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Lipase‐Driven Epoxidation Is A Two‐Stage Synergistic Process
Author(s) -
Tang Qingyun,
Popowicz Grzegorz M.,
Wang Xuping,
Liu Jinsong,
Pavlidis Ioannis V.,
Wang Yonghua
Publication year - 2016
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.201600254
Subject(s) - lipase , chemistry , catalytic triad , catalysis , serine , histidine , enzyme , hydrogen peroxide , catalytic cycle , combinatorial chemistry , organic chemistry
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.