Transesterification of a Tertiary Alcohol by Engineered Candida antarctica Lipase A.
biocatalysis
enzymes
kinetic resolution
protein engineering
tertiary alcohols
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
03 06 2019
03 06 2019
Historique:
received:
18
12
2018
pubmed:
25
1
2019
medline:
21
4
2020
entrez:
25
1
2019
Statut:
ppublish
Résumé
Tertiary alcohols are known to be challenging substrates for applications in asymmetric synthesis due to their complexity and steric hinderance. The occurrence of tertiary alcohols and their esters in nature indicates the presence of natural biocatalytic synthetic routes for their preparation. Lipase A from Candida antarctica (CalA) is a hydrolase that has previously been shown to catalyze the transesterification of racemic 2-phenylbut-3-yn-2-ol at a low rate. In this work, the activity of that enzyme was improved by protein engineering through a semi-rational design strategy. An enzyme library was created and screened for transesterification activity towards racemic 2-phenylbut-3-yn-2-ol in an organic solvent. One successful enzyme variant (L367G) showed a tenfold increased reaction rate compared to the wild-type enzyme, while maintaining a high enantioselectivity.
Identifiants
pubmed: 30676685
doi: 10.1002/cbic.201800792
doi:
Substances chimiques
Fungal Proteins
0
Lipase
EC 3.1.1.3
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1438-1443Informations de copyright
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.