Skip to main content
. Author manuscript; available in PMC: 2008 Dec 15.
Published in final edited form as: Arch Biochem Biophys. 2007 Oct 5;468(2):217–225. doi: 10.1016/j.abb.2007.09.023

Table 1.

Catalytic Activity of BbPDF and LpPDF Variantsa

enzyme metal content kcat (s−1) KM (μM) kcat/KM (M−1s−1)
Zn Co Fe
Zn-BbPDF1-HT 1.0 0 0 5.4 ± 0.1
20 ± 1b
2.5 ± 0.2
510 ± 70b
2.2 × 106
3.9 × 104b
Co-BbPDF1-HT 0.02 1.0 0 10 ± 1
26 ± 1b
3.9 ± 0.7
580 ± 60b
2.6 × 106
4.5 × 104b
Fe-BbPDF1-HT 0.08 0 0.59 3.8 ± 0.1 1.9 ± 0.2 2.0 × 106
Zn-BbPDF2-HT ND ND ND 5.3 ± 0.5 2.8 ± 1.0 2.0 × 106
Zn-BbPDF3-HT ND ND ND 0.062 ± 0.011 6.3 ± 1.2 1.0 × 104
Zn-BbPDF2 ND ND ND 5.6 ± 0.9 2.3 ± 0.6 2.5 × 106
Native BbPDF 1.1 0 0 4.5 ± 1.2 3.3 ± 0.4 1.4 × 106
Zn-LpPDF-HT ND ND ND 0.9 ± 0.1 17 ± 0 5.4 × 104
Co-LpPDF-HT ND ND ND 5.8 ± 0.3 22 ± 1 2.6 × 105
Fe-LpPDF-HT ND ND ND 4.3 ± 0.1 15 ± 1 3.0 × 105
a

Unless otherwise noted, the activities reported were determined with f-ML-pNA as substrate;

b

activity toward f-MAS; ND, not determined.