3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase

In enzymology, a 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA 24-hydroxylase (EC 1.17.99.3) is an enzyme that catalyzes the chemical reaction

(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H₂O + acceptor

\rightleftharpoons

(24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26- oyl-CoA + reduced acceptor

The 3 substrates of this enzyme are (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA, H₂O, and acceptor, whereas its two products are (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26-oyl-CoA, and reduced acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on CH or CH₂ groups with other acceptors. The systematic name of this enzyme class is (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA:ac ceptor 24-oxidoreductase (24R-hydroxylating). Other names in common use include trihydroxycoprostanoyl-CoA oxidase, THC-CoA oxidase, THCA-CoA oxidase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoyl-CoA oxidase, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate 24-hydroxylase. This enzyme participates in the ppar signaling pathway.

References

Gustafsson J (1975). "Biosynthesis of cholic acid in rat liver. 24-Hydroxylation of 3alpha, 7alpha, 12alpha-trihydroxy-5beta-cholestanoic acid". J. Biol. Chem. 250 (20): 8243–7. PMID 240854.
Schepers L, Van Veldhoven PP, Casteels M, Eyssen HJ, Mannaerts GP (1990). "Presence of three acyl-CoA oxidases in rat liver peroxisomes. An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase". J. Biol. Chem. 265 (9): 5242–6. PMID 2156865.
Goethals M, Vandekerckhove J, Van Veldhoven PP, Mannaerts GP (1996). "Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins". Eur. J. Biochem. 240 (3): 660–6. doi:10.1111/j.1432-1033.1996.0660h.x. PMID 8856068.
Pedersen JI, Eggertsen G, Hellman U, Andersson U, Bjorkhem I (1997). "Molecular cloning and expression of cDNA encoding 3alpha,7alpha,12alpha-trihydroxy-5beta-chole stanoyl-CoA oxidase from rabbit liver". J. Biol. Chem. 272 (29): 18481–9. doi:10.1074/jbc.272.29.18481. PMID 9218493.
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.

Other oxidoreductases (EC 1.15-1.21)

1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3

1.16: Oxidizing metal ions	Ceruloplasmin

1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase

1.18: Acting on iron-sulfur proteins as donors	Nitrogenase

1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)

1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5

1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

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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