Venoyl-CoA hydratase 2

Enoyl-CoA hydratase 2 (EC 4.2.1.119, 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 with systematic name (3R)-3-hydroxyacyl-CoA hydro-lyase.^[1]^[2]^[3]^[4]^[5]^[6] This enzyme catalyses the following chemical reaction

(3R)-3-hydroxyacyl-CoA

\rightleftharpoons

(2E)-2-enoyl-CoA + H₂O

This enzyme catalyses a hydration step in peroxisomal beta-oxidation.

References

↑ Koski, K.M., Haapalainen, A.M., Hiltunen, J.K. and Glumoff, T. (2005). "Crystal structure of 2-enoyl-CoA hydratase 2 from human peroxisomal multifunctional enzyme type 2". J. Mol. Biol. 345: 1157–1169. doi:10.1016/j.jmb.2004.11.009. PMID 15644212.
↑ Fukui, T., Shiomi, N. and Doi, Y. (1998). "Expression and characterization of (R)-specific enoyl coenzyme A hydratase involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae". J. Bacteriol. 180: 667–673. PMID 9457873.
↑ Koski, M.K., Haapalainen, A.M., Hiltunen, J.K. and Glumoff, T. (2003). "Crystallization and preliminary crystallographic data of 2-enoyl-CoA hydratase 2 domain of Candida tropicalis peroxisomal multifunctional enzyme type 2". Acta Crystallogr. D Biol. Crystallogr. 59: 1302–1305. doi:10.1107/s090744490300982x. PMID 12832794.
↑ Hisano, T., Fukui, T., Iwata, T. and Doi, Y. (2001). "Crystallization and preliminary X-ray analysis of (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis". Acta Crystallogr. D Biol. Crystallogr. 57: 145–147. doi:10.1107/s0907444900014062. PMID 11134939.
↑ Goepfert, S., Hiltunen, J.K. and Poirier, Y. (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". J. Biol. Chem. 281: 35894–35903. doi:10.1074/jbc.m606383200. PMID 16982622.
↑ Engeland, K. and Kindl, H. (1991). "Evidence for a peroxisomal fatty acid β-oxidation involving D-3-hydroxyacyl-CoAs. Characterization of two forms of hydro-lyase that convert D-(-)-3-hydroxyacyl-CoA into 2-trans-enoyl-CoA". Eur. J. Biochem. 200: 171–178. doi:10.1111/j.1432-1033.1991.tb21064.x. PMID 1879422.

External links

Enoyl-CoA hydratase 2 at the US National Library of Medicine Medical Subject Headings (MeSH)

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

4.2.3: Acting on phosphates	Threonine synthase

4.2.99: Other	Carboxymethyloxysuccinate lyase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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