Engineering Arabidopsis long-chain acyl-CoA synthetase 9 variants with enhanced enzyme activity.
Arabidopsis thaliana
LACS
Saccharomyces cerevisiae
error-prone PCR
protein engineering
Journal
The Biochemical journal
ISSN: 1470-8728
Titre abrégé: Biochem J
Pays: England
ID NLM: 2984726R
Informations de publication
Date de publication:
15 01 2019
15 01 2019
Historique:
received:
01
10
2018
revised:
11
12
2018
accepted:
17
12
2018
pubmed:
19
12
2018
medline:
5
9
2019
entrez:
19
12
2018
Statut:
epublish
Résumé
Long-chain acyl-CoA synthetase (LACS, EC 6.2.1.3) catalyzes the ATP-dependent activation of free fatty acid to form acyl-CoA, which, in turn, serves as the major acyl donor for various lipid metabolic pathways. Increasing the size of acyl-CoA pool by enhancing LACS activity appears to be a useful approach to improve the production and modify the composition of fatty acid-derived compounds, such as triacylglycerol. In the present study, we aimed to improve the enzyme activity of
Identifiants
pubmed: 30559328
pii: BCJ20180787
doi: 10.1042/BCJ20180787
doi:
Substances chimiques
Arabidopsis Proteins
0
Coenzyme A Ligases
EC 6.2.1.-
LACS9 protein, Arabidopsis
EC 6.2.1.3
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
151-164Informations de copyright
© 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.