Predominant Nonproductive Substrate Binding by Fungal Cellobiohydrolase I and Implications for Activity Improvement
Author:
Affiliation:
1. Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences; 33, bld. 2 Leninsky Ave. Moscow 119071 Russia
2. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences; Moscow 119991 Russia
Funder
State project
Publisher
Wiley
Subject
Molecular Medicine,Applied Microbiology and Biotechnology,General Medicine
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/biot.201700712/fullpdf
Reference100 articles.
1. Cellulosic ethanol: status and innovation
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3. Fungal Cellulases
4. Kinetics of the hydrolysis of cellulose by β-1,4-glucan cellobiohydrolase of Trichoderma viride
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1. Study on microscopic physical and chemical properties of biomass materials by AFM;Journal of Materials Research and Technology;2023-05
2. Enzyme kinetics by GH7 cellobiohydrolases on chromogenic substrates is dictated by non‐productive binding: insights from crystal structures and MD simulation;The FEBS Journal;2022-09-06
3. The dissociation mechanism of processive cellulases;Proceedings of the National Academy of Sciences;2019-10-30
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