WEKO3
インデックスリンク
アイテム
3-Ketosteroid-Δ1 -dehydrogenase of Rhodococcus rhodochrous: Sequencing of the genomic DNA and hyperexpression, purification, and characterization of the recombinant enzyme
http://hdl.handle.net/2297/14574
http://hdl.handle.net/2297/1457484d00522-e0a1-4bec-87de-e5e8cd1dfa44
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
SC-PR-ITAGAKI-E-1026.pdf (1.2 MB)
|
|
| Item type | 学術雑誌論文 / Journal Article(1) | |||||||
|---|---|---|---|---|---|---|---|---|
| 公開日 | 2017-10-03 | |||||||
| タイトル | ||||||||
| タイトル | 3-Ketosteroid-Δ1 -dehydrogenase of Rhodococcus rhodochrous: Sequencing of the genomic DNA and hyperexpression, purification, and characterization of the recombinant enzyme | |||||||
| 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 |
Fujii, Chifumi
× Fujii, Chifumi× Morii, Shingo× Miyoshi, Toshio× Iwami, Masafumi× Itagaki, Eiji |
|||||||
| 著者別表示 |
板垣, 英治
× 板垣, 英治
|
|||||||
| 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 124, 号 5, p. 1026-1032, 発行日 1998-11-01 |
|||||||
| ISSN | ||||||||
| 収録物識別子タイプ | ISSN | |||||||
| 収録物識別子 | 0021-924X | |||||||
| item_4_source_id_11 | ||||||||
| 収録物識別子タイプ | NCID | |||||||
| 収録物識別子 | AA00694073 | |||||||
| item_4_relation_12 | ||||||||
| 関連タイプ | isIdenticalTo | |||||||
| 識別子タイプ | DOI | |||||||
| 関連識別子 | https://www.doi.org/10.24517/00010996 | |||||||
| 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 gene encoding 3-ketosteroid-Δ1-dehydrogenase from Rhodococcus rhodochrous was cloned and sequenced. The gene (ksdD) consists of 1,536 nucleotides and encodes an enzyme protein of 511 amino acid residues. The amino terminal methionine residue was deleted in the mature protein. The amino acids involved in the flavin binding site are conserved in the dehydrogenase sequence. The deduced amino acid sequence is highly homologous to that from Arthrobacter simplex but less so to that from Pseudomonas testosteroni. Upstream of the gene was located a heat shock protein gene, dnaJ, and downstream, a gene of a hypothetical protein. The enzyme gene was ligated with an expression vector to construct a plasmid pDEX-3 and introduced into Escherichia coli cells. The transformed cells hyperexpressed the 3-ketosteroid-Δ1-dehydrogenase as an active and soluble protein at more than 30 times the level of R. rhodochrous cells. Purification of the recombinant 3-ketosteroid-Δ1-dehydrogenase from the E. coli cells by a simplified procedure yielded about 13 mg of enzyme protein/liter of the bacterial culture. The purified recombinant dehydrogenase exhibited identical molecular and catalytic properties to the R. rhodochrous enzyme. | |||||||
| 権利 | ||||||||
| 権利情報 | Copyright © 1998Japanese 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.a022195 | |||||||
