Probing the role of an invariant active site His in family GH1 β-glycosidases

The reaction mechanism of glycoside hydrolases belonging to family 1 (GH1) of carbohydrate-active enzymes classification, hydrolysing β-O-glycosidic bonds, is well characterised. This family includes several thousands of enzymes with more than 20 different EC numbers depending on the sugar glycone r...

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Main Authors: Andrea Strazzulli, Giuseppe Perugino, Marialuisa Mazzone, Mosè Rossi, Stephen G. Withers, Marco Moracci
Format: Article
Language:English
Published: Taylor & Francis Group 2019-01-01
Series:Journal of Enzyme Inhibition and Medicinal Chemistry
Subjects:
Online Access:http://dx.doi.org/10.1080/14756366.2019.1608198
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author Andrea Strazzulli
Giuseppe Perugino
Marialuisa Mazzone
Mosè Rossi
Stephen G. Withers
Marco Moracci
author_facet Andrea Strazzulli
Giuseppe Perugino
Marialuisa Mazzone
Mosè Rossi
Stephen G. Withers
Marco Moracci
author_sort Andrea Strazzulli
collection DOAJ
description The reaction mechanism of glycoside hydrolases belonging to family 1 (GH1) of carbohydrate-active enzymes classification, hydrolysing β-O-glycosidic bonds, is well characterised. This family includes several thousands of enzymes with more than 20 different EC numbers depending on the sugar glycone recognised as substrate. Most GH1 β-glycosidases bind their substrates with similar specificity through invariant amino acid residues. Despite extensive studies, the clear identification of the roles played by each of these residues in the recognition of different glycones is not always possible. We demonstrated here that a histidine residue, completely conserved in the active site of the enzymes of this family, interacts with the C2-OH of the substrate in addition to the C3-OH as previously shown by 3 D-structure determination.
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spelling doaj.art-0530f2b6eba446bd9eb035a48b6d9df82022-12-22T02:03:21ZengTaylor & Francis GroupJournal of Enzyme Inhibition and Medicinal Chemistry1475-63661475-63742019-01-0134197398010.1080/14756366.2019.16081981608198Probing the role of an invariant active site His in family GH1 β-glycosidasesAndrea Strazzulli0Giuseppe Perugino1Marialuisa Mazzone2Mosè Rossi3Stephen G. Withers4Marco Moracci5University of Naples "Federico II", Complesso Universitario di Monte S. AngeloInstitute of Biosciences and BioResources – National Research Council of ItalyInstitute of Biosciences and BioResources – National Research Council of ItalyInstitute of Biosciences and BioResources – National Research Council of ItalyUniversity of British ColumbiaUniversity of Naples "Federico II", Complesso Universitario di Monte S. AngeloThe reaction mechanism of glycoside hydrolases belonging to family 1 (GH1) of carbohydrate-active enzymes classification, hydrolysing β-O-glycosidic bonds, is well characterised. This family includes several thousands of enzymes with more than 20 different EC numbers depending on the sugar glycone recognised as substrate. Most GH1 β-glycosidases bind their substrates with similar specificity through invariant amino acid residues. Despite extensive studies, the clear identification of the roles played by each of these residues in the recognition of different glycones is not always possible. We demonstrated here that a histidine residue, completely conserved in the active site of the enzymes of this family, interacts with the C2-OH of the substrate in addition to the C3-OH as previously shown by 3 D-structure determination.http://dx.doi.org/10.1080/14756366.2019.1608198inhibitionreaction mechanismglycosidasesextremophiles
spellingShingle Andrea Strazzulli
Giuseppe Perugino
Marialuisa Mazzone
Mosè Rossi
Stephen G. Withers
Marco Moracci
Probing the role of an invariant active site His in family GH1 β-glycosidases
Journal of Enzyme Inhibition and Medicinal Chemistry
inhibition
reaction mechanism
glycosidases
extremophiles
title Probing the role of an invariant active site His in family GH1 β-glycosidases
title_full Probing the role of an invariant active site His in family GH1 β-glycosidases
title_fullStr Probing the role of an invariant active site His in family GH1 β-glycosidases
title_full_unstemmed Probing the role of an invariant active site His in family GH1 β-glycosidases
title_short Probing the role of an invariant active site His in family GH1 β-glycosidases
title_sort probing the role of an invariant active site his in family gh1 β glycosidases
topic inhibition
reaction mechanism
glycosidases
extremophiles
url http://dx.doi.org/10.1080/14756366.2019.1608198
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AT moserossi probingtheroleofaninvariantactivesitehisinfamilygh1bglycosidases
AT stephengwithers probingtheroleofaninvariantactivesitehisinfamilygh1bglycosidases
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