Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity
文献类型：期刊论文
| 作者 | Wu, Xiao-Bin1; Tian, Xiu-Yun1; Ji, Jun-Jie1; Wu, Wei-Bin1; Fan, Ke-Qiang1,2; Yang, Ke-Qian1 |
| 刊名 | BIOTECHNOLOGY LETTERS
 |
| 出版日期 | 2011-04-01 |
| 卷号 | 33期号:4页码:805-812 |
| 关键词 | Acremonium chrysogenum C-terminus Expandase Kinetics Mutagenesis |
| ISSN号 | 0141-5492 |
| 通讯作者 | Yang, KQ |
| 英文摘要 | Deacetoxy/deacetylcephalosporin C synthase (acDAOC/DACS) from Acremonium chrysogenum is a bifunctional enzyme that catalyzes both the ring-expansion of penicillin N to deacetoxycephalosporin C and the hydroxylation of the latter to deacetylcephalosporin C. The R308 residue located in close proximity to the C-terminus of acDAOC/DACS was mutated to the other 19 amino acids. In the resulting mutant pool, R308L, R308I, R308T and R308V showed significant improvement in their ability to convert penicillin analogs, thus confirming the role of R308 in controlling substrate selectivity, the four amino acids all possess short aliphatic sidechains that may improve hydrophobic interactions with the substrates. The mutant R308I showed the highest reactivity for penicillin G, with 3-fold increase in k(cat)/K(m) ratio and 7-fold increase in relative activity. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biotechnology & Applied Microbiology |
| 研究领域[WOS] | Biotechnology & Applied Microbiology |
| 关键词[WOS] | RING-EXPANSION ACTIVITY ; AMINO-ACID ALTERATIONS ; PENICILLIN-G ; COMPLETE LIBRARY ; CATALYSIS ; TERMINUS ; BINDING ; CONVERSION ; MUTATIONS ; ENZYME |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000288548900023 |
| 公开日期 | 2013-11-07 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/5071]  |
| 专题 | 过程工程研究所_生化工程国家重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, State Key Lab Microbial Resources, Inst Microbiol, Beijing 100190, Peoples R China 2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wu, Xiao-Bin,Tian, Xiu-Yun,Ji, Jun-Jie,et al. Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity[J]. BIOTECHNOLOGY LETTERS,2011,33(4):805-812. |
| APA | Wu, Xiao-Bin,Tian, Xiu-Yun,Ji, Jun-Jie,Wu, Wei-Bin,Fan, Ke-Qiang,&Yang, Ke-Qian.(2011).Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity.BIOTECHNOLOGY LETTERS,33(4),805-812. |
| MLA | Wu, Xiao-Bin,et al."Saturation mutagenesis of Acremonium chrysogenum deacetoxy/deacetylcephalosporin C synthase R308 site confirms its role in controlling substrate specificity".BIOTECHNOLOGY LETTERS 33.4(2011):805-812. |
入库方式： OAI收割
来源：过程工程研究所
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