Glycoside hydrolases: Mechanisms, specificities, and engineering

Planas, Antoni

doi:10.1016/b978-0-323-91805-3.00011-3

Cited by 4 publications

(1 citation statement)

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“…Glycoside hydrolases (GHs) are an expressive group among the CAZymes (http://www.cazy.org/Glycoside-Hydrolases.html), and they catalyze the hydrolysis of glycosidic bonds between two or more carbohydrates or between a carbohydrate and a noncarbohydrate moiety. 19 They are classified in EC (Enzyme Commission) numbers based mainly on their substrate specificity and the chemical reaction they catalyze. 20 GHs can be further categorized as endo or exo-enzymes, depending on whether the polysaccharide attack occurs somewhere within the polymer main chain or in one of its termini (reducing or non-reducing end).…”

Section: Lignocellulosic Biomass Compositionmentioning

confidence: 99%

Biochemical and biophysical characterization of two glucuronoxylanases aiming the production of xylooligosaccharides

Vacilotto

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Section: Lignocellulosic Biomass Compositionmentioning

confidence: 99%

Biochemical and biophysical characterization of two glucuronoxylanases aiming the production of xylooligosaccharides

Vacilotto

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Control of Substrate Conformation by Hydrogen Bonding in a Retaining β‐Endoglycosidase

Nin‐Hill,

Ardevol,

Biarnés

et al. 2023

Chemistry A European J

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Bacterial β‐glycosidases are hydrolytic enzymes that depolymerize polysaccharides such as β‐cellulose, β‐glucans and β‐xylans from different sources, which are used in a myriad of biomedical and industrial applications. It has been shown that a conformational change of the substrate, from a relaxed 4C1 conformation to a distorted 1S3/1,4B conformation of the reactive sugar, is necessary for catalysis. However, the molecular determinants that stabilize the substrate’s distortion are poorly understood. Here we use quantum mechanics/molecular mechanics (QM/MM)‐based molecular dynamics methods to assess the impact of the interaction between the reactive sugar, i.e. the one at subsite ‐1, and the catalytic nucleophile (a glutamate) on substrate conformation. We show that the hydrogen bond involving the C2 exocyclic group and the nucleophile controls substrate conformation: its presence preserves sugar distortion, whereas its absence (e.g. in an enzyme mutant) knocks it out. We also show that 2‐deoxy‐2‐fluoro derivatives, widely used to trap the reaction intermediates by X‐ray crystallography, reproduce the conformation of the hydrolysable substrate at the experimental conditions. These results highlight the importance of the 2‐OH···nucleophile interaction in substrate recognition and catalysis in endo‐glycosidases and can inform mutational campaigns aimed to search for more efficient enzymes.

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Enzymatic activities of Lactiplantibacillus plantarum: technological and functional role in food processing and human nutrition

Paventi,

Di Martino,

Crawford Jr

et al. 2024

Food Bioscience

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Glycoside hydrolases: Mechanisms, specificities, and engineering

Cited by 4 publications

References 94 publications

Biochemical and biophysical characterization of two glucuronoxylanases aiming the production of xylooligosaccharides

Biochemical and biophysical characterization of two glucuronoxylanases aiming the production of xylooligosaccharides

Control of Substrate Conformation by Hydrogen Bonding in a Retaining β‐Endoglycosidase

Enzymatic activities of Lactiplantibacillus plantarum: technological and functional role in food processing and human nutrition

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