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Essential histidine residue in 3-ketosteroid-Δ1-dehydrogenase
http://hdl.handle.net/2297/14566
http://hdl.handle.net/2297/14566e2027f6b-bb87-40a7-b81f-c46697cb4865
| 名前 / ファイル | ライセンス | アクション |
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SC-PR-ITAGAKI-E-594.pdf (862.6 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 | Essential histidine residue in 3-ketosteroid-Δ1-dehydrogenase | |||||||
| 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 |
Matsushita, Hiroyuki
× Matsushita, Hiroyuki× 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 111, 号 5, p. 594-599, 発行日 1992-01-01 |
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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 variation with pH of kinetic parameters was examined for 3-ketosteroid-Δ1-dehydrogenase from Nocardia corallina. The V(max)/K(m) profile for 4-androstenedione indicates that activity is lost upon protonation of a cationic acid-type group with a pK value of 7.7. The enzyme was inactivated by diethylpyrocarbonate at pH 7.4 and the inactivation was substantially prevented by androstadienedione. Analyses of reactivation with neutral hydroxylamine, pH variation, and spectral changes of the inactivated enzyme revealed that the inactivation arises from modification of a histidine residue. Studies with [14C]diethylpyrocarbonate provided Support for the idea that the 1-2 essential histidine residues are essential for the catalytic activity of the enzyme. Dye-sensitized photooxidation led to 50% inactivation of the enzyme with the decomposition of two histidine residues. This inactivation was also prevented by androstadienedione. Dancyl chloride caused a loss of the enzyme activity. Modifiers of glutamic acid, aspartic acid, cysteine, and lysine did not affect the enzyme activity. Butanedione and phenylglyoxal in the presence of borate rapidly inactivated the enzyme, indicating that arginine residues also have a crucial function in the active site. The data described support the previously proposed mechanism of β-oxidation of 3-ketosteroid. | |||||||
| 権利 | ||||||||
| 権利情報 | Copyright © 1992 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.a123803 | |||||||
