Glutamate formimidoyltransferase

Formiminotransferase domain, N-terminal subdomain

the crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase.

Identifiers

Symbol

FTCD_N

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Formiminotransferase domain

the crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase.

Identifiers

Symbol

FTCD

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

In molecular biology, Glutamate formimidoyltransferase is a methyltransferase enzyme which uses tetrahydrofolate as part of histidine catabolism. It catalyses two reactions:

5-formimidoyltetrahydrofolate + L-glutamate <=> tetrahydrofolate + N-formimidoyl-L-glutamate

5-formyltetrahydrofolate + L-glutamate <=> tetrahydrofolate + N-formyl-L-glutamate

It is classified under EC 2.1.2.5 and in mammals is found as part of a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase activity.^[1]

Structure

The formiminotransferase (FT) domain of formiminotransferase-cyclodeaminase (FTCD) forms a homodimer, with each protomer comprising two subdomains. The formiminotransferase domain has an N-terminal subdomain that is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.^[2] In humans, deficiency of this enzyme results in a disease phenotype.^[3]

References

^ MacKenzie RE, Aldridge M, Paquin J (10 October 1980). "The bifunctional enzyme formiminotransferase-cyclodeaminase is a tetramer of dimers". J. Biol. Chem. 255 (19): 9474–8. PMID 7410436. http://www.jbc.org/cgi/reprint/255/19/9474.
^ Kohls D, Sulea T, Purisima EO, MacKenzie RE, Vrielink A (January 2000). "The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme". Structure 8 (1): 35–46. doi:10.1016/S0969-2126(00)00078-2. PMID 10673422.
^ Hilton JF, Christensen KE, Watkins D, Raby BA, Renaud Y, de la Luna S, Estivill X, MacKenzie RE, Hudson TJ, Rosenblatt DS (July 2003). "The molecular basis of glutamate formiminotransferase deficiency". Hum. Mutat. 22 (1): 67–73. doi:10.1002/humu.10236. PMID 12815595.

External links

MeSH Glutamate+formimidoyltransferase

Transferase: one carbon transferases (EC 2.1)

2.1.1: Methyl-

N-	Histamine N-methyltransferase - Phenylethanolamine N-methyltransferase - Amine N-methyltransferase - Phosphatidylethanolamine N-methyltransferase

O-	5-hydroxyindole-O-methyltransferase/Acetylserotonin O-methyltransferase - Catechol-O-methyl transferase

Homocysteine	Betaine-homocysteine methyltransferase - Homocysteine methyltransferase - Methionine synthase

Other	Phosphatidyl ethanolamine methyltransferase - DNMT3B - Histone methyltransferase - Thymidylate synthase - DNA methyltransferase - Thiopurine methyltransferase

2.1.2: Hydroxymethyl-,
Formyl- and Related

Hydroxymethyltransferase	Serine hydroxymethyltransferase - 3-methyl-2-oxobutanoate hydroxymethyltransferase

Formyltransferase	Phosphoribosylglycinamide formyltransferase - Inosine monophosphate synthase

Other	Glutamate formimidoyltransferase - Aminomethyltransferase

2.1.3: Carboxy- and Carbamoyl

Carboxy	methylmalonyl-CoA carboxytransferase

Carbamoyl	Aspartate carbamoyltransferase - Ornithine carbamoyltransferase - Oxamate carbamoyltransferase - Putrescine carbamoyltransferase - 3-hydroxymethylcephem carbamoyltransferase - Lysine carbamoyltransferase - N-acetylornithine carbamoyltransferase

2.1.4: Amidino

Arginine:glycine amidinotransferase

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

This article incorporates text from the public domain Pfam and InterPro IPR013802

This article incorporates text from the public domain Pfam and InterPro IPR012886