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Information on EC 2.1.2.5 - glutamate formimidoyltransferase
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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 expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
formiminotransferase-cyclodeaminase, glutamate formiminotransferase, glutamate formyltransferase, formiminoglutamic acid formiminotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 2.1.2.6
-
-
formerly
-
formiminoglutamic acid formiminotransferase
-
-
-
-
formiminoglutamic acid transferase
-
-
-
-
formiminoglutamic formiminotransferase
-
-
-
-
formiminotransferase, glutamate
-
-
-
-
FTCD
glutamate formiminotransferase
glutamate formyltransferase
-
-
-
-
glutamate formiminotransferase
-
-
-
-
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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
mechanism
-
5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate
catalytic mechanism
-
5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
formimino group transfer
-
-
-
-
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9032-83-1
-
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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,S)-tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
-
-
-
-
r
(6S)-tetrahydropteroylpentaglutamate + N-formimidoyl-L-glutamate
5-formiminotetrahydropteroylpentaglutamate + L-glutamate
-
-
-
-
r
N-formimidoyl-L-Glu-L-Glu-L-Glu + tetrahydrofolate
N-formimidoyl-L-Glu-L-Glu + 5-formimidoyltetrahydrofolate
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-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formyltetrahydrofolate + L-glutamate
N-formyl-L-glutamate + tetrahydrofolate
-
formation of N5-formyltetrahydrofolate + 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
-
r
5-formyltetrahydrofolate + L-glutamate
N-formyl-L-glutamate + tetrahydrofolate
-
folinic acid binding site, preference for (6R)-enantiomer of folinic acid
-
-
?
N-formimidoyl-L-Glu-L-Glu-L-Glu + tetrahydrofolate
N-formimidoyl-L-Glu-L-Glu + 5-formimidoyltetrahydrofolate
-
-
-
-
?
N-formimidoyl-L-Glu-L-Glu-L-Glu + tetrahydrofolate
N-formimidoyl-L-Glu-L-Glu + 5-formimidoyltetrahydrofolate
-
-
-
-
?
N-formimidoyl-L-Glu-L-Glu-L-Glu + tetrahydrofolate
N-formimidoyl-L-Glu-L-Glu + 5-formimidoyltetrahydrofolate
-
-
-
-
?
N-formimidoyl-L-Glu-L-Glu-L-Glu + tetrahydrofolate
N-formimidoyl-L-Glu-L-Glu + 5-formimidoyltetrahydrofolate
-
-
-
-
?
N-formimidoyl-L-Glu-L-Glu-L-Glu + tetrahydrofolate
N-formimidoyl-L-Glu-L-Glu + 5-formimidoyltetrahydrofolate
-
-
-
-
?
N-formimidoyl-L-Glu-L-Glu-L-Glu + tetrahydrofolate
N-formimidoyl-L-Glu-L-Glu + 5-formimidoyltetrahydrofolate
-
-
-
-
?
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
in addition to its enzymatic activity enzyme may have a second physiological function in mediating interaction of Golgi-derived membranes with microtubules
-
-
?
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
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
bifunctional formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmatic surface of the Golgi apparatus in vivo
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
bifunctional formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmatic surface of the Golgi apparatus in vivo
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
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metabolic enzyme involved in the conversion of histidine to glutamic acid
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
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histidine metabolism pathway, reaction occurs in vivo within the soluble phase of cytoplasm
-
?
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
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enzyme serves as additional entry point for the folate pool in liver
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
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histidine degradation
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
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histidine degradation
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
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histidine degradation
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
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histidine degradation
natural biosynthetic product is N5-formiminotetrahydrofolate
?
tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
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-
-
?
tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
FTCD in the centrosome may be associated with polyglutamylated residues of centriole microtubules and may play a role in providing centrioles with glutamate produced by cyclodeaminase domains of FTCD
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-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
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r
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
alpha-L-formamidinoglutaric acid, absolute specificity with regard to the isomers of tetrahydrofolate at position 6, reduced pteroylaspartic acid and reduced pteroyltriglutamic acid can replace tetrahydrofolate
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r
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
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specificity, equilibrium lies far on formation of formiminotetrahydrofolate and glutamate
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r
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
-
r
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
-
r
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
-
r
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
-
r
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
-
r
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
transfer of a single carbon from formiminoglutamate to tetrahydrofolate, product is 5-formiminotetrahydrofolate
-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
-
?
