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Conversion of a Mono‐ and Diacylglycerol Lipase into a Triacylglycerol Lipase by Protein Engineering
Author(s) -
Lan Dongming,
Popowicz Grzegorz Maria,
Pavlidis Ioannis V.,
Zhou Pengfei,
Bornscheuer Uwe T.,
Wang Yonghua
Publication year - 2015
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201500163
Subject(s) - lipase , diacylglycerol lipase , biochemistry , diacylglycerol kinase , substrate (aquarium) , protein engineering , enzyme , monoacylglycerol lipase , directed evolution , chemistry , triacylglycerol lipase , biology , mutant , ecology , endocannabinoid system , receptor , protein kinase c , gene
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.