A "Pro-Asp-Thr" Amino Acid Repeat from
alginate lyase
alginate-binding module
multi-domain
soluble expression
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
26 May 2024
26 May 2024
Historique:
received:
17
01
2024
revised:
10
05
2024
accepted:
16
05
2024
medline:
19
6
2024
pubmed:
19
6
2024
entrez:
19
6
2024
Statut:
epublish
Résumé
Alginate lyases cleave the 1,4-glycosidic bond of alginate by eliminating sugar molecules from its bond. While earlier reported alginate lyases were primarily single catalytic domains, research on multi-module alginate lyases has been lfiguimited. This study identified VsAly7A, a multi-module alginate lyase present in
Identifiants
pubmed: 38891987
pii: ijms25115801
doi: 10.3390/ijms25115801
pii:
doi:
Substances chimiques
Polysaccharide-Lyases
EC 4.2.2.-
poly(beta-D-mannuronate) lyase
EC 4.2.2.3
Alginates
0
Bacterial Proteins
0
Recombinant Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Qingdao Marine Science and Technology Center
ID : 2022QNLM030003-1
Organisme : Natural Science Foundation of Shandong Province
ID : ZR2019ZD18
Organisme : Shandong Province Technology Innovation Guidance Program
ID : 2018YFC0311105
Organisme : Science & Technology Development Project of Qingdao
ID : 22-3-6-gjxm-5-gx
Organisme : Science & Technology Development Project of Qingdao
ID : 21-1-6-gjxm-27-gx
Organisme : Science & Technology Development Project of Qingdao
ID : 20-11-6-64-gx