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
relatively specific for formiminoglutamic acid
-
r
tetrahydrofolate + N-formimino-L-glutamate
5-formiminotetrahydrofolate + L-glutamate
-
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
-
optimum number of glutamates for channeling of the product to the cyclodeaminase domain is five
-
?
additional information
?
-
-
primary reaction of the over-all reaction formimino-L-glutamate + tetrahydrofolate = N10-formyltetrahydrofolate + glutamate + NH3
-
-
?
additional information
?
-
-
primary reaction of the over-all reaction formimino-L-glutamate + tetrahydrofolate = N10-formyltetrahydrofolate + glutamate + NH3
-
-
?
additional information
?
-
-
not: formamidinoacetic acid, formylisoglutamine, formylglutamine, acetylglutamic acid
-
-
?
additional information
?
-
-
formation of glutamic acid is reversible while formation of ammonia is not
-
-
?
additional information
?
-
p60: bifunctional formiminotransferase cyclodeaminase, can mediate interaction between trans-Golgi network derived vesicles and microtubule in vitro, p60 may bind to the polyglutamate on microtubules, globular hydrophilic protein
-
-
?
additional information
?
-
-
p60: bifunctional formiminotransferase cyclodeaminase, can mediate interaction between trans-Golgi network derived vesicles and microtubule in vitro, p60 may bind to the polyglutamate on microtubules, globular hydrophilic protein
-
-
?
additional information
?
-
-
58K: formiminotransferase cyclodeaminase, bifunctional enzyme catalyzing two consecutive steps in the modification of tetrahydrofolate to 5,10-methenyl tetrahydrofolate
-
-
?
additional information
?
-
-
58K: formiminotransferase cyclodeaminase, bifunctional enzyme catalyzing two consecutive steps in the modification of tetrahydrofolate to 5,10-methenyl tetrahydrofolate
-
-
?
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
?
-
-
primary reaction of the over-all reaction formimino-L-glutamate + tetrahydrofolate = N10-formyltetrahydrofolate + glutamate + NH3
-
-
?
additional information
?
-
-
not: formiminoglycine, very poor substrates: formimino-L-aspartic acid, formyl-L-glutamic acid
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
-
FTCD: bifunctional enzyme formiminotransferase cyclodeaminase, EC 2.1.2.5 and EC 4.3.1.4, formiminotransferase domain: N-terminal 326 residues, detailed structure
-
-
?
additional information
?
-
-
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
tetrahydrofolate + N-formimidoyl-L-glutamate
5-formimidoyltetrahydrofolate + L-glutamate
FTCD in the centrosome may be associated with polyglutamylated residues of centriole microtubules and may play a role in providing centrioles with glutamate produced by cyclodeaminase domains of FTCD
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
5-formimidoyltetrahydrofolate + L-glutamate
tetrahydrofolate + N-formimidoyl-L-glutamate
-
-
-
-
?
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
in addition to its enzymatic activity enzyme may have a second physiological function in mediating interaction of Golgi-derived membranes with microtubules
-
-
?
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
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
bifunctional formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmatic surface of the Golgi apparatus in vivo
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
bifunctional formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmatic surface of the Golgi apparatus in vivo
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
metabolic enzyme involved in the conversion of histidine to glutamic acid
-
?
N-formiminoglutamate + tetrahydrofolate
5-formiminotetrahydrofolate + L-glutamate
-
histidine metabolism pathway, reaction occurs in vivo within the soluble phase of cytoplasm
-
?
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
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NH4+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ca2+
-
0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
La3+
-
0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
Li+
-
0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
Mg2+
-
0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
Na+
-
0.1 M, strong inhibition in decreasing order: La3+, Ca2+, Mg2+, Li+, Na+, K+
proteinase K
-
degradation of bifunctional formiminotransferase cyclodeaminase
-
additional information
-
not inhibited by formamidinoacetic acid, gamma-benzyl-formamidinoglutaric acid, formic acid, formamide, formylglutamine, formylisoglutamine
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
glutamate formimidoyltransferase deficiency
Characteristics and outcomes of patients with formiminoglutamic aciduria detected through newborn screening.
glutamate formimidoyltransferase deficiency
Cloning and characterization of human FTCD on 21q22.3, a candidate gene for glutamate formiminotransferase deficiency.
glutamate formimidoyltransferase deficiency
Falsely elevated C4-carnitine as expression of glutamate formiminotransferase deficiency in tandem mass spectrometry newborn screening.
glutamate formimidoyltransferase deficiency
Formiminoglutamic aciduria in a slightly retarded boy with chronic obstructive lung disease.
glutamate formimidoyltransferase deficiency
Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer.
glutamate formimidoyltransferase deficiency
The molecular basis of glutamate formiminotransferase deficiency.
glutamate formimidoyltransferase deficiency
Update and new concepts in vitamin responsive disorders of folate transport and metabolism.
