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Lan, D.* ; Popowicz, G.M. ; Pavlidis, I.V.* ; Zhou, P.* ; Bornscheuer, U.T.* ; Wang, Y.*

Conversion of a mono- and diacylglycerol lipase into a triacylglycerol lipase by protein engineering.

ChemBioChem 16, 1431-1434 (2015)
DOI Verlagsversion bestellen
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Despite the fact that most lipases are believed to be active against triacylglycerides, there is a small group of lipases that are active only on mono- and diacylglycerides. The reason for this difference in substrate scope is not clear. We tried to identify the reasons for this in the lipase from Malassezia globosa. By protein engineering, and with only one mutation, we managed to convert this enzyme into a typical triacylglycerol lipase (the wild-type lipase does not accept triacylglycerides). The variant Q282L accepts a broad spectrum of triacylglycerides, although the catalytic behavior is altered to some extent. From in silico analysis it seems that specific hydrophobic interactions are key to the altered substrate specificity. A mono- and diglyceride lipase was engineered to a triacylglyceride lipase by introducing a single point mutation (Q282L). The variant has broad substrate specificity on triacylglycerides. The results indicate that the main reason that the wild-type enzyme does not accept triacylglycerides is not their bulkiness, but specific hydrophobic interactions.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Enzyme Catalysis ; Lipases ; Protein Engineering ; Steric Hindrance ; Substrate Specificity; Pichia-pastoris; Specificity; Brain
ISSN (print) / ISBN 1439-4227
e-ISSN 1439-7633
Zeitschrift ChemBioChem
Quellenangaben Band: 16, Heft: 10, Seiten: 1431-1434 Artikelnummer: , Supplement: ,
Verlag Wiley
Verlagsort Weinheim
Begutachtungsstatus Peer reviewed