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

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)-3α,7α,12α,24-tetrahydroxy-5beta-cholestanoyl-CoA hydro-lyase . Other names in common use include 46 kDa hydratase 2, and (24R,25R)-3α,7α,12α,24-tetrahydroxy-5β-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". The Biochemical Journal. 328 (2): 377–82. doi:10.1042/bj3280377. PMC 1218931. PMID 9371691.
Xu R, Cuebas DA (April 1996). "The reactions catalyzed by the inducible bifunctional enzyme of rat liver peroxisomes cannot lead to the formation of bile acids". Biochemical and Biophysical Research Communications. 221 (2): 271–8. doi:10.1006/bbrc.1996.0585. PMID 8619845.
Kokawa NI; 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; 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.
Kurosawa T, Sato M, Nakano H, Fujiwara M, Murai T, Yoshimura T, Hashimoto T (February 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". Annual Review of Biochemistry. 72: 137–74. doi:10.1146/annurev.biochem.72.121801.161712. PMID 12543708.

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)

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