Hepatitis, Autoimmune
Characterization of the antigenicity of the formiminotransferase-cyclodeaminase in type 2 autoimmune hepatitis.
Hepatitis, Autoimmune
Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer.
Malnutrition
Resistance of liver formiminoglutamic acid transferase to experimental protein malnutrition in weanling rats.
methionine synthase deficiency
Update and new concepts in vitamin responsive disorders of folate transport and metabolism.
methylenetetrahydrofolate dehydrogenase (nad+) deficiency
Update and new concepts in vitamin responsive disorders of folate transport and metabolism.
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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
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
chicken, several isoforms of p60, bifunctional formiminotransferase cyclodeaminase
Uniprot
brenda
no activity in Herpetosiphon aurantiacus
the gene encoding glycine formimidoyltransferase is an inactive pseudogene, the histidine utilization hut operon in Herpetosiphon aurantiacus is entirely broken up, suggesting that this pathway no longer functions
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
DU249 chicken hepatoma cells, contain p60 but no measurable formiminotransferase activity, may be due to the low expression of p60
brenda
additional information
-
richest tissue source of formiminotransferase cyclodeaminase, liver-specific enzyme
brenda
additional information
-
no activity in the soluble proteins of brain, heart, lung, testis, intestinal mucosa, diaphragm muscle or spleen
brenda
additional information
-
undetectable in adrenal gland, blood cells, marrow cells, brain, epididymis, heart, small intestine, kidney, lung, skeletal muscle, spleen and testis
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
more abundantly around the mother centriole. The centrosome localization of FTCD continues throughout the cell cycle and is not disrupted after Golgi fragmentation, which is induced by colcemid and brefeldin A. FTCD in the centrosome may be associated with polyglutamylated residues of centriole microtubules and may play a role in providing centrioles with glutamate produced by cyclodeaminase domains of FTCD
brenda
localized on Golgi membranes as well as on some potentially Golgi complex-derived vesicular structures
-
brenda
additional information
reversibly associated with membrane, complex formation is increased by anti-liver cytosol type 1 autoantibodies
brenda
localized on Golgi membranes as well as on some potentially Golgi complex-derived vesicular structures
brenda
-
formiminotransferase cyclodeaminase, 58K, is associated with the cytoplasmic surface of the Golgi apparatus in vivo, cytoplasmically oriented peripheral membrane protein of the Golgi membranes
brenda
-
formiminotransferase cyclodeaminase, 58K, is a peripherically associated Golgi protein, binding is tight but not dependent on presence of intact microtubules, association is likely to be mediated by a protein, dynamic component of the Golgi, a proportion of FTCD molecules cycles between the Golgi and earlier compartments of the secretory pathway
brenda
-
formiminotransferase cyclodeaminase binds bovine brain microtubules, but not rat liver microtubules in vitro
brenda
additional information
no interaction of enzyme with liver-specific cytoskeleton proteins
-
brenda
additional information
-
no interaction of enzyme with liver-specific cytoskeleton proteins
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme deficiency results in formiminoglutamic aciduria with elevated plasma and urine formiminoglutamic acid levels
metabolism
physiological function
metabolism
-
glutamate formiminotransferase is a histidine breakdown enzyme. 5-Formimidoyltetrahydrofolate in C1-metabolism, overview
metabolism
-
glutamate formiminotransferase is a histidine breakdown enzyme. 5-Formimidoyltetrahydrofolate in C1-metabolism, overview
metabolism
-
glutamate formiminotransferase is a histidine breakdown enzyme. 5-Formimidoyltetrahydrofolate in C1-metabolism, overview
metabolism
-
glutamate formiminotransferase is a histidine breakdown enzyme. 5-Formimidoyltetrahydrofolate in C1-metabolism, overview
metabolism
-
glutamate formiminotransferase is a histidine breakdown enzyme. 5-Formimidoyltetrahydrofolate in C1-metabolism, overview
-
metabolism
-
glutamate formiminotransferase is a histidine breakdown enzyme. 5-Formimidoyltetrahydrofolate in C1-metabolism, overview
-
physiological function
-
utilization of supplied 5-formyltetrahydrofolate by Streptococcus pyogenes requires expression of the native glutamate formiminotransferase
physiological function
-
utilization of supplied 5-formyltetrahydrofolate by Streptococcus pyogenes requires expression of the native glutamate formiminotransferase
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
480000
58000
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
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
480000
-
approximately, native octameric bifunctional enzyme with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4
480000
approximately, native octameric bifunctional enzyme with formiminotransferase and cyclodeaminase activity, EC 2.1.2.5 and EC 4.3.1.4
58000
-
2 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE, a single 35 kDa protein is cross-linked to each dimer, it may play a role in the association of the protein to the Golgi membrane, functional formiminotransferase activity unit of FTCD is a dimer with binding sites for glutamate and folate
