Domain Characterization of Cyclosporin Regio-Specific Hydroxylases in Rare Actinomycetes
文献类型：期刊论文
| 作者 | Woo, Min-Woo1; Lee, Bo-Ram1; Nah, Hee-Ju1; Choi, Si-Sun1; Li, Shengying2 ; Kim, Eung-Soo1
|
| 刊名 | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
 |
| 出版日期 | 2015-10-01 |
| 卷号 | 25期号:10页码:1634-1639 |
| 关键词 | Cytochrome P450 cyclosporin A regio-selectivity actinomycetes |
| 英文摘要 | Cytochrome P450 hydroxylase (CYP) in actinomycetes plays an important role in the biosynthesis and bioconversion of various secondary metabolites. Two unique CYPs named CYP-sb21 and CYP-pa1, which were identified from Sebekia benihana and Pseudonocardia autotrophica, respectively, were proven to transfer a hydroxyl group at the 4th or 9th N-methyl leucine position of immunosuppressive agent cyclosporin A (CsA). Interestingly, these two homologous CYPs showed different CsA regio-selectivities. CYP-sb21 exhibited preferential hydroxylation activity at the 4th position over the 9th position, whereas CYP-pa1 showed the opposite preference. To narrow down the CYP domain critical for CsA regio-selectivity, each CYP was divided into four domains, and each domain was swapped with its counterpart from the other CYP. A total of 18 hybrid CYPs were then individually tested for CsA regioselectivity. Although most of the hybrid CYPs failed to exhibit a significant change in regioselectivity in the context of CsA hydroxylation, hybrid CYP-pa1 swapped with the second domain of CYP-sb21 showed a higher preference for the 9th position. Moreover, hybrid CYP-sb21 containing seven amino acids from the 2nd domain of CYP-pa1 showed higher preference for the 4th position. These results imply that the 2nd domain of CsA-specific CYP plays a critical role in CsA regio-selectivity, thereby setting the stage for biotechnological application of CsA regio-selective hydroxylation. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biotechnology & Applied Microbiology ; Microbiology |
| 研究领域[WOS] | Biotechnology & Applied Microbiology ; Microbiology |
| 关键词[WOS] | CYTOCHROME-P450 COMPLEMENT CYPOME ; SEBEKIA-BENIHANA ; FERREDOXIN REDUCTASE ; STREPTOMYCES ; GENE ; DISRUPTION ; CONVERSION ; BINDING |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000365443800008 |
| 公开日期 | 2016-02-26 |
| 源URL | [http://ir.qibebt.ac.cn/handle/337004/6799]  |
| 专题 | 青岛生物能源与过程研究所_酶工程团队 |
| 作者单位 | 1.Inha Univ, Dept Biol Engn, Inchon 402751, South Korea 2.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Qingdao 266101, Shandong, Peoples R China |
| 推荐引用方式 GB/T 7714 | Woo, Min-Woo,Lee, Bo-Ram,Nah, Hee-Ju,et al. Domain Characterization of Cyclosporin Regio-Specific Hydroxylases in Rare Actinomycetes[J]. JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY,2015,25(10):1634-1639. |
| APA | Woo, Min-Woo,Lee, Bo-Ram,Nah, Hee-Ju,Choi, Si-Sun,Li, Shengying,&Kim, Eung-Soo.(2015).Domain Characterization of Cyclosporin Regio-Specific Hydroxylases in Rare Actinomycetes.JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY,25(10),1634-1639. |
| MLA | Woo, Min-Woo,et al."Domain Characterization of Cyclosporin Regio-Specific Hydroxylases in Rare Actinomycetes".JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY 25.10(2015):1634-1639. |
入库方式： OAI收割
来源：青岛生物能源与过程研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。