Enzymatic properties of squalene epoxidase from Saccharomyces cerevisiea
書誌事項
- タイトル別名
-
- Enzymatic Properties of Squalene Epoxidase from Saccharomyces cerevisiae.
この論文をさがす
説明
Squalene epoxidase is a microsomal membrane-associated enzyme that acts as an important regulator in the sterol biosynthetic pathway. In this study, the enzymatic properties of squalene epoxidase from Saccharomyces cerevisiae were examined. Unlike Candida squalene epoxidase, S. cerevisiae squalene epoxidase required NADPH for enzyme reaction. However, S. cerevisiae enzyme reaction did not require FAD or autologous S105 fraction. Unlike rat squalene epoxidase, the activity of S. cerevisiae was reduced by Triton X-100, a nonionic detergent. Terbinafine, an inhibitor of fungal squalene epoxidase, inhibited the enzyme in a non-competitive manner, while NB-598, an inhibitor of mammalian squalene epoxidase, barely inhibited it in a partially non-competitive manner. Thus, the properties of squalene epoxidase from S. cerevisiae were different from those of squalene epoxidase from rats and Candida, which were previously known. We propose that a species difference of squalene epoxidase exists not only between animals and fungi but between Candida and Saccharomyces.
収録刊行物
-
- Biological & Pharmaceutical Bulletin
-
Biological & Pharmaceutical Bulletin 16 (4), 349-352, 1993
公益社団法人 日本薬学会
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1390282679598875776
-
- NII論文ID
- 110003640249
-
- NII書誌ID
- AA10885497
-
- ISSN
- 13475215
- 09186158
-
- PubMed
- 8358382
-
- 本文言語コード
- en
-
- 資料種別
- journal article
-
- データソース種別
-
- JaLC
- Crossref
- PubMed
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可