58000
-
4 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE
58000
-
8 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
-
N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, dimer interface is important for the function of the domain
homooctamer
octamer
tetramer
-
4 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE
dimer
-
2 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE, a single 35 kDa protein is cross-linked to each dimer, it may play a role in the association of the protein to the Golgi membrane, functional formiminotransferase activity unit of FTCD is a dimer with binding sites for glutamate and folate
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 * 58000, bifunctional formiminotransferase cyclodeaminase exists as dimeric, tetrameric and octameric complexes, SDS-PAGE
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
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
p60, bifunctional formiminotransferase cyclodeaminase, is post-translationally modified
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
arrangement of subunits like a square doughnut, coupling of three subunits governs the octamer-dependent sequential enzyme activities
crystal structure of the monofunctional formiminotransferase domain of FTCD, hanging-drop method
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R135C
-
mutation naturally occuring in patient with mild form of putative glutamate formiminotransferase deficiency
R299P
-
mutation naturally occuring in patient with mild form of putative glutamate formiminotransferase deficiency
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no loss of activity after dialysis against phosphate buffer or 0.05 M EDTA, pH 7.4
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified desalted recombinant enzyme, 100 mM K-phosphate, pH 7.3, 10% v/v glycerol, flash frozen in liquid N2, loss of 80% activity after 8 weeks
-
-80C, purified desalted recombinant enzyme, 100 mM K-phosphate, pH 7.3, 10% v/v glycerol, flash frozen in liquid N2, stable for at least 8 weeks
-80C, purified desalted recombinant enzyme, 100 mM K-phosphate, pH 7.3, 10% v/v glycerol, flash frozen in liquid N2, stable for at least 8 weeks
-
-80C, purified desalted recombinant enzyme, 100 mM K-phosphate, pH 7.3, 10% v/v glycerol, flash frozen in liquid N2, stable for at least 8 weeks
-
-80C, purified desalted recombinant enzyme, 100 mM K-phosphate, pH 7.3, 10% v/v glycerol, flash frozen in liquid N2, stable for at least 8 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification from liver
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
-
recombinant enzyme from Escherichia coli strain BL21-CodonPlus (DE3)-RIPL by affinity chormatography
recombinant enzyme from Escherichia coli strain BL21-CodonPlus (DE3)-RIPL by affinity chormatography
-
recombinant enzyme from Escherichia coli strain BL21-CodonPlus (DE3)-RIPL by affinity chormatography
-
recombinant enzyme from Escherichia coli strain BL21-CodonPlus (DE3)-RIPL by affinity chormatography
-
recombinant enzyme from Escherichia coli strain BL21-CodonPlus (DE3)-RIPL by affinity chormatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA encoding formiminotransferase cyclodeaminase is cloned and sequenced
-
cDNA encoding formiminotransferase cyclodeaminase is cloned, characterized and partially sequenced
-
cloning and sequencing of the cDNA coding for p60, the chicken homologue of bifunctional formiminotransferase cyclodeaminase, a protein of 541 amino acids
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
-
glutamate formiminotransferase, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, functional complementation of an Escherichia coli DELTAygfA 5-CHO-THF cycloligase deletion mutant with strain MG1655 background
-
glutamate formiminotransferase, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, functional complementation of an Escherichia coli DELTAygfA 5-formimidoyltetrahydrofolate cycloligase deletion mutant with strain MG1655 background
glutamate formiminotransferase, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, functional complementation of an Escherichia coli DELTAygfA 5-N-formimidoyltetrahydrofolate cycloligase deletion mutant with strain MG1655 background
-
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
glutamate formiminotransferase, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, functional complementation of an Escherichia coli DELTAygfA 5-formimidoyltetrahydrofolate cycloligase deletion mutant with strain MG1655 background
-
glutamate formiminotransferase, phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21-CodonPlus (DE3)-RIPL, functional complementation of an Escherichia coli DELTAygfA 5-formimidoyltetrahydrofolate cycloligase deletion mutant with strain MG1655 background
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
subcellular localization of protein may influence production of autoantibodies and their role in the pathogenesis of type 2 autoimmune hepatitis
molecular biology
-
bifunctional formiminotransferase cyclodeaminase provides a novel marker to study ER-Golgi dynamics
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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
brenda
Hennig, D.; Scales, S.J.; Moreau, A.; Murley, L.L.; De Mey, J.; Kreis, T.E.
