Y.; Gao, Y.
Expression, purification, crystallization and preliminary X-ray diffraction crystallographic study of PurH from Escherichia coli
Acta Crystallogr. Sect. F
67
1590-1594
2011
Escherichia coli
Manually annotated by BRENDA team
Sah, S.; Shah, R.; Govindan, A.; Varada, R.; Rex, K.; Varshney, U.
Utilisation of 10-formyldihydrofolate as substrate by dihydrofolate reductase (DHFR) and 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) tranformylase/IMP cyclohydrolase (PurH) in Escherichia coli
Microbiology
164
982-991
2018
Escherichia coli, Escherichia coli (P15639), Escherichia coli K12 (P15639)
Manually annotated by BRENDA team