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Information on EC 2.1.2.5 - glutamate formimidoyltransferase and Organism(s) Sus scrofa and UniProt Accession P53603
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2.1.2.5 glutamate formimidoyltransferaseIUBMB Comments
The enzyme also catalyses formyl transfer from 5-formyltetrahydrofolate to L-glutamate. In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
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Word Map
- 2.1.2.5
-
octameric
-
megaloblastic
-
aciduria
-
formylation
-
folinic
- polyglutamate
-
figlu
-
monofunctional
-
polyglutamylated
- methylenetetrahydrofolate
- histidase
- medicine
- molecular biology
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
formiminotransferase-cyclodeaminase, glutamate formiminotransferase, glutamate formyltransferase, formiminoglutamic acid formiminotransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
formiminoglutamic acid formiminotransferase
-
-
-
-
formiminoglutamic acid transferase
-
-
-
-
formiminoglutamic formiminotransferase
-
-
-
-
formiminotransferase, glutamate
-
-
-
-
glutamate formiminotransferase
-
-
-
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glutamate formyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate
mechanism
-
5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate
catalytic mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
formimino group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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-
SYSTEMATIC NAME
IUBMB Comments
5-formimidoyltetrahydrofolate:L-glutamate N-formimidoyltransferase
The enzyme also catalyses formyl transfer from 5-formyltetrahydrofolate to L-glutamate. In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
CAS REGISTRY NUMBER
COMMENTARY
9032-83-1
-
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
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
?
(6R,S)-tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
-
-
-
-
r
(6S)-tetrahydropteroylpentaglutamate + N-formimidoyl-L-glutamate
5-formiminotetrahydropteroylpentaglutamate + L-glutamate
-
-
-
-
r
tetrahydropteroic acid + N-formimino-L-glutamate
5-formiminotetrahydropteroic acid + L-glutamate
-
tetrahydropteroic acid is a good alternate substrate
-
?
tetrahydropteroylpentaglutamate + N-formimino-L-glutamate
5-formiminotetrahydropteroylpentaglutamate + L-glutamate
5-formyltetrahydrofolate + L-glutamate
N-formyl-L-glutamate + tetrahydrofolate
-
N5-formyl group of Citrovorum factor, specific with respect to substrates, formation of N5-formiminotetrahydrofolate and anhydro-Citrovorum factor precedes the formation of the N10-formyl folate derivatives
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r
5-formyltetrahydrofolate + L-glutamate
N-formyl-L-glutamate + tetrahydrofolate
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folinic acid binding site, preference for (6R)-enantiomer of folinic acid
-
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
physiological substrate is (6S)-tetrahydrofolate
natural biosynthetic product is N5-formiminotetrahydrofolate
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
enzyme serves as additional entry point for the folate pool in liver
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
histidine degradation
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
histidine degradation
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
histidine degradation
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
histidine degradation
natural biosynthetic product is N5-formiminotetrahydrofolate
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
relatively specific for formiminoglutamic acid
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r
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
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mode of substrate binding and channeling, 3 glutamate-binding sites, mechanism for product release, His-82 may act as catalytic base required for the formiminotransferase mechanism, an electrostatic tunnel through the width of the domain facilitates recognition of the substrates
labile 5-formiminotetrahydrofolate product
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
tetrahydropteroic acid can replace tetrahydrofolate
-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
transfer of a single carbon from formiminoglutamate to tetrahydrofolate, product is 5-formiminotetrahydrofolate
-
?
tetrahydropteroylpentaglutamate + N-formimino-L-glutamate
5-formiminotetrahydropteroylpentaglutamate + L-glutamate
-
bifunctional formiminotetrahydrofolate cyclodeaminase: preference for polyglutamylated substrates, polyglutamylation improves binding of both the folate substrates and formiminoglutamate
-
?
tetrahydropteroylpentaglutamate + N-formimino-L-glutamate
5-formiminotetrahydropteroylpentaglutamate + L-glutamate
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optimum number of glutamates for channeling of the product to the cyclodeaminase domain is five
-
?
additional information
?
