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Wang, X.* ; Tang, Q.* ; Popowicz, G.M. ; Yang, B.* ; Wang, Y.*

A mechanistic study into the epoxidation of carboxylic acid and alkene in a mono, di-acylglycerol lipase.

Biochem. Biophys. Res. Commun. 460, 392-396 (2015)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
More and more industrial chemistry reactions relies on green technologies. Enzymes are finding increasing use in diverse chemical processes. Epoxidized vegetable oils have recently found applications as plasticizers and additives for PVC production. We report here an unusual activity of the M. globosa lipase (SMG1) that is able to catalyze epoxidation of alkenes. SMG1 catalyzes formation of peroxides from long chain carboxylic acids that subsequently react with double bonds of alkenes to produce epoxides. The SMG1 is selective towards carboxylic acids and active also as a mutant lacking hydrolase activity. Moreover we present previously unobserved mechanism of catalysis that does not rely on acyl-substrate complex nor tetrahedral intermediate. Since SMG1 lipase is activated by allosteric change upon binding to the lipophilic-hydrophilic phase interface we reason that it can be used to drive the epoxidation in the lipohilic phase exclusively.
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Publication type Article: Journal article
Document type Scientific Article
Keywords M. Globosa Lipase ; Alkene ; Carboxylic Acid ; Epoxidation ; Mechanism ; Oil; Epoxidized Sunflower Oil; Malassezia-globosa; Soybean Oil; Diacylglycerol Lipase; Hydrogen-peroxide; Perhydrolysis; Catalysis; Alpha
Language english
Publication Year 2015
HGF-reported in Year 2015
ISSN (print) / ISBN 0006-291X
e-ISSN 1090-2104
Journal Biochemical and Biophysical Research Communications
Quellenangaben Volume: 460, Issue: 2, Pages: 392-396 Article Number: , Supplement: ,
Publisher Elsevier
Publishing Place San Diego
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503000-003
PubMed ID 25783054
DOI 10.1016/j.bbrc.2015.03.044
WOS ID WOS:000354230300043
Scopus ID 84937965398
Scopus ID 84925428233
Erfassungsdatum 2015-03-20
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