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Essential tyrosine residues in 3-ketosteroid-Δ1-dehydrogenase from Rhodococcus rhodochrous
http://hdl.handle.net/2297/14570
http://hdl.handle.net/2297/14570f013eac8-6dcd-43a7-a0c2-7ee3ab42920d
| 名前 / ファイル | ライセンス | アクション |
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SC-PR-ITAGAKI-E-662.pdf (846.3 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 tyrosine residues in 3-ketosteroid-Δ1-dehydrogenase from Rhodococcus rhodochrous | |||||||
| 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 |
Fujii, Chifumi
× Fujii, Chifumi× Morii, Shingo× Kadode, Michiaki× Sawamoto, Shizue× Iwami, Masafumi× 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 126, 号 4, p. 662-667, 発行日 1999-01-01 |
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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 | |||||||
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| 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.a022500 | |||||||
| 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 | Tetranitromethane treatment of 3-ketosteroid-Δ1-dehydrogenase of Rhodococcus rhodechrous caused loss of the catalytic activity in a time- and concentration-dependent manner. Peptides (P-81) and (PN-83) were isolated from tryptic digests of the native and tetranitromethane-treated enzyme proteins, respectively. PN-83 was the nitrated form of P-81. The amino acid sequence was GGAPLIDYLESDDDLEFMVYPWPDYFGK (positions 97-124 of the dehydrogenase sequence). PN-83 showed a low yield of PTH-Tyr of position 116, i.e. less than 5% of that of P-81, and instead a high yield of PTH-3-nitrotyrosine. This indicated that tetranitromethane modifies Y-116 under the experimental conditions used. Mutation of Y-104, Y-116, and Y-121 to smaller amino acid residues, Phe, Ser, or Ala, significantly changed the catalytic activity of the dehydrogenase. All of the mutants contained FAD and exhibited the same spectrophotometric properties as those of the wild type enzyme. The K(m) values for 4-androstene-3,17-dione of the Y-104, Y-116, and Y-121 mutants changed to large values. The most drastic change was observed for Y116A. The K(d) values for 1,4-androstadiene-3,17-dione of the Y116 mutants changed to 1.5-2.6-fold larger values than that of the recombinant enzyme. The Y-121 mutant enzymes exhibited catalytic activities like those of the recombinant enzyme, but the catalytic efficiencies of Y121F and Y121A drastically decreased to 0.014-0.054% of that of the recombinant enzyme. The present results indicate that Y-121 plays an important role in the catalytic function, and that Y-116 and Y-104 act on binding of the substrate steroid. | |||||||
| 権利 | ||||||||
| 権利情報 | Copyright © 1999 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 | |||||||
