中国科学院大连化学物理研究所机构知识库
Advanced  
DICP OpenIR  > 中国科学院大连化学物理研究所  > 期刊论文
题名: Fully Deacetylated Chitooligosaccharides Act as Efficient Glycoside Hydrolase Family 18 Chitinase Inhibitors.
作者: Chen, Lei1;  Zhou, Yong2;  Qu, Mingbo1;  Zhao, Yong3;  Yang, Qing1
刊名: JOURNAL OF BIOLOGICAL CHEMISTRY
发表日期: 2014-06-20
DOI: 10.1074/jbc.M114.564534
卷: 289, 期:25, 页:17932-17940
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine
类目[WOS]: Biochemistry & Molecular Biology
研究领域[WOS]: Biochemistry & Molecular Biology
英文摘要: Small molecule inhibitors against chitinases have potential applications as pesticides, fungicides, and antiasthmatics. Here, we report that a series of fully deacetylated chitooligosaccharides (GlcN)(2-7) can act as inhibitors against the insect chitinase OfChtI, the human chitinase HsCht, and the bacterial chitinases SmChiA and SmChiB with IC50 values at micromolar to millimolar levels. The injection of mixed (GlcN)(2-7) into the fifth instar larvae of the insect Ostrinia furnacalis resulted in 85% of the larvae being arrested at the larval stage and death after 10 days, also suggesting that (GlcN)(2-7) might inhibit OfChtI in vivo. Crystal structures of the catalytic domain of OfChtI (OfChtI-CAD) complexed with (GlcN)(5,6) were obtained at resolutions of 2.0 angstrom. These structures, together with mutagenesis and thermodynamic analysis, suggested that the inhibition was strongly related to the interaction between the -1 GlcN residue of the inhibitor and the catalytic Glu(148) of the enzyme. Structure-based comparison showed that the fully deacetylated chitooligosaccharides mimic the substrate chitooligosaccharides by binding to the active cleft. This work first reports the inhibitory activity and proposed inhibitory mechanism of fully deacetylated chitooligosaccharides. Because the fully deacetylated chitooligosaccharides can be easily derived from chitin, one of the most abundant materials in nature, this work also provides a platform for developing eco-friendly inhibitors against chitinases.
关键词[WOS]: SERRATIA-MARCESCENS 2170 ;  GLIOCLADIUM SP FTD-0668 ;  BACTERIAL CHITINASES ;  ALLOSAMIDIN ;  PRODUCT ;  COMPLEX ;  MECHANISM ;  ARGIFIN ;  BINDING ;  CLONING
语种: 英语
WOS记录号: WOS:000338018100053
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/145732
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

Files in This Item:

There are no files associated with this item.


作者单位: 1.Dalian Univ Technol, Sch Life Sci & Biotechnol, Dalian 116024, Liaoning, Peoples R China
2.Dalian Univ Technol, Sch Software, Dalian 116620, Peoples R China
3.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian 116023, Peoples R China

Recommended Citation:
Chen, Lei,Zhou, Yong,Qu, Mingbo,et al. Fully Deacetylated Chitooligosaccharides Act as Efficient Glycoside Hydrolase Family 18 Chitinase Inhibitors.[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2014,289(25):17932-17940.
Service
 Recommend this item
 Sava as my favorate item
 Show this item's statistics
 Export Endnote File
Google Scholar
 Similar articles in Google Scholar
 [Chen, Lei]'s Articles
 [Zhou, Yong]'s Articles
 [Qu, Mingbo]'s Articles
CSDL cross search
 Similar articles in CSDL Cross Search
 [Chen, Lei]‘s Articles
 [Zhou, Yong]‘s Articles
 [Qu, Mingbo]‘s Articles
Related Copyright Policies
Null
Social Bookmarking
  Add to CiteULike  Add to Connotea  Add to Del.icio.us  Add to Digg  Add to Reddit 
所有评论 (0)
暂无评论
 
评注功能仅针对注册用户开放,请您登录
您对该条目有什么异议,请填写以下表单,管理员会尽快联系您。
内 容:
Email:  *
单位:
验证码:   刷新
您在IR的使用过程中有什么好的想法或者建议可以反馈给我们。
标 题:
 *
内 容:
Email:  *
验证码:   刷新

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

 

 

Valid XHTML 1.0!
Powered by CSpace