Pyranose dehydrogenases: Rare enzymes for electrochemistry and biocatalysis.
Bioelectrochemistry
; 132: 107399, 2020 Apr.
Article
em En
| MEDLINE
| ID: mdl-31835110
ABSTRACT
Pyranose dehydrogenase is a flavin-dependent carbohydrate oxidoreductase classified among Auxiliary Activities Family 3, along with structurally and catalytically related enzymes like pyranose oxidase and cellobiose dehydrogenase, and probably fulfils biological functions in lignocellulose breakdown. It is limited to a rather small group of litter-decomposing basidiomycetes adapted to humic-rich habitats, and shows an equally rare combination of structural and biochemical properties. It displays broader substrate specificity and regioselectivity compared to similar enzymes, catalyzing monooxidations at C1, C2, C3 or dioxidations at C2, 3 or C3, 4, depending on the pyranose sugar form (mono-/di-/oligo-saccharide or glycoside) and the enzyme source. It is unable to utilize oxygen as electron acceptor, using substituted benzoquinones and (organo)metallic ions instead, which suggests a role in redox cycling of (hydro)quinones and complexed metal ions. Pyranose dehydrogenase is a promising candidate for enzymatic sensors of various sugars, for the anodic reaction in enzymatic biofuel cells powered by carbohydrate mixtures, and as a versatile biocatalyst for the production of di- and tri-carbonyl sugar derivatives as chiral intermediates for the synthesis of rare sugars, novel drugs and fine chemicals.
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1
Base de dados:
MEDLINE
Assunto principal:
Desidrogenases de Carboidrato
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Técnicas Eletroquímicas
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Biocatálise
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article