Transient Kinetics and Rate-Limiting Steps for the Processive Cellobiohydrolase Cel7A: Effects of Substrate Structure and Carbohydrate Binding Domain-Reference-Cited by-同舟云学术

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Transient Kinetics and Rate-Limiting Steps for the Processive Cellobiohydrolase Cel7A: Effects of Substrate Structure and Carbohydrate Binding Domain

Published:2013-11-20 Issue:49 Volume:52 Page:8938-8948
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Cruys-Bagger Nicolaj¹,Tatsumi Hirosuke²,Ren Guilin Robin¹,Borch Kim³,Westh Peter¹

Affiliation:

1. Research Unit for Functional Biomaterials, NSM, Roskilde University, Universitetsvej 1, DK-4000 Roskilde, Denmark

2. Department of Chemistry, Faculty of Science, Shinshu University, Matsumoto, Nagano 390-8621, Japan

3. Novozymes A/S, Krogshøjvej 36, DK-2880 Bagsværd, Denmark

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi401210n

Reference48 articles.

1. Mechanisms of glycosyl transferases and hydrolases

2. Crystalline cellulose degradation: new insight into the function of cellobiohydrolases

3. Computational Investigation of Glycosylation Effects on a Family 1 Carbohydrate-binding Module

4. An amperometric enzyme biosensor for real-time measurements of cellobiohydrolase activity on insoluble cellulose

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1. Interrelationship of Substrate Crystallinity, Enzyme Binding Strength, and Cellulase Activity;2024-08-20

2. CANDy: Automated analysis of domain architectures in carbohydrate-active enzymes;PLOS ONE;2024-07-11

3. Unveiling the Inhibition of Enzymatic Hydrolysis of Cellulose by Lignin-Derived Phenolics: Interfacial Kinetics and Molecular Simulations;ACS Sustainable Chemistry & Engineering;2024-06-19

4. Engineering of glycoside hydrolase family 7 cellobiohydrolases directed by natural diversity screening;Journal of Biological Chemistry;2024-03

5. Impact of Synergy Partner Cel7B on Cel7A Binding Rates: Insights from Single-Molecule Data;The Journal of Physical Chemistry B;2024-01-16

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