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Title of Journal: Appl Biochem Biotechnol

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Abbravation: Applied Biochemistry and Biotechnology

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Springer US

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DOI

10.1007/bf02567370

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1559-0291

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A highly Conserved Aspartic Acid Residue of the Ch

Authors: Zhanping Zhou Shuangzhi Zhao Yang Liu Zhengying Chang Yanhe Ma Jian Li Jiangning Song
Publish Date: 2016/06/18
Volume: 180, Issue: 6, Pages: 1167-1179
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Abstract

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 sitedirect 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 ie the aspartic acid residue at position 318 We found that apart from asparagine mutation of Asp318 resulted in significant loss of enzyme activity Indepth 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 activityThis work was supported in part by grants from the Hundred Talents Program of the Chinese Academy of Sciences CAS the Knowledge Innovation Program of CAS KSCX2EWG8 and the Tianjin Municipal Science and Technology Commission 10ZCKFSY05600 JL is an Australian National Health and Medical Council NHMRC Senior Research Fellow JS is a recipient of the Hundred Talents Program of CAS

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