Biology:Glutamate formimidoyltransferase
| Formiminotransferase domain, N-terminal subdomain | |||||||||
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 Formiminotransferase domain of formiminotransferase-cyclodeaminase, homodimer, Sus scrofa | |||||||||
| Identifiers | |||||||||
| Symbol | FTCD_N | ||||||||
| Pfam | PF07837 | ||||||||
| InterPro | IPR012886 | ||||||||
| SCOP2 | 1qd1 / SCOPe / SUPFAM | ||||||||
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| Formiminotransferase domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 the crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase. | |||||||||
| Identifiers | |||||||||
| Symbol | FTCD | ||||||||
| Pfam | PF02971 | ||||||||
| InterPro | IPR013802 | ||||||||
| SCOP2 | 1qd1 / SCOPe / SUPFAM | ||||||||
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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
- ↑ "The bifunctional enzyme formiminotransferase-cyclodeaminase is a tetramer of dimers". J. Biol. Chem. 255 (19): 9474–8. 10 October 1980. doi:10.1016/S0021-9258(19)70586-9. PMID 7410436. http://www.jbc.org/cgi/reprint/255/19/9474.
- ↑ "The crystal structure of the formiminotransferase domain of formiminotransferase-cyclodeaminase: implications for substrate channeling in a bifunctional enzyme". Structure 8 (1): 35–46. January 2000. doi:10.1016/S0969-2126(00)00078-2. PMID 10673422.
- ↑ "The molecular basis of glutamate formiminotransferase deficiency". Hum. Mutat. 22 (1): 67–73. July 2003. doi:10.1002/humu.10236. PMID 12815595. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=33776.
External links
- Glutamate+formimidoyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)
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