| Value |
0.03
sec^-1
|
| 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 1 Table - link PubMed 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). |
| Comments |
2±0.1min^-1. Note-In 'The metabolic pathway engineering handbook' (CRC Press), ed. C.D. Smolke 2010, Chapter 2-23, Nair and Zhao point that researchers in the above experiment used ~5×10^5 mutants and increased catalytic efficiency of CALB for 6,8-difluoro-4-methylumbelliferyl octanoate nearly 29 fold (see table link). |
| Entered by |
Uri M |
| ID |
105430 |