Glutamate formimidoyltransferase
| Formiminotransferase domain, N-terminal subdomain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Formiminotransferase domain of formiminotransferase-cyclodeaminase, homodimer, Sus scrofa | |||||||||
| Identifiers | |||||||||
| Symbol | FTCD_N | ||||||||
| Pfam | PF07837 | ||||||||
| InterPro | IPR012886 | ||||||||
| SCOP2 | 1qd1 / SCOPe / SUPFAM | ||||||||
| |||||||||
| Formiminotransferase domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 the crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase. | |||||||||
| Identifiers | |||||||||
| Symbol | FTCD | ||||||||
| Pfam | PF02971 | ||||||||
| InterPro | IPR013802 | ||||||||
| SCOP2 | 1qd1 / SCOPe / SUPFAM | ||||||||
| |||||||||
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
[edit]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
[edit]- ^ 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. doi:10.1016/S0021-9258(19)70586-9. PMID 7410436.[permanent dead link]
- ^ 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. S2CID 38730850.
External links
[edit]- Glutamate+formimidoyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
