Home
Deutsch
Advanced Search
Browse by ...
Publication overview
Contact persons
Help
DOI
 |
|
Open Access Green as soon as Postprint is submitted to ZB.
Lipase-driven epoxidation is a two-stage synergistic process.
ChemistrySelect 1, 836-839 (2016)
Lipases show high stability in lipophilic solvents and catalyze reactions at the water-oil interfaces, which are of great industrial interest. One promising application of lipases is the production of epoxides from alkenes and hydrogen peroxide. So far, little attention has been given to uncover the reaction mechanism for this in detail at the molecular level. Here, we present structural and mutational analysis of a lipase from Penicillium camembertii that indicates a two-stage synergistic mechanism for this reaction. Surprisingly, a mutant devoid of the catalytic serine retains a fraction of activity while histidine from the catalytic triad is absolutely critical to maintain the enzyme activity. Histidine appears to perform a dual-activation role acting both towards hydrogen peroxide and the catalytic serine. These results thus allow a better understanding of enzymatic epoxidation and engineering of more potent, stable and selective enzymes.
Altmetric
Additional Metrics?
Edit extra informations
Login
Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Epoxidation ; Peroxides ; Enzyme ; Industrial Catalysis ; Protein Structure; Renewable Raw-materials; Chemistry; Fats; Oils
ISSN (print) / ISBN
2365-6549
e-ISSN
2365-6549
Journal
ChemistrySelect
Quellenangaben
Volume: 1,
Issue: 4,
Pages: 836-839
Publisher
Wiley
Publishing Place
Weinheim
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)