中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
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
DOI10.1016/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。