Discovery of a catalytic domain defines a new glycoside hydrolase family containing endo-1,3-fucanase.
AlphaFold2
Catalytic domain
Fucanase
Glycoside hydrolase
Polysaccharide utilization locus
Sulfated fucan
Journal
Carbohydrate polymers
ISSN: 1879-1344
Titre abrégé: Carbohydr Polym
Pays: England
ID NLM: 8307156
Informations de publication
Date de publication:
01 Jan 2024
01 Jan 2024
Historique:
received:
27
07
2023
revised:
23
09
2023
accepted:
27
09
2023
medline:
10
11
2023
pubmed:
9
11
2023
entrez:
8
11
2023
Statut:
ppublish
Résumé
Sulfated fucans are important marine polysaccharides with various bioactivities. Fucanases are desirable tools for the structural elucidations and oligosaccharides preparation of sulfated fucans. Herein, a gene with unknown function was screened from a sulfated fucan utilization locus in genome of marine bacterium Wenyingzhuangia aestuarii OF219 with the assistance of a machine learning approach on the structural biology. An undefined catalytic domain that presented in this gene was further cloned and expressed in Escherichia coli. Utilizing a sulfated fucan tetrasaccharide with definite structure as substrate, the endo-acting cleavage point of expressed protein (named Fun187A) was identified as the α-l-1,3-glycosidic bond between Fucp and Fucp(2OSO
Identifiants
pubmed: 37940306
pii: S0144-8617(23)00907-4
doi: 10.1016/j.carbpol.2023.121442
pii:
doi:
Substances chimiques
Glycoside Hydrolases
EC 3.2.1.-
Polysaccharides
0
Oligosaccharides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
121442Informations de copyright
Copyright © 2023 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.