Effect and mechanism analysis of different linkers on efficient catalysis of subunit-fused nitrile hydratase-Reference-Cited by-同舟云学术

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Effect and mechanism analysis of different linkers on efficient catalysis of subunit-fused nitrile hydratase

Published:2021-06 Issue: Volume:181 Page:444-451
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Guo Junling,Cheng Zhongyi,Berdychowska Julia,Zhu Xiaonan,Wang Lingling,Peplowski Lukasz,Zhou Zhemin

Funder

China Postdoctoral Science Foundation

Priority Academic Program Development of Jiangsu Higher Education Institutions

National Natural Science Foundation of China

Major Basic Research Project of the Natural Science Foundation of the Jiangsu Higher Education Institutions

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference52 articles.

1. Design of the linkers which effectively separate domains of a bifunctional fusion protein;Arai;Protein Eng.,2001

2. Effect of linker length and flexibility on the Clostridium thermocellum esterase displayed on Bacillus subtilis spores;Chen;Appl. Biochem. Biotechnol.,2017

3. Insertion of the designed helical linker led to increased expression of Tf-based fusion proteins, pharm;Amet;Res,2008

4. A flexible protein linker improves the function of epitope-tagged proteins in Saccharomyces cerevisiae;Sabourin;Yeast (Chichester, England),2007

5. Immunoabsorbent nanoparticles based on a tobamovirus displaying protein A;Werner;Proc. Natl. Acad. Sci. U. S. A.,2006

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2. Recent progress of activator of an industrially important enzyme–Nitrile hydratase;Molecular Catalysis;2024-07

3. An eco-friendly process for low-degree polymerization xylo-oligosaccharides production from corncob via enzyme adsorption-hydrolysis integrated approach by reconstructing fusion protein;Journal of Cleaner Production;2024-02

4. Highly efficient biosynthesis of isonicotinamide through a substrate access tunnel engineered nitrile hydratase from Carbonactinospora thermoautotrophicus;New Journal of Chemistry;2023

5. Modification of nitrile hydratase from Rhodococcus erythropolis CCM2595 by semirational design to enhance its substrate affinity;Biointerphases;2022-11

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