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J. Biochem, 1992, Vol. 112, No. 6 845-848
© 1992 Japanese Biochemical Society

research-article

Physiological Roles of Acetoacetyl-CoA Thiolase in n-Alkane-Utilizable Yeast, Candida tropicalis: Possible Contribution to Alkane Degradation and Sterol Biosynthesis

Tatsuo Kurihara*, Mitsuyoshi Ueda*, Naomi Kamasawa**, Masako Osumi** and Atsuo Tanaka*,1

*Laboratory of Industrial Biochemistry, Department of Industrial Chemistry, Faculty of Engineering, Kyoto University Yoshida, Sakyo-ku, Kyoto 606-01
**Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University Mejiro-dai, Bunkyo-ku, Tokyo 112

2To whom correspondence should b addressed

The presence of two types of thiolases, acetoacetyl-CoA thiolase and 3-ketoacyl-CoA thiolase, was demonstrated in peroxisomes of n-alkane-grown Candida tropicalis [Kurihara, T., Ueda, M., & Tanaka, A. (1989) J. Biochem. 106, 474–478], while acetoacetyl-CoA thiolase was also shown to be present in cytosol. The activity of the enzyme in cytosol was constant irrespective of culture conditions, while the peroxisomal enzyme was inducibly synthesized in the alkane-grown yeast cells. These results indicate that peroxisomal acetoacetyl-CoA thiolase participates in alkane degradation, while the cytosolic enzyme is associated with other fundamental metabolic processes, probably sterol biosynthesis, because this enzyme can catalyze the first step of the sterol biosynthesis. 3-Hydroxy-3-methylglutaryl (HMG)-CoA reductase, a key regulatory enzyme of sterol biosynthesis, was found to be localized exclusively in microsomes of the alkane-grown yeast cells. These results suggest that yeast peroxisomes do not contribute to sterol biosynthesis, unlike the case of mammalian cells.


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