A formiminotransferase cyclodeaminase isoform is localized to the Golgi complex and can mediate interaction of trans-Golgi network-derived vesicles with microtubules
J. Biol. Chem.
273
19602-19611
1998
Meleagris gallopavo, Gallus gallus (Q9YH58)
brenda
Gao, Y.S.; Alvarez, C.; Nelson, D.S.; Sztul, E.
Molecular cloning, characterization, and dynamics of rat formiminotransferase cyclodeaminase, a Golgi-associated 58-kDa protein
J. Biol. Chem.
273
33825-33834
1998
Rattus norvegicus
brenda
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, Oryctolagus cuniculus, Felis catus, Homo sapiens, Mus musculus, Sus scrofa
brenda
Miller, A.; Waelsch, H.
Formimino transfer from formamidinoglutaric acid to tetrahydrofolic acid
J. Biol. Chem.
228
397-417
1957
Bos taurus, Rattus norvegicus
brenda
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
brenda
Beaudet, R.; Mackenzie, R.
Kinetic mechanism of formininotransferase from porcine liver
Biochim. Biophys. Acta
410
252-261
1975
Sus scrofa
brenda
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)
brenda
Bashour, A.M.; Bloom, G.S.
58K, a microtubule-binding Golgi protein, is a formiminotransferase cyclodeaminase
J. Biol. Chem.
273
19612-19617
1998
Rattus norvegicus
brenda
Murley, L.L.; MacKenzie, R.E.
The two monofunctional domains of octameric formiminotransferase-cyclodeaminase exist as dimers
Biochemistry
34
10358-10364
1995
Sus scrofa
brenda
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
brenda
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
brenda
Renous, R.; Lapierre, P.; Djilali-Saiah, I.; Vitozzi, S.; Alvarez, F.
Characterization of the antigenicity of the formiminotransferase-cyclodeaminase in type 2 autoimmune hepatitis
Exp. Cell Res.
292
332-341
2004
Homo sapiens (O95954), Homo sapiens
brenda
Mao, Y.; Vyas, N.K.; Vyas, M.N.; Chen, D.H.; Ludtke, S.J.; Chiu, W.; Quiocho, F.A.
Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer
EMBO J.
23
2963-2971
2004
Rattus norvegicus (O88618)
brenda
Hilton, J.F.; Christensen, K.E.; Watkins, D.; Raby, B.A.; Renaud, Y.; de la Luna, S.; Estivill, X.; MacKenzie, R.E.; Hudson, T.J.; Rosenblatt, D.S.
The molecular basis of glutamate formiminotransferase deficiency
Hum. Mutat.
22
67-73
2003
Homo sapiens, Sus scrofa
brenda
Hagiwara, H.; Tajika, Y.; Matsuzaki, T.; Suzuki, T.; Aoki, T.; Takata, K.
Localization of Golgi 58K protein (formiminotransferase cyclodeaminase) to the centrosome
Histochem. Cell Biol.
126
251-259
2006
Homo sapiens (O05954)
brenda
Jeanguenin, L.; Lara-Nunez, A.; Pribat, A.; Mageroy, M.H.; Gregory, J.F.; Rice, K.C.; de Crecy-Lagard, V.; Hanson, A.D.
Moonlighting glutamate formiminotransferases can functionally replace 5-formyltetrahydrofolate cycloligase
J. Biol. Chem.
285
41557-41566
2010
Streptococcus pyogenes, Thermoplasma acidophilum, Picrophilus torridus, Candidatus Koribacter versatilis, no activity in Herpetosiphon aurantiacus, Candidatus Koribacter versatilis Ellin345, Streptococcus pyogenes M1
brenda
Majumdar, R.; Yori, A.; Rush, P.W.; Raymond, K.; Gavrilov, D.; Tortorelli, S.; Matern, D.; Rinaldo, P.; Feldman, G.L.; Oglesbee, D.
Allelic spectrum of formiminotransferase-cyclodeaminase gene variants in individuals with formiminoglutamic aciduria
Mol. Genet. Genomic Med.
5
795-799
2017
Homo sapiens
brenda
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