Enoyl-CoA hydratase 2

Enoyl-CoA hydratase 2 (2-enoyl-CoA hydratase 2, AtECH2, ECH2, MaoC, MFE-2, PhaJAc, D-3-hydroxyacyl-CoA hydro-lyase, D-specific 2-trans-enoyl-CoA hydratase) is an enzyme (EC 4.2.1.119) with systematic name (3R)-3-hydroxyacyl-CoA hydro-lyase. This enzyme catalyses the following chemical reaction on D-3-hydroxyacyl-CoA

This enzyme catalyses a hydration step in peroxisomal beta oxidation.

References

Koski KM, Haapalainen AM, Hiltunen JK, Glumoff T (February 2005). "Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzyme type 2". Journal of Molecular Biology. 345 (5): 1157–69. doi:10.1016/j.jmb.2004.11.009. PMID 15644212.
Fukui T, Shiomi N, Doi Y (February 1998). "Expression and characterization of (R)-specific enoyl coenzyme A hydratase involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae". Journal of Bacteriology. 180 (3): 667–73. PMC 106937. PMID 9457873.
Koski MK, Haapalainen AM, Hiltunen JK, Glumoff T (July 2003). "Crystallization and preliminary crystallographic data of 2-enoyl-CoA hydratase 2 domain of Candida tropicalis peroxisomal multifunctional enzyme type 2". Acta Crystallographica Section D. 59 (Pt 7): 1302–5. doi:10.1107/s090744490300982x. PMID 12832794.
Hisano T, Fukui T, Iwata T, Doi Y (January 2001). "Crystallization and preliminary X-ray analysis of (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis" (PDF). Acta Crystallographica Section D. 57 (Pt 1): 145–7. doi:10.1107/s0907444900014062. PMID 11134939.
Goepfert S, Hiltunen JK, Poirier Y (November 2006). "Identification and functional characterization of a monofunctional peroxisomal enoyl-CoA hydratase 2 that participates in the degradation of even cis-unsaturated fatty acids in Arabidopsis thaliana". The Journal of Biological Chemistry. 281 (47): 35894–903. doi:10.1074/jbc.m606383200. PMID 16982622.
Engeland K, Kindl H (August 1991). "Evidence for a peroxisomal fatty acid beta-oxidation involving D-3-hydroxyacyl-CoAs. Characterization of two forms of hydro-lyase that convert D-(-)-3-hydroxyacyl-CoA into 2-trans-enoyl-CoA". European Journal of Biochemistry. 200 (1): 171–8. doi:10.1111/j.1432-1033.1991.tb21064.x. PMID 1879422.

External links

Enoyl-CoA+hydratase+2 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e Carbon–oxygen lyases (EC 4.2) (primarily dehydratases)
4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase
4.2.2: Acting on polysaccharides	Hyaluronate lyase Pectin lyase
4.2.3: Acting on phosphates	Threonine synthase
4.2.99: Other	Carboxymethyloxysuccinate lyase Hydroperoxide lyase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 4.2.1