期刊
CHEMCATCHEM
卷 1, 期 2, 页码 252-258出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.200900041
关键词
enzyme catalysis; enzyme promiscuity; lipases; Michael addition; molecular modeling
Suppression of,the,native hydrolytic activity of Pseudozyma antarctica lipase B (PalB) (formerly Candida antarctica lipase B) in water is demonstrated. By replacing the catalytic Ser 105 residue with an alanine unit, promiscuous Michael addition activity is favored. A Michael addition reaction between methyl acrylate and acetylacetone was explored as a model system. For the PalB Ser 105 Ala mutant, the hydrolytic activity was suppressed more than 1000 times and at the same time, the Michael addition activity was increased by a factor of 100. Docking studies and molecular dynamics simulations revealed an increased ability of the PalB Ser 105 Ala mutant to harbor the substrates close to a catalytically competent conformation.
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