Molecular recognition in the product site of cellobiohydrolase Cel7A regulates processive step length
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چکیده
منابع مشابه
Processive action of cellobiohydrolase Cel7A from Trichoderma reesei is revealed as 'burst' kinetics on fluorescent polymeric model substrates.
Reaction conditions for the reducing-end-specific derivatization of cellulose substrates with the fluorogenic compound, anthranilic acid, have been established. Hydrolysis of fluorescence-labelled celluloses by cellobiohydrolase Cel7A from Trichoderma reesei was consistent with the active-site titration kinetics (burst kinetics), which allowed the quantification of the processivity of the enzym...
متن کاملKinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity.
Cellobiohydrolases are exo-active glycosyl hydrolases that processively convert cellulose to soluble sugars, typically cellobiose. They effectively break down crystalline cellulose and make up a major component in industrial enzyme mixtures used for deconstruction of lignocellulosic biomass. Identification of the rate-limiting step for cellobiohydrolases remains controversial, and recent report...
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Building on our previous efforts to generate thermostable chimeric fungal cellobiohydrolase I (CBH I, also known as Cel7A) cellulases by structure-guided recombination, we used FoldX and a 'consensus' sequence approach to identify individual mutations present in the five homologous parent CBH I enzymes which further stabilize the chimeras. Using the FoldX force field, we calculated the effect o...
متن کاملMolecular simulation evidence for processive motion of Trichoderma reesei Cel7A during cellulose depolymerization
0009-2614/$ see front matter 2008 Elsevier B.V. A doi:10.1016/j.cplett.2008.05.060 * Corresponding author. Fax: +1 615 343 7951. E-mail address: [email protected] (C. McCa We present free energy calculations for the Trichoderma reesei Cel7A (cellobiohydrolase I) linker peptide from molecular dynamics simulations directed towards understanding the linker role in cellulose hydrolysis. The c...
متن کاملBinding site dynamics and aromatic-carbohydrate interactions in processive and non-processive family 7 glycoside hydrolases.
In nature, processive and non-processive cellulase enzymes deconstruct cellulose to soluble sugars. From structural studies, the consensus is that processive cellulases exhibit tunnels lined with aromatic and polar residues, whereas non-processive cellulases exhibit open clefts with fewer ligand contacts. To gain additional insight into the differences between processive and non-processive cell...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2020
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bcj20190770