Fluoroacetyl-CoA thioesterase
| Fluoroacetyl-CoA thioesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.2.29 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
The enzyme fluoroacetyl-CoA thioesterase (EC 3.1.2.29; systematic name fluoroacetyl-CoA hydrolase) catalyses the following reaction:[1][2][3]
- fluoroacetyl-CoA + H2O fluoroacetate + CoA
Fluoroacetate is extremely toxic.
References
[edit]- ^ Meyer JJ, Grobbelaar N, Vleggaar R, Louw AI (1992). "Fluoroacetyl-coenzyme-A hydrolase-like activity in Dichapetalum cymosum". J. Plant Physiol. 139 (3): 369–372. doi:10.1016/s0176-1617(11)80352-4.
- ^ Huang F, Haydock SF, Spiteller D, Mironenko T, Li TL, O'Hagan D, Leadlay PF, Spencer JB (May 2006). "The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: a thioesterase confers resistance to fluoroacetyl-coenzyme A". Chemistry & Biology. 13 (5): 475–84. doi:10.1016/j.chembiol.2006.02.014. PMID 16720268.
- ^ Dias MV, Huang F, Chirgadze DY, Tosin M, Spiteller D, Dry EF, Leadlay PF, Spencer JB, Blundell TL (July 2010). "Structural basis for the activity and substrate specificity of fluoroacetyl-CoA thioesterase FlK". The Journal of Biological Chemistry. 285 (29): 22495–504. doi:10.1074/jbc.m110.107177. PMC 2903362. PMID 20430898.
External links
[edit]- Fluoroacetyl-CoA+thioesterase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
