A Cold-Active Flavin-Dependent Monooxygenase from
Journal
ACS catalysis
ISSN: 2155-5435
Titre abrégé: ACS Catal
Pays: United States
ID NLM: 101562209
Informations de publication
Date de publication:
17 Mar 2023
17 Mar 2023
Historique:
received:
19
10
2022
revised:
31
01
2023
entrez:
27
3
2023
pubmed:
28
3
2023
medline:
28
3
2023
Statut:
epublish
Résumé
Cold-active enzymes maintain a large part of their optimal activity at low temperatures. Therefore, they can be used to avoid side reactions and preserve heat-sensitive compounds. Baeyer-Villiger monooxygenases (BVMO) utilize molecular oxygen as a co-substrate to catalyze reactions widely employed for steroid, agrochemical, antibiotic, and pheromone production. Oxygen has been described as the rate-limiting factor for some BVMO applications, thereby hindering their efficient utilization. Considering that oxygen solubility in water increases by 40% when the temperature is decreased from 30 to 10 °C, we set out to identify and characterize a cold-active BVMO. Using genome mining in the Antarctic organism
Identifiants
pubmed: 36970468
doi: 10.1021/acscatal.2c05160
pmc: PMC10028610
doi:
Types de publication
Journal Article
Langues
eng
Pagination
3549-3562Informations de copyright
© 2023 The Authors. Published by American Chemical Society.
Déclaration de conflit d'intérêts
The authors declare no competing financial interest.
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