Mining and modification of Oryza sativa-derived squalene epoxidase for improved β-amyrin production in Saccharomyces cerevisiae.
Metabolic engineering
Protein engineering
Saccharomyces cerevisiae
Squalene epoxidase
β-Amyrin
Journal
Journal of biotechnology
ISSN: 1873-4863
Titre abrégé: J Biotechnol
Pays: Netherlands
ID NLM: 8411927
Informations de publication
Date de publication:
20 Sep 2023
20 Sep 2023
Historique:
received:
07
03
2023
revised:
13
07
2023
accepted:
14
08
2023
medline:
18
9
2023
pubmed:
20
8
2023
entrez:
19
8
2023
Statut:
ppublish
Résumé
β-Amyrin is a pentacyclic triterpenoid and has anti-viral, anti-bacterial and anti-inflammatory activities. The synthetic pathway of β-amyrin has been analyzed and its heterogeneous synthesis has been achieved in Saccharomyces cerevisiae. Squalene epoxidase (SQE) catalyzes the oxygenation of squalene to form 2,3-oxidosqualene and is rate-limiting in the synthetic pathways of β-amyrin. The endogenous SQE in S. cerevisiae is insufficient for high production of β-amyrin. Herein, eight squalene epoxidases derived from different plants were selected and characterized in S. cerevisiae for improved biosynthesis of β-amyrin. Among them, the squalene epoxidase from Oryza sativa (OsSQE52) showed the best performance compared to other plant-derived sources. Through protein remodeling, the mutant OsSQE52
Identifiants
pubmed: 37597655
pii: S0168-1656(23)00143-8
doi: 10.1016/j.jbiotec.2023.08.004
pii:
doi:
Substances chimiques
Squalene Monooxygenase
EC 1.14.14.17
2,3-oxidosqualene
0
oxidosqualene
2Y5JJZ8E4W
Squalene
7QWM220FJH
beta-amyrin
KM8353IPSO
Triterpenes
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1-11Informations de copyright
Copyright © 2023 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.