Coevolutionary analysis reveals a distal amino acid residue pair affecting the catalytic activity of GH5 processive endoglucanase from <i>Bacillus subtilis</i> BS‐5-Reference-Cited by-同舟云学术

Coevolutionary analysis reveals a distal amino acid residue pair affecting the catalytic activity of GH5 processive endoglucanase from Bacillus subtilis BS‐5

Published:2022-05-05 Issue:8 Volume:119 Page:2105-2114
ISSN:0006-3592
Container-title:Biotechnology and Bioengineering
language:en
Short-container-title:Biotech & Bioengineering

Author:

Wu Mujunqi¹,Lv Kemin¹,Li Jiahuang²,Wu Bin¹^ORCID,He Bingfang³

Affiliation:

1. College of Biotechnology and Pharmaceutical Engineering Nanjing Tech University Nanjing Jiangsu China

2. School of Biopharmacy China Pharmaceutical University Nanjing Jiangsu China

3. School of Pharmaceutical Sciences Nanjing Tech University Nanjing Jiangsu China

Funder

National Natural Science Foundation of China

Publisher

Wiley

Subject

Applied Microbiology and Biotechnology,Bioengineering,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/bit.28113

Reference44 articles.

1. Origins of coevolution between residues distant in protein 3D structures

2. MolADI: A Web Server for Automatic Analysis of Protein–Small Molecule Dynamic Interactions

3. Truncation of the processive Cel5A ofThermotoga maritimaresults in soluble expression and several fold increase in activity

4. Engineering the conserved and noncatalytic residues of a thermostable β-1,4-endoglucanase to improve specific activity and thermostability

5. Engineering Robust Cellulases for Tailored Lignocellulosic Degradation Cocktails

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