Scrutiny of Metal Ion Binding Sites in Different Alginate Lyases through In Silico Analysis.
Alginate lyase
Biotherapeutic agent
Computational analysis
Enzyme
Metal ion affinity
Journal
Applied biochemistry and biotechnology
ISSN: 1559-0291
Titre abrégé: Appl Biochem Biotechnol
Pays: United States
ID NLM: 8208561
Informations de publication
Date de publication:
Jan 2022
Jan 2022
Historique:
received:
15
07
2021
accepted:
21
10
2021
pubmed:
8
1
2022
medline:
8
2
2022
entrez:
7
1
2022
Statut:
ppublish
Résumé
Alginate lyases are epitomized as prospective therapeutic mediators for treating Pseudomonas aeruginosa infections, particularly in the cystic fibrosis airway through alginate degradation thereby improving the efficacy of anti-pseudomonal antibiotics. Investigation of metal-binding residues is significant for expounding the ion specificity of an enzyme and will provide a broad understanding of the potential roles of metal ions in enzyme function and stability. However, experimental analysis of metal ion-binding sites in proteins is time consuming and expensive. Concerning the clinical importance of this therapeutic enzyme, the present study was focused on the prediction and characterization of metal ion-binding sites of different alginate lyases reported in the literature through a computational approach using a Metal Ion-Binding Site Prediction and Docking Server. 3D structures of different alginate lyase from different organisms were retrieved, and these retrieved proteins were docked with twelve different metal ions such as Ca
Identifiants
pubmed: 34993770
doi: 10.1007/s12010-021-03746-y
pii: 10.1007/s12010-021-03746-y
doi:
Substances chimiques
Bacterial Proteins
0
Metals
0
Polysaccharide-Lyases
EC 4.2.2.-
poly(beta-D-mannuronate) lyase
EC 4.2.2.3
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
124-147Informations de copyright
© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
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