1992年12月
PHYSIOLOGICAL ROLES OF ACETOACETYL-COA THIOLASE IN N-ALKANE-UTILIZABLE YEAST, CANDIDA-TROPICALIS - POSSIBLE CONTRIBUTION TO ALKANE DEGRADATION AND STEROL BIOSYNTHESIS
JOURNAL OF BIOCHEMISTRY
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- ,
- ,
- ,
- 巻
- 112
- 号
- 6
- 開始ページ
- 845
- 終了ページ
- 848
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- 出版者・発行元
- JAPANESE BIOCHEMICAL SOC
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.
- リンク情報
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- J-GLOBAL
- https://jglobal.jst.go.jp/detail?JGLOBAL_ID=200902069632666049
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/1363552
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:A1992KB75200023&DestApp=WOS_CPL
- ID情報
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- ISSN : 0021-924X
- J-Global ID : 200902069632666049
- PubMed ID : 1363552
- Web of Science ID : WOS:A1992KB75200023