-
FTCD: bifunctional enzyme with 5-formiminotetrahydrofolate:L-glutamate N-formiminotransferase activity, EC 2.1.2.5, and formiminotetrahydrofolate cyclodeaminase activity, EC 4.3.1.4
-
-
?
additional information
?
-
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primary reaction of the over-all reaction formimino-L-glutamate + tetrahydrofolate = N10-formyltetrahydrofolate + glutamate + NH3
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-
?
additional information
?
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not: formiminoglycine, very poor substrates: formimino-L-aspartic acid, formyl-L-glutamic acid
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-
?
additional information
?
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twin enzyme EC 2.1.2.5 and formiminotetrahydrofolate cyclodeaminase EC 4.3.1.4: enzyme system forming N5,10-methenyltetrahydrofolate from formiminoglutamate and tetrahydrofolate
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-
?
additional information
?
-
-
FTCD: bifunctional enzyme formiminotransferase cyclodeaminase efficiently channels polyglutamated folate between catalytic sites, only the octamer is able to directly transfer pentaglutamated intermediate between active sites, subunit structure
-
-
?
additional information
?
-
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FTCD: bifunctional enzyme formiminotransferase cyclodeaminase, EC 2.1.2.5 and EC 4.3.1.4, formiminotransferase domain: N-terminal 326 residues, detailed structure
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-
?
additional information
?
-
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molecular enzyme complex with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4, both activities are contained in a single polypeptide chain, no substrate: formiminoaspartate
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-
?
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
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
physiological substrate is (6S)-tetrahydrofolate
natural biosynthetic product is N5-formiminotetrahydrofolate
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
enzyme serves as additional entry point for the folate pool in liver
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
histidine degradation
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
histidine degradation
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
histidine degradation
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
histidine degradation
natural biosynthetic product is N5-formiminotetrahydrofolate
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.111
(6R,S)-tetrahydrofolate
-
recombinant His-tagged formiminotransferase domain
0.141
(6R,S)-tetrahydrofolate
-
wild-type bifunctional formiminotransferase cyclodeaminase
0.148
(6R,S)-tetrahydrofolate
-
recombinant His-tagged bifunctional formiminotransferase cyclodeaminase
0.0017
(6S)-tetrahydropteroylpentaglutamate
-
recombinant His-tagged bifunctional formiminotransferase cyclodeaminase
0.075
(6S)-tetrahydropteroylpentaglutamate
-
recombinant His-tagged formiminotransferase domain
5.8
N-formimino-L-glutamate
-
wild-type bifunctional formiminotransferase cyclodeaminase
6.7
N-formimino-L-glutamate
-
recombinant His-tagged bifunctional formiminotransferase cyclodeaminase
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
26000 per min per mol or 3250 per min per chain
-
additional information
additional information
-
3480-4620 per min: bifunctional formiminotransferase cyclodeaminase, 1920 per min: recombinant His-tagged formiminotransferase domain
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE 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). FTCD_PIG
541
0
58930
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
480000
approximately, native octameric bifunctional enzyme with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4
58926
8 * 58926, recombinant bifunctional enzyme with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4, calculated from cDNA sequence
37000
-
2 * 37000, recombinant His-tagged N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, calculated from the amino acid sequence
380000
-
recombinant His-tagged bifunctional formiminotransferase cyclodeaminase, gel filtration
438000
-
wild-type bifunctional formiminotransferase cyclodeaminase, gel filtration
62000
-
8 * 62000, bifunctional formiminotransferase cyclodeaminase, arranged as a circular tetramer of dimers
83000
-
recombinant His-tagged N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
