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Journal of Lipid Research, Vol. 41, 93-98, January 2000
Copyright © 2000 by Lipid Research, Inc.

Original Article

Substrate specificities of peroxisomal members of short-chain alcohol dehydrogenase superfamily: expression and characterization of dehydrogenase part of Candida tropicalis multifunctional enzyme

Yong-Mei Qina,b, Matti H. Poutanenc, and Dmitry K. Novikova,b
a Biocenter Oulu, University of Oulu, FIN-90570 Oulu, Finland
b Department of Biochemistry, University of Oulu, FIN-90570 Oulu, Finland
c Department of Physiology, University of Turku, FIN-20520 Turku, Finland

Correspondence to: Dmitry K. Novikov

In addition to several other enzymes, the short-chain alcohol dehydrogenase superfamily includes a group of peroxisomal multifunctional enzymes involved in fatty acid and cholesterol side-chain ß-oxidation. Mammalian peroxisomal multifunctional enzyme type 2 (perMFE-2) is a 2-enoyl-CoA hydratase-2/(R)-3-hydroxyacyl-CoA dehydrogenase. As has been shown previously, perMFE-2 hydrates (24E)-3{alpha},7{alpha},12{alpha}-trihydroxy-5ß-cholest-24-enoyl-CoA to (24R, 25R)-3{alpha},7{alpha},12{alpha},24{xi}-tetrahydroxy-5ß-cholestanoyl-CoA, which has been characterized as a physiological intermediate in cholic acid synthesis. Out of four possible stereoisomers of 3{alpha},7{alpha},12{alpha},24{xi}-tetrahydroxy-5ß-cholestanoyl-CoA, the mammalian perMFE-2 dehydrogenates only the (24R,25R)-isomer. The yeast peroxisomal multifunctional enzyme (MFE) was first described as 2-enoyl-CoA hydratase-2/(R)-3-hydroxyacyl-CoA dehydrogenase. To investigate the stereospecificity of yeast peroxisomal MFE, the two dehydrogenase domains of C. tropicalis MFE were expressed in E. coli as a 65 kDa recombinant protein. This protein catalyzes the dehydrogenation of straight-chain (R)-3-hydroxyacyl-CoAs, but it is devoid of (S)-3-hydroxyacyl-CoA dehydrogenase and 2-enoyl-CoA hydratase activities. The protein dehydrogenates (24R,25R)- and (24R,25S)-isomers of 3{alpha},7{alpha}, 12{alpha},24{xi}-tetrahydroxy-5ß-cholestanoyl-CoA. Interestingly, the protein also shows 17ß-estradiol dehydrogenase activity.

As a monofunctional (R)-specific 3-hydroxyacyl-CoA dehydrogenase is currently unavailable, this recombinant enzyme can be used to study the stereochemistry of bile acid synthesis.—Qin, Y-M., M. H. Poutanen, and D. K. Novikov. Substrate specificities of peroxisomal members of short-chain alcohol dehydrogenase superfamily: expression and characterization of dehydrogenase part of Candida tropicalis multifunctional enzyme. J. Lipid Res. 2000. 41: 93;–98.

Supplementary key words: short-chain alcohol dehydrogenase superfamily, peroxisomes, fatty acids, bile acids


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