Rationally engineered double substituted variants of Yarrowia lipolytica lipase with enhanced activity coupled with highly inverted enantioselectivity towards 2-bromo phenyl acetic acid esters

• Published in: Biotechnology and bioengineering Vol. 106; no. 6; pp. 852 - 859
• Main Authors: Cambon, Emmanuelle, Piamtongkam, Rungtiwa, Bordes, Florence, Duquesne, Sophie, André, Isabelle, Marty, Alain
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 15.08.2010; Wiley Subscription Services, Inc; Wiley
• Subjects: Acetates - metabolism; Acetic acid; Amino Acid Substitution; Amino acids; Bioengineering; Biotechnology; enantioselectivity; Enzymatic activity; enzyme evolution; Enzyme kinetics; Esters; Fungal Proteins - genetics; Fungal Proteins - metabolism; Hydrocarbons, Brominated - metabolism; Life Sciences; lipase; Lipase - genetics; Lipase - metabolism; Molecular Dynamics Simulation; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Pharmaceutical industry; Phenylacetates - metabolism; Protein folding; rational engineering; Stereoisomerism; Substrate Specificity; Yarrowia - enzymology; Yarrowia lipolytica

Inverting enzyme enantioselectivity by protein engineering is still a great challenge. Lip2p lipase from Yarrowia lipolytica, which demonstrates a low S-enantioselectivity (E-value = 5) during the hydrolytic kinetic resolution of 2-bromo-phenyl acetic acid octyl esters (an important class of chemica...