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Structural Insights into the Dual-Substrate Recognition and Catalytic Mechanisms of a Bifunctional Acetyl Ester-Xyloside Hydrolase from Caldicellulosiruptor lactoaceticus

文献类型：期刊论文

作者Cao, Hao1; Sun, Lichao1; Huang, Ying1; Liu, Xin1,2; Yang, Dong3; Liu, Tengfei4; Jia, Xiaojing5,6; Wen, Boting1; Gu, Tianyi1; Wang, Fengzhong1
刊名ACS CATALYSIS
出版日期2019-03-01
卷号9期号:3页码:1739-1747
关键词bifunctional hydrolase acetyl esterase beta-1,4-xylanase dual-substrate catalytic mechanisms
ISSN号2155-5435
DOI10.1021/acscatal.8b03383
英文摘要Enzymes are usually characterized by their evolutionarily conserved catalytic domains; however, this work presents the incidental gain-of-function of an enzyme in a loop region by natural evolution of its amino acids. A bifunctional acetyl ester-xyloside hydrolase (CLH10) was heterologously expressed, purified, and characterized. The primary sequence of CLH10 contains the fragments of the conserved sequence of esterase and glycosidase, which distribute in a mixed type. The crystal structure revealed that the primary sequence folded into two independent structural regions to undertake both acetyl esterase and beta-1,4-xylanase hydrolase functions. CLH10 is capable of cleaving both the beta-1,4-xylosidic bond-linked main chain and the ester bond-linked acetylated side chain of xylan, which renders it valuable because it can degrade acetylated xylan within one enzyme. Significantly, the beta-1,4-xylanase activity of CLH10 appears to have been fortuitously obtained because of the variable Asp10 and Glu139 located in its loop region, which suggested that the exposed loop region might act as a potential hot-spot for the design and generation of promising enzyme function in both directed evolution and rational protein design.
WOS关键词XYLAN ESTERASE ; CONSERVATION ; SOFTWARE ; FAMILIES ; CLONING ; ENZYME ; ACID
资助项目National Key Research and Development Plan "modern food processing and food storage and transportation technology and equipment"[2017YFD0400204] ; China Postdoctoral Science Foundation[2018M630230] ; National Natural Science Foundation of China[31801475] ; National Natural Science Foundation of China[31700701]
WOS研究方向Chemistry
语种英语
WOS记录号WOS:000460600600016
出版者AMER CHEMICAL SOC
资助机构National Key Research and Development Plan "modern food processing and food storage and transportation technology and equipment" ; China Postdoctoral Science Foundation ; National Natural Science Foundation of China
源URL[http://ir.ipe.ac.cn/handle/122111/28322]  
专题中国科学院过程工程研究所
通讯作者Wang, Fengzhong; Xin, Fengjiao
作者单位1.Chinese Acad Agr Sci, Inst Food Sci & Technol, Lab Biomfg & Food Engn, Beijing 100193, Peoples R China
2.Univ Sci & Technol China, Sch Life Sci, Hefei Natl Lab Phys Sci Microscale, Hefei 230027, Anhui, Peoples R China
3.China Agr Univ, Coll Food Sci & Nutr Engn, Beijing 100083, Peoples R China
4.Beijing Univ Chinese Med, Sch Chinese Materia Med, Beijing 100102, Peoples R China
5.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
6.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
推荐引用方式
GB/T 7714		 Cao, Hao,Sun, Lichao,Huang, Ying,et al. Structural Insights into the Dual-Substrate Recognition and Catalytic Mechanisms of a Bifunctional Acetyl Ester-Xyloside Hydrolase from Caldicellulosiruptor lactoaceticus[J]. ACS CATALYSIS,2019,9(3):1739-1747.
APA Cao, Hao.,Sun, Lichao.,Huang, Ying.,Liu, Xin.,Yang, Dong.,...&Xin, Fengjiao.(2019).Structural Insights into the Dual-Substrate Recognition and Catalytic Mechanisms of a Bifunctional Acetyl Ester-Xyloside Hydrolase from Caldicellulosiruptor lactoaceticus.ACS CATALYSIS,9(3),1739-1747.
MLA Cao, Hao,et al."Structural Insights into the Dual-Substrate Recognition and Catalytic Mechanisms of a Bifunctional Acetyl Ester-Xyloside Hydrolase from Caldicellulosiruptor lactoaceticus".ACS CATALYSIS 9.3(2019):1739-1747.

入库方式： OAI收割

来源：过程工程研究所

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