Essential Role of Gly33 in a Novel Organic Solvent-Tolerant Lipase from Serratia marcescens ECU1010 as Determined by Site-Directed Mutagenesis

被引：7

作者：

Li, Su-Xia ^{[1
]}

Ma, Qiang ^{[1
]}

Lin, Kang ^{[1
]}

Wu, Jiao-Jiao ^{[1
]}

Wu, Yi-Xin ^{[2
]}

Xu, Jian-He ^{[1
]}

机构：

[1] E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

[2] Hamamatsu Univ Sch Med, Dept Biochem, Hamamatsu, Shizuoka 4313192, Japan

来源：

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY | 2014年 / 172卷 / 06期

关键词：

Lipase; Site-directed mutagenesis; Organic solvent stability; Molecular modeling; Serratia marcescens ECU1010; FAMILY I.3 LIPASE; EXTRACELLULAR LIPASE; ENZYME ACTIVATION; ESCHERICHIA-COLI; ACID-RESIDUES; PURIFICATION; HYDROLYSIS;

D O I：

10.1007/s12010-013-0690-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A novel lipase lipB from Serratia marcescens ECU1010 is highly stable in the presence of organic solvents. By sequence and structure comparison with homologous lipase lipA, three amino acid residues were found to be different between them. To identify the residues which increase the organic solvent stability of lipB, residues that potentially provide this stability were mutated to the ones of lipA at equivalent positions. The replacement of Gly at position 33 by Asp obviously decreased its stability in organic solvents. Molecular modeling and structural analysis also suggested that the Gly33 residue is important for the organic solvent stability of lipB.

引用

页码：2945 / 2954

页数：10

共 5 条

[1] Essential Role of Gly33 in a Novel Organic Solvent-Tolerant Lipase from Serratia marcescens ECU1010 as Determined by Site-Directed Mutagenesis
Su-Xia Li
Qiang Ma
Kang Lin
Jiao-Jiao Wu
Yi-Xin Wu
Jian-He Xu
Applied Biochemistry and Biotechnology, 2014, 172 : 2945 - 2954
[2] Refolding, purification and characterization of an organic solvent-tolerant lipase from Serratia marcescens ECU1010
Li, Suxia
Pang, Huaiyu
Lin, Kang
Xu, Jianhe
Zhao, Jian
Fan, Liqiang
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 2011, 71 (3-4) : 171 - 176
[3] Biochemical properties and potential applications of an organic solvent-tolerant lipase isolated from Serratia marcescens ECU1010
Zhao, Li-Li
Xu, Jian-He
Zhao, Jian
Pan, Jiang
Wang, Zhi-Long
PROCESS BIOCHEMISTRY, 2008, 43 (06) : 626 - 633
[4] Enhancing activity and thermostability of lipase A from Serratia marcescens by site-directed mutagenesis
Mohammadi, Mohsen
Sepehrizadeh, Zargham
Ebrahim-Habibi, Azadeh
Shahverdi, Ahmad Reza
Faramarzi, Mohammad Ali
Setayesh, Neda
ENZYME AND MICROBIAL TECHNOLOGY, 2016, 93-94 : 18 - 28
[5] ESSENTIAL CATALYTIC ROLE OF GLU-134 IN ENDO-BETA-1,3-1,4-D-GLUCAN 4-GLUCANOHYDROLASE FROM BACILLUS-LICHENIFORMIS AS DETERMINED BY SITE-DIRECTED MUTAGENESIS
PLANAS, A
JUNCOSA, M
LLOBERAS, J
QUEROL, E
FEBS LETTERS, 1992, 308 (02) : 141 - 145

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