Glycoside hydrolase family 18 chitinases: The known and the unknown.
Catalytic mechanism
Chitinase
Crystal structure
Glycoside hydrolase
Inhibitor
Physiological function
Journal
Biotechnology advances
ISSN: 1873-1899
Titre abrégé: Biotechnol Adv
Pays: England
ID NLM: 8403708
Informations de publication
Date de publication:
01 11 2020
01 11 2020
Historique:
received:
08
01
2020
revised:
09
03
2020
accepted:
20
04
2020
pubmed:
23
5
2020
medline:
13
1
2021
entrez:
23
5
2020
Statut:
ppublish
Résumé
Glycoside hydrolase family 18 (GH18) chitinases, which catalyze the biodegradation of β-1,4 glycosidic bond in amino polysaccharides via a substrate-assisted retention mechanism, are widely distributed in nature and have diverse functions. Many organisms produce several GH18 chitinases which take part in multiple physiological processes, including tissue degradation and remodeling, nutrition uptake, invasion and pathogenesis as well as immune response regulation. Because of their physiological importance, mounting crystallographic investigations have been conducted for GH18 chitinases, and their inhibitors have also been developed. However, there is still much unclear concerning these enzymes, such as the explicit mechanisms underlying their involvement in disease development, the direct connection of structure to processivity, and selectivity of the inhibitors. In this article, research progress on biological function, structural information and inhibition of GH18 chitinases has been reviewed and the remaining uncertainties are highlighted. This review may also facilitate those who intent to develop drugs or agrochemicals based on these enzymes.
Identifiants
pubmed: 32439576
pii: S0734-9750(20)30050-1
doi: 10.1016/j.biotechadv.2020.107553
pii:
doi:
Substances chimiques
Glycoside Hydrolases
EC 3.2.1.-
Chitinases
EC 3.2.1.14
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
107553Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.