| enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase | |||||||
|---|---|---|---|---|---|---|---|
 Enoyl-CoA hydratase hexamer from a rat with active site in orange and substrate in red. | |||||||
| Identifiers | |||||||
| Symbol | EHHADH | ||||||
| Alt. symbols | ECHD | ||||||
| NCBI gene | 1962 | ||||||
| HGNC | 3247 | ||||||
| OMIM | 607037 | ||||||
| RefSeq | NM_001966 | ||||||
| UniProt | Q08426 | ||||||
| Other data | |||||||
| EC number | 4.2.1.17 | ||||||
| Locus | Chr. 3 q26.3-q28 | ||||||
| |||||||
Enoyl-CoA hydratase (ECH) or crotonase[1] is an enzyme EC 4.2.1.17 that hydrates the double bond between the second and third carbons on 2-trans/cis-enoyl-CoA:[2]
ECH is essential to metabolizing fatty acids in beta oxidation to produce both acetyl CoA and energy in the form of ATP.[2]
ECH of rats is a hexameric protein (this trait is not universal, but human enzyme is also hexameric), which leads to the efficiency of this enzyme as it has 6 active sites. This enzyme has been discovered to be highly efficient, and allows people to metabolize fatty acids into energy very quickly. In fact this enzyme is so efficient that the rate for short chain fatty acids is equivalent to that of diffusion-controlled reactions.[3]
- ^ "EC 4.2.1.17". www.sbcs.qmul.ac.uk. Retrieved 2018-09-05.
- ^ a b Allenbach, L; Poirier, Y (2000). "Analysis of the Alternative Pathways for the β-Oxidation of Unsaturated Fatty Acids Using Transgenic Plants Synthesizing Polyhydroxyalkanoates in Peroxisomes". Plant Physiology. 124 (3): 1159–1168. doi:10.1104/pp.124.3.1159. ISSN 0032-0889. PMC 59215. PMID 11080293.
- ^ Engel CK, Kiema TR, Hiltunen JK, Wierenga RK (February 1998). "The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule". Journal of Molecular Biology. 275 (5): 847–59. doi:10.1006/jmbi.1997.1491. PMID 9480773.