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Structural analyses of the deduced amino acid sequences of a novel type heme-copper terminal oxidase, cytochrome aco3, from alkalophilic Bacillus YN-2000
https://doi.org/10.24517/00010121
https://doi.org/10.24517/0001012193622878-9b2a-44ab-8008-4781eab62671
| 名前 / ファイル | ライセンス | アクション |
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SC-PR-FUKUMORI-Y-1075.pdf (600.1 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 | Structural analyses of the deduced amino acid sequences of a novel type heme-copper terminal oxidase, cytochrome aco3, from alkalophilic Bacillus YN-2000 | |||||||
| 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 | 10.24517/00010121 | |||||||
| ID登録タイプ | JaLC | |||||||
| 著者 |
Denda, Kimitoshi
× Denda, Kimitoshi× Oshima, Akira× Fukumori, Yoshihiro |
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| 著者別表示 |
福森, 義宏
× 福森, 義宏
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| 提供者所属 | ||||||||
| 内容記述タイプ | Other | |||||||
| 内容記述 | 金沢大学大学院自然科学研究科動態生理学 | |||||||
| 書誌情報 |
Canadian Journal of Microbiology 巻 47, 号 12, p. 1075-1081, 発行日 2001-01-01 |
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| ISSN | ||||||||
| 収録物識別子タイプ | ISSN | |||||||
| 収録物識別子 | 0008-4166 | |||||||
| NCID | ||||||||
| 収録物識別子タイプ | NCID | |||||||
| 収録物識別子 | AA00597703 | |||||||
| DOI | ||||||||
| 関連タイプ | isIdenticalTo | |||||||
| 識別子タイプ | DOI | |||||||
| 関連識別子 | 10.1139/cjm-47-12-1075 | |||||||
| 出版者 | ||||||||
| 出版者 | National Research Council Canada | |||||||
| 抄録 | ||||||||
| 内容記述タイプ | Abstract | |||||||
| 内容記述 | Cytochrome aco3 from a facultatively alkalophilic bacterium, Bacillus YN-2000, was found to be alkaline- and heat-tolerant. To better understand the structural features of Bacillus YN-2000 cytochrome aco3, the gene encoding this enzyme was cloned and sequenced. Nucleotide sequence analyses of the region neighboring the acoI (subunit I) gene revealed that the acoII (subunit II) and acoIII (subunit III) genes were concomitantly clustered upstream and downstream of the acoI gene, respectively, forming an operon with transcriptional polarity. The deduced amino acid sequence of subunit I was highly similar to that of cytochrome caa3 from thermophilic bacterium Bacillus PS3 in which the heme a3 could be replaced with heme o. Furthermore, a marked paucity of basic amino acid residues was found in the cytochrome c-binding subunit II, which might be a result of the adaptation to a highly alkaline external milieu. | |||||||
| 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 | |||||||
