Literature summary for 2.1.2.5 extracted from

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 (2000), Structure, 8, 35-46.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the monofunctional formiminotransferase domain of FTCD, hanging-drop method	Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
62000	-	8 * 62000, bifunctional formiminotransferase cyclodeaminase, arranged as a circular tetramer of dimers	Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
N-formiminoglutamate + tetrahydrofolate	Sus scrofa	physiological substrate is (6S)-tetrahydrofolate	5-formiminotetrahydrofolate + L-glutamate	natural biosynthetic product is N5-formiminotetrahydrofolate	?
N-formiminoglutamate + tetrahydrofolate	Sus scrofa	histidine degradation	5-formiminotetrahydrofolate + L-glutamate	natural biosynthetic product is N5-formiminotetrahydrofolate	?

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
purification of recombinant hexahistidine-tagged formiminotransferase domain of FTCD	Sus scrofa

Reaction

Reaction	Comment	Organism	Reaction ID
5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate	catalytic mechanism	Sus scrofa	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5-formyltetrahydrofolate + L-glutamate	folinic acid binding site, preference for (6R)-enantiomer of folinic acid	Sus scrofa	N-formyl-L-glutamate + tetrahydrofolate	-	?
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	Sus scrofa	?	-	?
N-formiminoglutamate + tetrahydrofolate	physiological substrate is (6S)-tetrahydrofolate	Sus scrofa	5-formiminotetrahydrofolate + L-glutamate	natural biosynthetic product is N5-formiminotetrahydrofolate	?
N-formiminoglutamate + tetrahydrofolate	histidine degradation	Sus scrofa	5-formiminotetrahydrofolate + L-glutamate	natural biosynthetic product is N5-formiminotetrahydrofolate	?
tetrahydrofolate + N-formimino-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	Sus scrofa	5-formiminotetrahydrofolate + L-glutamate	labile 5-formiminotetrahydrofolate product	?
tetrahydropteroylpentaglutamate + N-formimino-L-glutamate	optimum number of glutamates for channeling of the product to the cyclodeaminase domain is five	Sus scrofa	5-formiminotetrahydropteroylpentaglutamate + L-glutamate	-	?

Subunits

Subunits	Comment	Organism
homodimer	N-terminal formiminotransferase domain of bifunctional formiminotransferase cyclodeaminase, dimer interface is important for the function of the domain	Sus scrofa
octamer	8 * 62000, bifunctional formiminotransferase cyclodeaminase, arranged as a circular tetramer of dimers	Sus scrofa

Cofactor

Cofactor	Comment	Organism	Structure
tetrahydrofolate	-	Sus scrofa

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Release 2023.1 (January 2023)