Engineering of D-fructose-6-phosphate aldolase A for improved activity towards cinnamaldehyde

被引：7
作者：
Yang, Xiaohong [1 ]
Ye, Lidan [1 ]
Li, Aipeng [1 ]
Yang, Chengcheng [1 ]
Yu, Huilei [2 ]
Gu, Jiali [3 ]
Guo, Fei [1 ]
Jiang, Ling [1 ,4 ]
Wang, Fan [1 ]
Yu, Hongwei [1 ]
机构：
[1] Zhejiang Univ, Coll Chem & Biol Engn, Inst Bioengn, Hangzhou 310027, Zhejiang, Peoples R China
[2] East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai, Peoples R China
[3] Huzhou Univ, Coll Life Sci, Dept Chem Mat, Huzhou 313000, Peoples R China
[4] Zhejiang Univ Technol, Collaborat Innovat Ctr Yangtze River Delta Green, Hangzhou 310014, Zhejiang, Peoples R China
来源：
CATALYSIS SCIENCE & TECHNOLOGY | 2017年 / 7卷 / 02期
关键词：
ESCHERICHIA-COLI; FRUCTOSE-6-PHOSPHATE ALDOLASE; CRYSTAL-STRUCTURE; F6P ALDOLASE; TRANSALDOLASE; GLYCOLALDEHYDE; INTERMEDIATE; INHIBITORS; SUBSTRATE; COMPLEX;
D O I：
10.1039/c6cy01622g
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
D-Fructose-6-phosphate aldolase A (FSAA) from Escherichia coli was engineered for enhanced catalytic efficiency towards cinnamaldehyde. The result implies that the site 59 residue possibly affects the activity of FSAA towards cinnamaldehyde through a residue interaction network rather than binding to the catalytic water as generally regarded.
引用
收藏
页码：382 / 386
页数：5
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