Apparent Kinetic Constants for Selected lipase B Variants with p-Nitrophenol butyrate and DiFMU Octanoate as Substrates

Range Table - link
Organism Yeast Candida antarctica
Reference Qian Z, Lutz S. Improving the catalytic activity of Candida antarctica lipase B by circular permutation. J Am Chem Soc. 2005 Oct 5 127(39):13466-7. Table 1PubMed ID16190688
Method Directed evolution: To examine the impact of circular permutation on catalysis, researchers selected eight functional lipase B from Candida antarctica (CALB) variants with termini in or near the active site for detailed kinetic characterization (Figure 2). Following overexpression in P. pastoris, the proteins were purified to homogeneity, and kinetic data for these variants were measured on two standard lipase substrates, p-nitrophenol butyrate (pNB) and 6.8-difluoro-4-methylumbelliferyl (DiFMU) octanoate (table link).
Entered by Uri M
ID 105428