3alfa,7alfa,12alfa-triidrossi-5beta-colestanoil-CoA 24-idrossilasi

3alfa,7alfa,12alfa-triidrossi- -5beta-colestanoil-CoA 24-idrossilasi
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Numero EC1.17.99.3
ClasseOssidoreduttasi
Nome sistematico
(25R)-3α,7α,12α-triidrossi-5β-colestan-26-oil-CoA:accettore 24-ossidoreduttasi (24R-idrossilante)
Altri nomi
triidrossicoprostanoil-CoA ossidasi; THC-CoA ossidasi; THCA-CoA ossidasi; 3α,7α,12α-triidrossi-5β-colestanoil-CoA ossidasi; 3α,7α,12α-triidrossi-5β-colestan-26-oato 24-idrossilasi
Banche datiBRENDA, EXPASY, GTD, PDB (RCSB PDB PDBe PDBj PDBsum)
Fonte: IUBMB

La 3alfa,7alfa,12alfa-triidrossi-5beta-colestanoil-CoA 24-idrossilasi è un enzima appartenente alla classe delle ossidoreduttasi, che catalizza la seguente reazione:

(25R)-3α,7α,12α-triidrossi-5β-colestan-26-oil-CoA + H2O + accettore (24R,25R)-3α,7α,12α,24-tetraidrossi-5β-colestan-26-oil-CoA + accettore ridotto

L'enzima richiede ATP. La reazione nei mammiferi probabilmente coinvolge una deidrogenazione per generare un doppio legame 24(25), seguita da un'idratazione. In ogni caso, negli anfibi come il rospo Bombina orientalis, è probabile che il prodotto venga formato attraverso l'idrossilazione diretta della catena laterale satura del (25R)-3α,7α,12α-triidrossi-5β-colestan-26-oato e non mediante idratazione del doppio legame 24(25). Nei microsomi, l'acido libero è preferito all'estere del coenzima A, mentre nei mitocondri l'estere del coenzima A è preferito alla forma di acido libero del substrato.

Bibliografia

  • Dieuaide-Noubhani, M., Novikov, D., Baumgart, E., Vanhooren, J.C., Fransen, M., Goethals, M., Vandekerckhove, J., Van Veldhoven, P.P. and Mannaerts, G.P., Erratum report. 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, in Eur. J. Biochem., vol. 243, 1997, pp. 537–537, Entrez PubMed 8856068.
  • Dieuaide-Noubhani, M., Novikov, D., Baumgart, E., Vanhooren, J.C., Fransen, M., Goethals, M., Vandekerckhove, J., Van Veldhoven, P.P. and Mannaerts, G.P., 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, in Eur. J. Biochem., vol. 240, 1996, pp. 660–666, Entrez PubMed 8856068.
  • Schepers, L., Van Veldhoven, P.P., Casteels, M., Eyssen, H.J. and Mannaerts, G.P., 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, in J. Biol. Chem., vol. 265, 1990, pp. 5242–5246, Entrez PubMed 2156865.
  • Gustafsson, J., Biosynthesis of cholic acid in rat liver. 24-Hydroxylation of 3α,7α,12α-trihydroxy-5β-cholestanoic acid, in J. Biol. Chem., vol. 250, 1975, pp. 8243–8247, Entrez PubMed 240854.
  • Pedersen, J.I., Eggertsen, G., Hellman, U., Andersson, U. and Björkhem, I., Molecular cloning and expression of cDNA encoding 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA oxidase from rabbit liver, in J. Biol. Chem., vol. 272, 1997, pp. 18481–18489, Entrez PubMed 9218493.
  • Russell, D.W., The enzymes, regulation, and genetics of bile acid synthesis, in Annu. Rev. Biochem., vol. 72, 2003, pp. 137–174, Entrez PubMed 12543708.
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