A highly Conserved Aspartic Acid Residue of the Chitosanase from Bacillus Sp TS Is Involved in the Substrate Binding

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	A highly Conserved Aspartic Acid Residue of the Chitosanase from Bacillus Sp TS Is Involved in the Substrate Binding
	Zhou, Zhanping 1,2; Zhao, Shuangzhi 3; Liu, Yang 1,2; Chang, Zhengying 1,2; Ma, Yanhe 1,2; Li, Jian 4; Song, Jiangning 1,2,5,6
刊名	APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
	2016-11-01
卷号	180 期号:6 页码:1167-1179
关键词	Chitosanase Glycoside hydrolase family 8 Aspartic acid Enzyme-substrate interaction
英文摘要	The chitosanase from Bacillus sp. TS (CsnTS) is an enzyme belonging to the glycoside hydrolase family 8. The sequence of CsnTS shares 98 % identity with the chitosanase from Bacillus sp. K17. Crystallography analysis and site-direct mutagenesis of the chitosanase from Bacillus sp. K17 identified the important residues involved in the catalytic interaction and substrate binding. However, despite progress in understanding the catalytic mechanism of the chitosanase from the family GH8, the functional roles of some residues that are highly conserved throughout this family have not been fully elucidated. This study focused on one of these residues, i.e., the aspartic acid residue at position 318. We found that apart from asparagine, mutation of Asp318 resulted in significant loss of enzyme activity. In-depth investigations showed that mutation of this residue not only impaired enzymatic activity but also affected substrate binding. Taken together, our results showed that Asp318 plays an important role in CsnTS activity.
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
类目[WOS]	Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
研究领域[WOS]	Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
关键词[WOS]	STREPTOMYCES SP N174 ; ANTIFUNGAL CHITOSANASE ; CRYSTAL-STRUCTURE ; MECHANISM ; GENE ; PURIFICATION ; CHITOOLIGOSACCHARIDES ; IDENTIFICATION ; SPECIFICITY ; EXPRESSION
收录类别	SCI
语种	英语
WOS记录号	WOS:000387544700010
内容类型	期刊论文
源URL	[http://124.16.173.210/handle/834782/2301]
专题	天津工业生物技术研究所_结构生物信息学和整合系统生物学实验室宋江宁_期刊论文
作者单位	1.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Natl Engn Lab Ind Enzymes, Tianjin 300308, Peoples R China 2.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Key Lab Syst Microbial Biotechnol, Tianjin 300308, Peoples R China 3.Shandong Acad Agr Sci, Inst Agrofood Sci & Technol, Jinan, Peoples R China 4.Monash Univ, Drug Delivery Disposit & Dynam, Monash Inst Pharmaceut Sci, Parkville, Vic 3052, Australia 5.Monash Univ, Dept Biochem & Mol Biol, Melbourne, Vic 3800, Australia 6.Monash Univ, Fac Informat Technol, Monash Ctr Data Sci, Melbourne, Vic 3800, Australia
推荐引用方式 GB/T 7714	Zhou, Zhanping,Zhao, Shuangzhi,Liu, Yang,et al. A highly Conserved Aspartic Acid Residue of the Chitosanase from Bacillus Sp TS Is Involved in the Substrate Binding[J]. APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY,2016,180(6):1167-1179.
APA	Zhou, Zhanping.,Zhao, Shuangzhi.,Liu, Yang.,Chang, Zhengying.,Ma, Yanhe.,...&Song, Jiangning.(2016).A highly Conserved Aspartic Acid Residue of the Chitosanase from Bacillus Sp TS Is Involved in the Substrate Binding.APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY,180(6),1167-1179.
MLA	Zhou, Zhanping,et al."A highly Conserved Aspartic Acid Residue of the Chitosanase from Bacillus Sp TS Is Involved in the Substrate Binding".APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY 180.6(2016):1167-1179.