Rational Enzyme Design without Structural Knowledge: A Sequence-Based Approach for Efficient Generation of Transglycosylases.
enzyme catalysis
hydrolases
multiple sequences alignment
oligosaccharide synthesis
protein engineering
transglycosylation
Journal
Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
Titre abrégé: Chemistry
Pays: Germany
ID NLM: 9513783
Informations de publication
Date de publication:
16 Jul 2021
16 Jul 2021
Historique:
received:
11
01
2021
pubmed:
30
4
2021
medline:
21
7
2021
entrez:
29
4
2021
Statut:
ppublish
Résumé
Glycobiology is dogged by the relative scarcity of synthetic, defined oligosaccharides. Enzyme-catalysed glycosylation using glycoside hydrolases is feasible but is hampered by the innate hydrolytic activity of these enzymes. Protein engineering is useful to remedy this, but it usually requires prior structural knowledge of the target enzyme, and/or relies on extensive, time-consuming screening and analysis. Here, a straightforward strategy that involves rational rapid in silico analysis of protein sequences is described. The method pinpoints 6-12 single-mutant candidates to improve transglycosylation yields. Requiring very little prior knowledge of the target enzyme other than its sequence, the method is generic and procures catalysts for the formation of glycosidic bonds involving various d/l-, α/β-pyranosides or furanosides, and exo or endo action. Moreover, mutations validated in one enzyme can be transposed to others, even distantly related enzymes.
Identifiants
pubmed: 33914359
doi: 10.1002/chem.202100110
doi:
Substances chimiques
Oligosaccharides
0
Glycosyltransferases
EC 2.4.-
Glycoside Hydrolases
EC 3.2.1.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
10323-10334Subventions
Organisme : Novo Nordisk Fonden
ID : NNF17OC0025660
Informations de copyright
© 2021 Wiley-VCH GmbH.
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