An anchoring residue adjacent to the substrate access tunnel entrance of a nitrile hydratase directs its catalytic activity towards 3-cyanopyridine

被引：5

作者：

Cheng, Zhongyi ^{[1
]}

Zhang, Weimiao ^{[1
]}

Xia, Yuanyuan ^{[1
]}

Ma, Dong ^{[1
]}

Zhou, Zhemin ^{[1
,2
]}

机构：

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

[2] Jiangnan Univ Rugao Food Biotechnol Res Inst, Rugao 226500, Jiangsu, Peoples R China

来源：

CATALYSIS SCIENCE & TECHNOLOGY | 2021年 / 11卷 / 23期

基金：

中国国家自然科学基金; 中国博士后科学基金;

关键词：

MECHANISM;

D O I：

10.1039/d1cy01566d

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 Glu50 residue located adjacent to the substrate access tunnel entrance of the nitrile hydratase from Pseudonocardia thermophila JCM3095 acts as an anchoring residue. Breaking the salt bridge between the beta 50 residue and its surrounding residues can increase the flexibility of the tunnel entrance structure and make it conducive to substrate migration.

引用

页码：7525 / 7529

页数：5

共 4 条

[1] Tailoring the Hinge Residue at the Substrate Access Tunnel Entrance Improves the Catalytic Performance of Industrialized Nitrile Hydratase Toward 3-Cyanopyridine
Xia, Yuanyuan
Yin, Meng
Peplowski, Lukasz
Cheng, Zhongyi
Zhou, Zhemin
CHEMISTRYSELECT, 2022, 7 (34):
[2] Substrate access tunnel engineering for improving the catalytic activity of a thermophilic nitrile hydratase toward pyridine and pyrazine nitriles
Cheng, Zhongyi
Jiang, Shijin
Zhou, Zhemin
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2021, 575 : 8 - 13
[3] Substrate access tunnel engineering of a Fe-type nitrile hydratase from Pseudomonas fluorescens ZJUT001 for substrate preference adjustment and catalytic performance enhancement
Li, Shu-Fang
Gao, Yan-Chi
Xu, Hao-Bo
Xu, Cheng-Long
Wang, Ya-Jun
Liu, Zhi-Qiang
Zheng, Yu-Guo
BIOORGANIC CHEMISTRY, 2024, 152
[4] Role of a Mutated Residue at the Entrance of the Substrate Access Channel in Cytochrome P450 Engineered for Vitamin D3 Hydroxylation Activity
Fukunishi, Hiroaki
Yagi, Hirotaka
Kamijo, Ken'ichi
Shimada, Jiro
BIOCHEMISTRY, 2011, 50 (39) : 8302 - 8310

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