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

(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 and x-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.

Automated summary

Hyperthermophilic archaeal glycosidases are enzymes that break down complex sugars and polysaccharides at high temperatures. They have a unique structure that allows them to remain stable and functional in extreme environments. This review provides an overview of the current knowledge on the structures and functions of these enzymes and their potential applications in various fields, with a focus on their structural characteristics and catalytic activity.