3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase

In enzymology, a 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase (EC 4.2.1.107) is an enzyme that catalyzes the chemical reaction

(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA

\rightleftharpoons

(24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA + H₂O

Thus, the substrate of this enzyme are (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA, whereas its two products are (24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA and H₂O.

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA hydro-lyase [(24E)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA-forming]. Other names in common use include 46 kDa hydratase 2, and (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA hydro-lyase.

References

Qin YM, Haapalainen AM, Conry D, Cuebas DA, Hiltunen JK, Novikov DK (December 1997). "Recombinant 2-enoyl-CoA hydratase derived from rat peroxisomal multifunctional enzyme 2: role of the hydratase reaction in bile acid synthesis". Biochem. J. 328: 377–82. PMC 1218931. PMID 9371691.
Xu R, Cuebas DA (1996). "The reactions catalyzed by the inducible bifunctional enzyme of rat liver peroxisomes cannot lead to the formation of bile acids". Biochem. Biophys. Res. Commun. 221 (2): 271–8. doi:10.1006/bbrc.1996.0585. PMID 8619845.
Kokawa NI and Morisaki M (1988). "Synthesis and determination of stereochemistry of four diastereoisomers at the C-24 and C-25 positions of 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oic acid and cholic acid". Chem. Pharm. Bull. 36: 134–141. doi:10.1248/cpb.36.134.
Sonoda Y, Sato Y and Morisaki M (1988). "Non-stereoselective conversion of the four diastereoisomers at the C-24 and C-25 positions of 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oic acid and cholic acid". Chem. Pharm. Bull. 36: 142–145. doi:10.1248/cpb.36.142.
Hashimoto T; Sato, M; Nakano, H; Fujiwara, M; Murai, T; Yoshimura, T; Hashimoto, T (2001). "Conjugation reactions catalyzed by bifunctional proteins related to beta-oxidation in bile acid biosynthesis". Steroids. 66 (2): 107–14. doi:10.1016/S0039-128X(00)00217-8. PMID 11146090.
Russell DW (2003). "The enzymes, regulation, and genetics of bile acid synthesis". Annu. Rev. Biochem. 72: 137–74. doi:10.1146/annurev.biochem.72.121801.161712. PMID 12543708.

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)

This article is issued from Wikipedia - version of the Thursday, March 31, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.