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Tang, Q.* ; Popowicz, G.M. ; Wang, X.* ; Liu, J.* ; Pavlidis, I.V.* ; Wang, Y.*

Lipase-driven epoxidation is a two-stage synergistic process.

ChemistrySelect 1, 836-839 (2016)
DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Epoxidation ; Peroxides ; Enzyme ; Industrial Catalysis ; Protein Structure; Renewable Raw-materials; Chemistry; Fats; Oils
ISSN (print) / ISBN 2365-6549
e-ISSN 2365-6549
Zeitschrift ChemistrySelect
Quellenangaben Band: 1, Heft: 4, Seiten: 836-839 Artikelnummer: , Supplement: ,
Verlag Wiley
Verlagsort Weinheim
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)