Glycoside hydrolases from (hyper)thermophilic archaea : structure, function, and applications

© 2023 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society..

(Hyper)thermophilic archaeal glycosidases are enzymes that catalyze the hydrolysis of glycosidic bonds to break down complex sugars and polysaccharides at high temperatures. These enzymes have an unique structure that allows them to remain stable and functional in extreme environments such as hot springs and hydrothermal vents. This review provides an overview of the current knowledge and milestones on the structures and functions of (hyper)thermophilic archaeal glycosidases and their potential applications in various fields. In particular, this review focuses on the structural characteristics of these enzymes and how these features relate to their catalytic activity by discussing different types of (hyper)thermophilic archaeal glycosidases, including β-glucosidases, chitinase, cellulases and α-amylases, describing their molecular structures, active sites, and mechanisms of action, including their role in the hydrolysis of carbohydrates. By providing a comprehensive overview of (hyper)thermophilic archaeal glycosidases, this review aims to stimulate further research into these fascinating enzymes.

Medienart:

E-Artikel

Erscheinungsjahr:

2023

Erschienen:

2023

Enthalten in:

Zur Gesamtaufnahme - volume:67

Enthalten in:

Essays in biochemistry - 67(2023), 4 vom: 11. Aug., Seite 731-751

Sprache:

Englisch

Beteiligte Personen:

Iacono, Roberta [VerfasserIn]
De Lise, Federica [VerfasserIn]
Moracci, Marco [VerfasserIn]
Cobucci-Ponzano, Beatrice [VerfasserIn]
Strazzulli, Andrea [VerfasserIn]

Links:

Volltext

Themen:

Archaea
CAZymes
EC 3.2.1.-
Extremozymes
Glycosidases
Glycoside Hydrolases
Hyperthermophiles
Journal Article
Research Support, Non-U.S. Gov't
Review

Anmerkungen:

Date Completed 14.08.2023

Date Revised 15.08.2023

published: Print

Citation Status MEDLINE

doi:

10.1042/EBC20220196

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM358426235