8 * 58926, recombinant bifunctional enzyme with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4, calculated from cDNA sequence
dimer
homodimer
-
N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, dimer interface is important for the function of the domain
homooctamer
octamer
dimer
-
2 * 37000, recombinant His-tagged N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, calculated from the amino acid sequence
dimer
-
transferase domain is expressed in Escherichia coli as monofunctional dimer
homooctamer
-
each identical subunit of octameric bifunctional formiminotransferase cyclodeaminase consists of a transferase and a deaminase domain connected by a short linker sequence
octamer
-
8 * 62000, bifunctional formiminotransferase cyclodeaminase, arranged as a circular tetramer of dimers
octamer
-
8 * 59000-60000, bifunctional formiminotransferase cyclodeaminase, calculated from the amino acid sequence, circular tetramer of dimers, each subunit consists of an N-terminal transferase active domain and a C-terminal deaminase active domain separated by a linker sequence of 8-12 residues, both domains self-dimerize: existence of two types of subunit interfaces, transferase and deaminase activities are dependent on the formation of specific subunit interfaces
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the monofunctional formiminotransferase domain of FTCD, hanging-drop method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R135C
-
mutation analogous to mutant found in patient with glutamate formiminotransferase deficiency, reduction of enzyme activity to 61% of wild-type
R299P
-
mutation analogous to mutant found in patient with glutamate formiminotransferase deficiency, reduction of enzyme activity to 57% of wild-type
additional information
-
deletion mutants of formiminotransferase cyclodeaminase with transferase activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of recombinant bifunctional enzyme with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4, expressed in Escherichia coli
purification of recombinant hexahistidine-tagged formiminotransferase domain of FTCD
-
purification of twin enzyme EC 2.1.2.5 and formiminotetrahydrofolate cyclodeaminase EC 4.3.1.4, combination of affinity chromatography and isoelectric focusing
-
purification of wild type bifunctional formiminotransferase cyclodeaminase, 150fold purification of His-tagged recombinant enzyme, 60fold purification of His-tagged transferase domain, expressed in Escherichia coli BL21/DE3
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isolation and sequencing of cDNA clones encoding bifunctional enzyme with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4, cDNA encodes an amino acid sequence of 541 residues, expression in Escherichia coli
expression of full-length formiminotransferase cyclodeaminase and of isolated N-terminal transferase and C-terminal deaminase domains in Escherichia coli BL21/DE3 as His-tagged proteins
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Slavik, K.; Zizkovsky, V.; Slavikova, V.; Fort, P.
The purification of formiminotransferase and cyclodeaminase by combination of affinity chromatography and isoelectric focusing
Biochem. Biophys. Res. Commun.
59
1173-1184
1974
Sus scrofa
Tabor, H.; Wyngarden, L.
The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid
J. Biol. Chem.
234
1830-1846
1959
Bos taurus, Cavia porcellus, Felis catus, Homo sapiens, Mus musculus, Oryctolagus cuniculus, Sus scrofa
Silverman, M.; Keresztesy, J.C.; Koval, G.J.; Gardiner, R.C.
Citrovorum factor and the synthesis of formylglutamic acid
J. Biol. Chem.
226
83-94
1957
Sus scrofa
Beaudet, R.; Mackenzie, R.
Kinetic mechanism of formininotransferase from porcine liver
Biochim. Biophys. Acta
410
252-261
1975
Sus scrofa
Murley, L.L.; Mejia, N.R.; MacKenzie, R.E.
The nucleotide sequence of porcine formiminotransferase cyclodeaminase. Expression and purification from Escherichia coli
J. Biol. Chem.
268
22820-22824
1993
Sus scrofa (P53603)
Murley, L.L.; MacKenzie, R.E.
The two monofunctional domains of octameric formiminotransferase-cyclodeaminase exist as dimers
Biochemistry
34
10358-10364
1995
Sus scrofa
Kohls, D.; Sulea, T.; Purisima, E.O.; MacKenzie, R.E.; Vrielink, A.
The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: Implications for substrate channeling in a bifunctional enzyme
Structure
8
35-46
2000
Sus scrofa
Murley, L.L.; MacKenzie, R.E.
Monofunctional domains of formiminotransferase-cyclodeaminase retain similar conformational stabilities outside the bifunctional octamer
Biochim. Biophys. Acta
1338
223-232
1997
Sus scrofa
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