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3-keto-5α-steroid-Δ4-dehydrogenase from Nocardia corallina: Purification and characterization
http://hdl.handle.net/2297/14569
http://hdl.handle.net/2297/145696a15a922-4f9e-400a-af95-bbaa8fd358ed
| 名前 / ファイル | ライセンス | アクション |
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SC-PR-ITAGAKI-E-581.pdf (746.1 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||||
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| 公開日 | 2017-10-03 | |||||||
| タイトル | ||||||||
| タイトル | 3-keto-5α-steroid-Δ4-dehydrogenase from Nocardia corallina: Purification and characterization | |||||||
| 言語 | en | |||||||
| 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 | |||||||
| 著者 |
Hatta, Takashi
× Hatta, Takashi× Wakabayashi, Teruko× Itagaki, Eiji |
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| 著者別表示 |
板垣, 英治
× 板垣, 英治
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| 提供者所属 | ||||||||
| 内容記述タイプ | Other | |||||||
| 内容記述 | 金沢大学自然科学研究科 | |||||||
| 提供者所属 | ||||||||
| 内容記述タイプ | Other | |||||||
| 内容記述 | 金沢大学理工研究域自然システム学系 | |||||||
| 書誌情報 |
Journal of Biochemistry 巻 109, 号 4, p. 581-586, 発行日 1991-01-01 |
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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 | 日本生化学会 = Japanese Biochemical Society | |||||||
| 抄録 | ||||||||
| 内容記述タイプ | Abstract | |||||||
| 内容記述 | The inducible 3-keto-5α-steroid-Δ4-dehydrogenase of Nocardia corallina was purified to homogeneity using affinity chromatography on 19-nortestosterone-17-acetoxyaminoethyl Sepharose 4B. SDS-polyacrylamide gel electrophoresis, gel filtration and spectral analysis of flavin suggest that the purified dehydrogenase is a monomeric protein of M(r) 60,000 containing one flavin. It has a typical absorption spectrum of flavoprotein with maxima at 457, 375, and 277 nm. The values shifted to 470 and 395 nm on binding of 19-nortestosterone. The enzyme catalyzed the dehydrogenation of 3-keto-5α-steroid at the 4- and 5-position, e.g. the conversion of 5α-androst-1-ene-3,17-dione to 1,4-androstadiene-3,17-dione with the reduction of phenazine methosulfate. The substrate 3-ketosteroid has essentially the 5α-configuration. The enzyme did not reduce potassium ferricyanide but did reduce cytochrome c at a moderate rate, and exhibited only a weak steroid oxidase activity. Stereochemical study demonstrated that the enzyme abstracts the 4β, 5α-hydrogens of the substrate as a hydrogen ion through a protein-based reaction and as a hydride ion by transfer to FAD, respectively. The enzyme oxidizes a wide variety of 3-keto-5α-steroids but not 3β-hydroxysteroid. The dehydrogenase also catalyzed steroid transhydrogenation between 3-keto-5α-steroid and 3-keto-1,4-diene-steroid. The properties of this enzyme are compared with those of 3-keto-steroid-Δ1-dehydrogenase. | |||||||
| 権利 | ||||||||
| 権利情報 | Copyright © 1991 Japanese Biochemical Society | |||||||
| 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 | ||||||||
| 関連タイプ | isIdenticalTo | |||||||
| 識別子タイプ | DOI | |||||||
| 関連識別子 | https://doi.org/10.1093/oxfordjournals.jbchem.a123423 | |||||||
