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Studies on Steroid Monooxygenase from Cylindrocarpon radicicola ATCC 11011.1 Purification and Characterization
https://doi.org/10.24517/00060082
https://doi.org/10.24517/0006008293eaf8f6-0719-44b8-983a-ec7d1ec0d398
| 名前 / ファイル | ライセンス | アクション |
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SC-PR-ITAGAKI-E-99_815.pdf (817.9 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||||
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| 公開日 | 2020-12-03 | |||||||
| タイトル | ||||||||
| タイトル | Studies on Steroid Monooxygenase from Cylindrocarpon radicicola ATCC 11011.1 Purification and Characterization | |||||||
| 言語 | ||||||||
| 言語 | eng | |||||||
| 資源タイプ | ||||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||||
| 資源タイプ | journal article | |||||||
| ID登録 | ||||||||
| ID登録 | 10.24517/00060082 | |||||||
| ID登録タイプ | JaLC | |||||||
| 著者 |
Itagaki, Eiji
× Itagaki, Eiji |
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| 著者別表示 |
板垣, 英治
× 板垣, 英治
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| 書誌情報 |
The Journal of Biochemistry 巻 99, 号 3, p. 815-824, 発行日 1986 |
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| ISSN | ||||||||
| 収録物識別子タイプ | ISSN | |||||||
| 収録物識別子 | 0021-924X | |||||||
| NCID | ||||||||
| 収録物識別子タイプ | NCID | |||||||
| 収録物識別子 | AA00694073 | |||||||
| 出版者 | ||||||||
| 出版者 | The Japanese Biochemical Society | |||||||
| 出版者（別名） | ||||||||
| 出版者 | 日本生化学会 | |||||||
| 抄録 | ||||||||
| 内容記述タイプ | Abstract | |||||||
| 内容記述 | A steroid monooxygenase from cells of a fungus, Cylindrocarpon radicicola ATCC 11011, grown in the presence of progesterone has been purified by affinity chromatography on a pregnenolone-Sepharose column. The obtained enzyme was gel electrophoretically homogeneous and exhibited a molecular weight of about 115, 000. SDS-gel electrophoresis revealed that the enzyme consisted of two equal-sized subunits with a molecular weight of 56, 000. Sedimentation equilibrium analysis at 20°C indicated that the enzyme protein behaved as a mixture of monomeric and dimeric subunit species. The enzyme contained one molecule of FAD in each subunit and exhibited absorption maxima at 375 and 440 nm. The monooxygenase catalyzed a Baeyer-Villiger type oxidation, i.e., oxygenative esterification of C21-20-ketosteroid to form an acetate ester of C19- 17β-hydroxysteroid with consumptions of NADPH and molecular oxygen. The enzyme displayed a wide substrate specificity toward C21-20-ketosteroids, while it strictly required NADPH as the external electron donor in a ratio of 1:1:1 for ketosteroid: NADPH: molecular oxygen. Kinetic study showed the enzyme to have very high affinity for progesterone. |
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| 権利 | ||||||||
| 権利情報 | Copyright © The Japanese Biochemical Society 日本生化学会 | |||||||
| 著者版フラグ | ||||||||
| 出版タイプ | VoR | |||||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||
| 関連URI | ||||||||
| 識別子タイプ | URI | |||||||
| 関連識別子 | http://www.jbsoc.or.jp/ | |||||||
| 関連名称 | http://www.jbsoc.or.jp/ | |||||||
| 関連URI | ||||||||
| 識別子タイプ | URI | |||||||
| 関連識別子 | https://academic.oup.com/jb | |||||||
| 関連名称 | https://academic.oup.com/jb | |||||||
| 関連URI | ||||||||
| 識別子タイプ | URI | |||||||
| 関連識別子 | https://www.jstage.jst.go.jp/browse/biochemistry1922/-char/ja | |||||||
| 関連名称 | https://www.jstage.jst.go.jp/browse/biochemistry1922/-char/ja | |||||||
