DICP OpenIR
Environment-induced conformational and functional changes of L-2-haloacid dehalogenase
Wang, Yayue1,2; Cao, Xupeng1; Feng, Yanbin1; Xue, Song1
KeywordL-2-haloacid Dehalogenase Circular Dichroism Environmental Effects Conformation
Source PublicationJOURNAL OF BIOSCIENCE AND BIOENGINEERING
2016-05-01
ISSN1389-1723
DOI10.1016/j.jbiosc.2015.09.008
Volume121Issue:5Pages:491-496
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS SubjectBiotechnology & Applied Microbiology ; Food Science & Technology
WOS Research AreaBiotechnology & Applied Microbiology ; Food Science & Technology
WOS KeywordBACTERIAL 2-HALOACID DEHALOGENASES ; XANTHOBACTER-AUTOTROPHICUS GJ10 ; SPONGE HYMENIACIDON-PERLEVIS ; BURKHOLDERIA-CEPACIA MBA4 ; PSEUDOMONAS SP. YL ; HALOACID DEHALOGENASE ; CIRCULAR-DICHROISM ; ACID DEHALOGENASE ; CRYSTAL-STRUCTURE ; THERMAL-DENATURATION
Abstract2-Haloacid dehalogenases have been highly studied due to their potential applications in chemical industries and bioremediation. Although biochemical and structural characterizations of the enzyme have been detailed, no information was available regarding environmental effects on the structure function relationship. Here, circular dichroism spectroscopy (CD) was used to investigate the correlation between changes on the conformation and the function of L-2-haloacid dehalogenase (HadL AJ1) from the Pseudomonas putida induced by the environmental factors. Decreased alpha-helix and increased beta-sheet contents were observed in the structure of HadL AJ1 along with activity losses caused by pH, temperature and inhibitors. Regardless of which factor above-mentioned existed, more than 65.0% of HadL AJ1 activity could be remained if its alpha-helix content was over 12.0%. The maintenance of alpha-helical structure in HadL All was indispensable to its catalysis, while beta-sheet increase restricts its activity. This study revealed the variation of enzymatic activity due to environmental conditions resulting in structural changes monitored by CD, which contributed to rational modification and was instructive for predicting changes of the enzymatic activity during application. (C) 2015, The Society for Biotechnology, Japan. All rights reserved.
Language英语
WOS IDWOS:000376695300003
PublisherSOC BIOSCIENCE BIOENGINEERING JAPAN
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/170993
Collection中国科学院大连化学物理研究所
Corresponding AuthorXue, Song
Affiliation1.Chinese Acad Sci, Dalian Inst Chem Phys, Marine Bioengn Grp, Dalian 116023, Peoples R China
2.Univ Chinese Acad Sci, Sch Chem & Chem Engn, Beijing 100049, Peoples R China
Recommended Citation
GB/T 7714
Wang, Yayue,Cao, Xupeng,Feng, Yanbin,et al. Environment-induced conformational and functional changes of L-2-haloacid dehalogenase[J]. JOURNAL OF BIOSCIENCE AND BIOENGINEERING,2016,121(5):491-496.
APA Wang, Yayue,Cao, Xupeng,Feng, Yanbin,&Xue, Song.(2016).Environment-induced conformational and functional changes of L-2-haloacid dehalogenase.JOURNAL OF BIOSCIENCE AND BIOENGINEERING,121(5),491-496.
MLA Wang, Yayue,et al."Environment-induced conformational and functional changes of L-2-haloacid dehalogenase".JOURNAL OF BIOSCIENCE AND BIOENGINEERING 121.5(2016):491-496.
Files in This Item:
There are no files associated with this item.
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Wang, Yayue]'s Articles
[Cao, Xupeng]'s Articles
[Feng, Yanbin]'s Articles
Baidu academic
Similar articles in Baidu academic
[Wang, Yayue]'s Articles
[Cao, Xupeng]'s Articles
[Feng, Yanbin]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Wang, Yayue]'s Articles
[Cao, Xupeng]'s Articles
[Feng, Yanbin]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.