A switch in a substrate tunnel for directing regioselectivity of nitrile hydratases towards α,ω-dinitriles

被引：18

作者：

Cheng, Zhongyi ^{[1
]}

Cui, Wenjing ^{[1
]}

Liu, Zhongmei ^{[1
]}

Zhou, Li ^{[1
]}

Wang, Min ^{[2
]}

Kobayashi, Michihiko ^{[3
,4
]}

Zhou, Zhemin ^{[1
]}

机构：

[1] Jiangnan Univ, Sch Biotechnol, Key Lab Ind Biotechnol, Minist Educ, Wuxi 214122, Peoples R China

[2] Tianjin Univ Sci & Technol, Coll Biotechnol, 29 13th St TEDA, Tianjin 300457, Peoples R China

[3] Univ Tsukuba, Inst Appl Biochem, 1-1-1 Tennodai, Tsukuba, Ibaraki 3058572, Japan

[4] Univ Tsukuba, Grad Sch Life & Environm Sci, 1-1-1 Tennodai, Tsukuba, Ibaraki 3058572, Japan

来源：

CATALYSIS SCIENCE & TECHNOLOGY | 2016年 / 6卷 / 05期

基金：

国家高技术研究发展计划(863计划); 中国国家自然科学基金;

关键词：

CRYSTAL-STRUCTURE; RESTING CELLS; 5-CYANOVALERAMIDE; REVEALS; AMIDASE; AJ270;

D O I：

10.1039/c5cy01997d

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：

The beta 37 residue of nitrile hydratase (NHase) from Pseudomonas putida and NHase from Comamonas testosteroni played a critical role in directing enzyme regioselectivity. Amino acid substitution in this site modulated or even inverted enzyme regioselectivity towards aliphatic alpha,omega-dinitriles.

引用

页码：1292 / 1296

页数：5

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