C-terminus mutations of acremonium chrysogenum deacetoxy/deacetylcephalosporin c synthase with improved activity toward penicillin analogs
文献类型:期刊论文
作者 | Wu, XB; Fan, KQ; Wang, QH; Yang, KQ |
刊名 | Fems microbiology letters
![]() |
出版日期 | 2005-05-01 |
卷号 | 246期号:1页码:103-110 |
关键词 | Daoc Dac Deacetoxy/deacetylcephalosporin c synthase C-terminus Mutagenesis Acremonium chrysogenum Kinetics |
ISSN号 | 0378-1097 |
DOI | 10.1016/j.femsle.2005.03.043 |
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 (daoc) and the hydroxylation of the latter to deacetylcephalosporin c (dac). three residues n305, 8307 and 8308 located in close proximity to the c-terminus of acdaoc/dacs were each mutated to leucine. the n305l and r308l mutant acdaoc/dacss showed significant improvement in their ability to convert penicillin analogs. 8308 was identified for the first time as a critical residue for daoc/dacs activity. kinetic analyses of purified r308l enzyme indicated its improved catalytic efficiency is due to combined improvements of k-m and k(cat). comparative modeling of acdaoc/dacs supports the involvement of 8308 in the formation of substrate-binding pocket. (c) 2005 federation of european microbiological societies. published by elsevier b.v. all rights reserved. |
WOS关键词 | STREPTOMYCES-CLAVULIGERUS ; SUBSTRATE ; ENZYME ; CONVERSION ; ACID ; HYDROXYLASE ; CATALYSIS ; BINDING ; DAOCS ; SITE |
WOS研究方向 | Microbiology |
WOS类目 | Microbiology |
语种 | 英语 |
WOS记录号 | WOS:000229231400014 |
出版者 | ELSEVIER SCIENCE BV |
URI标识 | http://www.irgrid.ac.cn/handle/1471x/2378149 |
专题 | 中国科学院大学 |
通讯作者 | Yang, KQ |
作者单位 | 1.Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Resources, Beijing 100080, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100080, Peoples R China |
推荐引用方式 GB/T 7714 | Wu, XB,Fan, KQ,Wang, QH,et al. C-terminus mutations of acremonium chrysogenum deacetoxy/deacetylcephalosporin c synthase with improved activity toward penicillin analogs[J]. Fems microbiology letters,2005,246(1):103-110. |
APA | Wu, XB,Fan, KQ,Wang, QH,&Yang, KQ.(2005).C-terminus mutations of acremonium chrysogenum deacetoxy/deacetylcephalosporin c synthase with improved activity toward penicillin analogs.Fems microbiology letters,246(1),103-110. |
MLA | Wu, XB,et al."C-terminus mutations of acremonium chrysogenum deacetoxy/deacetylcephalosporin c synthase with improved activity toward penicillin analogs".Fems microbiology letters 246.1(2005):103-110. |
入库方式: iSwitch采集
来源:中国科学院大学
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。