Structural and biochemical insight into mode of action and subsite specificity of a chitosan degrading enzyme from Bacillus spec. MN.
Acetylation
Acetylglucosamine
/ chemistry
Bacillus
/ enzymology
Bacterial Proteins
/ chemistry
Binding Sites
Chitosan
/ chemistry
Glucosamine
/ chemistry
Glycoside Hydrolases
/ chemistry
Models, Molecular
Molecular Docking Simulation
Protein Binding
Protein Conformation
Protein Multimerization
Substrate Specificity
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
04 02 2019
04 02 2019
Historique:
received:
04
09
2018
accepted:
14
11
2018
entrez:
6
2
2019
pubmed:
6
2
2019
medline:
21
8
2020
Statut:
epublish
Résumé
Chitosans, partially de-N-acetylated derivatives of chitin, are multifunctional biopolymers. In nature, biological activities of partially acetylated chitosan polymers are mediated in part by their oligomeric breakdown products, which are generated in situ by the action of chitosanolytic enzymes. Understanding chitosanolytic enzymes, therefore, can lead to the production of chitosan oligomers with fully defined structures that may confer specific bioactivities. To address whether defined oligomer products can be produced via chitosanolytic enzymes, we here characterized a GH8 family chitosanase from Bacillus spec. MN, determining its mode of action and product profiles. We found that the enzyme has higher activity towards polymers with lower degree of acetylation. Oligomeric products were dominated by GlcN
Identifiants
pubmed: 30718524
doi: 10.1038/s41598-018-36213-6
pii: 10.1038/s41598-018-36213-6
pmc: PMC6362164
doi:
Substances chimiques
Bacterial Proteins
0
Chitosan
9012-76-4
Glycoside Hydrolases
EC 3.2.1.-
chitosanase
EC 3.2.1.132
Glucosamine
N08U5BOQ1K
Acetylglucosamine
V956696549
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1132Références
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