Characterization of a Haloarchaeal GH Family 18 Chitinase with Additional Acidic Amino Acids on Its Protein Surface

Y. Zhang, R. An, R. Yatsunami, M. Sato, K. Orishimo, Y. Hatori, T. Fukui, Satoshi Nakamura
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引用次数: 2

Abstract

A chitinase (ChiN1) from Halobacterium salinarum NRC-1 belongs to the glycoside hydrolase family 18. According to the three-dimensional structure model of ChiN1, Asn239 and Gln242 on a small helix between Phe237 and Arg247 were targeted for mutagenesis. Mutants N239D (Asn239 was replaced by Asp) and Q242E (Gln242 was replaced by Glu) were expressed in Haloarcula japonica and then characterized. Characterization of the mutants revealed that halotolerancy could be improved by introducing an acidic amino acid on the surface of ChiN1.
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盐古菌GH家族18几丁质酶蛋白表面附加酸性氨基酸的特性研究
来自盐盐杆菌NRC-1的几丁质酶(ChiN1)属于糖苷水解酶家族18。根据ChiN1的三维结构模型,在Phe237和Arg247之间的一个小螺旋上的Asn239和Gln242被靶向诱变。突变体N239D (Asn239被Asp取代)和Q242E (Gln242被Glu取代)在Haloarcula japonica中表达并被鉴定。突变体的特性表明,在ChiN1表面引入酸性氨基酸可以提高其耐盐性。
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