Phenylalanine to leucine point mutation in oxyanion hole improved catalytic efficiency of Lip12 from Yarrowia lipolytica.

Abstract

In lipases, oxyanion hole has crucial role in the stabilisation of enzyme-substrate complex. Majority of lipases from Yarrowia lipolytica consist of two oxyanion hole residues viz.; Thr and Leu. However, Lip12 has Phe instead of Leu at second oxyanion hole residue. It was observed that Lip12 has lower specific activity and catalytic efficiency than other… (More)
DOI: 10.1016/j.enzmictec.2013.08.004

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