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https://hdl.handle.net/2440/138637
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Type: | Journal article |
Title: | Molecular mechanisms of processive glycoside hydrolases underline catalytic pragmatism |
Author: | Hrmova, M. Schwerdt, J.G. |
Citation: | Biochemical Society Transactions, 2023; 51(3):1387-1403 |
Publisher: | Portland Press |
Issue Date: | 2023 |
ISSN: | 0300-5127 1470-8752 |
Statement of Responsibility: | Maria Hrmova and Julian G. Schwerdt |
Abstract: | Processive and distributive catalysis defines the conversion continuum, thus underpinning the transformation of oligo- and polymeric substrates by enzymes. Distributive catalysis follows an association–transformation–dissociation pattern during the formation of enzyme–reactant complexes, whereas during processive catalysis, enzymes partner with substrates and complete multiple catalytic events before dissociation from an enzyme–substrate complex. Here, we focus on processive catalysis in glycoside hydrolases (GHs), which ensures efficient conversions of substrates with high precision, and has the advantage over distributive catalysis in efficiency. The work presented here examines a recent discovery of substrate-product-assisted processive catalysis in the GH3 family enzymes with enclosed pocket-shaped active sites. We detail how GH3 β-D-glucan glucohydrolases exploit a transiently formed lateral pocket for product displacement and reactants sliding (or translocation motion) through the catalytic site without dissociation, including movements during nanoscale binding/unbinding and sliding. The phylogenetic tree of putative 550 Archaean, bacterial, fungal, Viridiplantae, and Metazoan GH3 entries resolved seven lineages that corresponded to major substrate specificity groups. This analysis indicates that two tryptophan residues in plant β-D-glucan glucohydrolases that delineate the catalytic pocket, and infer broad specificity, high catalytic efficiency, and substrate-product-assisted processivity, have evolved through a complex evolutionary process, including horizontal transfer and neo-functionalisation. We conclude that the definition of thermodynamic and mechano-structural properties of processive enzymes is fundamentally important for theoretical and practical applications in bioengineering applicable in various biotechnologies. |
Keywords: | Animals Plants Glucans Glycoside Hydrolases Phylogeny Catalytic Domain Substrate Specificity Catalysis |
Description: | Version of Record published: 2 June 2023 |
Rights: | © 2023 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY). |
DOI: | 10.1042/bst20230136 |
Grant ID: | http://purl.org/au-research/grants/arc/DP120100900 |
Published version: | http://dx.doi.org/10.1042/bst20230136 |
Appears in Collections: | Agriculture, Food and Wine publications |
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hdl_138637.pdf | Published version | 3.24 MB | Adobe PDF | View/Open |
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