Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase (GH1) from Antarctic Marinomonas sp. ef1.
cold-active enzyme
crystal structure
glucose tolerance
psychrophiles
β-glucosidase
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
23 Feb 2024
23 Feb 2024
Historique:
revised:
19
01
2024
received:
24
07
2023
accepted:
07
02
2024
medline:
24
2
2024
pubmed:
24
2
2024
entrez:
24
2
2024
Statut:
aheadofprint
Résumé
Cold-active enzymes support life at low temperatures due to their ability to maintain high activity in the cold and can be useful in several biotechnological applications. Although information on the mechanisms of enzyme cold adaptation is still too limited to devise general rules, it appears that very diverse structural and functional changes are exploited in different protein families and within the same family. In this context, we studied the cold adaptation mechanism and the functional properties of a member of the glycoside hydrolase family 1 (GH1) from the Antarctic bacterium Marinomonas sp. ef1. This enzyme exhibits all typical functional hallmarks of cold adaptation, including high catalytic activity at 5 °C, broad substrate specificity, low thermal stability, and higher lability of the active site compared to the overall structure. Analysis of the here-reported crystal structure (1.8 Å resolution) and molecular dynamics simulations suggest that cold activity and thermolability may be due to a flexible region around the active site (residues 298-331), whereas the dynamic behavior of loops flanking the active site (residues 47-61 and 407-413) may favor enzyme-substrate interactions at the optimal temperature of catalysis (T
Banques de données
RefSeq
['WP_100188174.1']
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Università degli Studi di Milano
Organisme : Italian Ministry of University and Research (MUR) through grant "Dipartimenti di Eccellenza 2023"
Organisme : Fondo di Ateneo of the University of Milano-Bicocca
ID : 2018-ATE-0320
Organisme : Fondo di Ateneo of the University of Milano-Bicocca
ID : 2023-ATE-0015
Organisme : Italian Ministry of University and Research (MUR)
Informations de copyright
© 2024 Federation of European Biochemical Societies.
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