TABLE 3.
Pen and Pal enzyme properties
ND means not determined.
| Pen | Pal | pseB (C. jejuni)a | pseB (H. pylori)b | |
|---|---|---|---|---|
| Optimal pHc | 7.6 | 7.6 | 7.0 | 7.0 |
| Optimal temperature (°C)d | 37 | 30 | 42 | 37 |
| Km (mm)e | 0.143 ± 0.006 | ND | 0.050 | 0.159 |
| Vmax (nm s−1) | 15.01 ± 0.29 | ND | ||
| kcat (min−1) | 30.02 ± 0.58 | ND | 1.51 | 5.7 |
| kcat/Km (mm−1 min−1) | 209.9 ± 12.9 | ND | 30.6 | 35.9 |
| Protein monomer (kDa)f | 40 | 37.1 | 37.4 | 37.4 |
a Kinetic data of pseB in C. jejuni was from Ref. 35.
b Kinetic data of pseB in H. pylori was from Ref. 36.
c For Pen, optimal pH assays were determined using phosphate buffer in which Pen yielded the highest activity compared with MOPS-NaOH, Tris-HCl, and MES buffer. For Pal, optimal pH assays were determined using Tris-HCl buffer.
d Optimal temperature assays were determined using Tris-HCl for both Pen and Pal.
e The reaction was determined by HPLC-UV after a 5-min 30 °C incubation for Pen.
f The active forms of proteins eluted from the size-exclusion column were 192.8 kDa for Pen and 87.6 kDa for Pal, presumably suspected to be a tetramer and a dimer, respectively.