Table 1.
kcat or kex (s−1) | Km or Kd (M) |
kcat/Km or kex/Kd (M−1 s−1) |
||||
---|---|---|---|---|---|---|
Wildtype | R235A | Wildtype | R235A | Wildtype | R235A | |
OMP b | 15 | 1.0 | 1.4 × 10−6 | 1.1 × 10−3 | 1.1 × 107 | 910 |
Effect of mutation | 15-fold decrease | 790-fold increase | 12000-fold decrease | |||
FOMP c | 95 | 92 | 8 ×10−6 | 5.8 × 10−4 | 1.2 × 107 | 1.6 × 105 |
Effect of mutation | No effect | 73-fold increase | 75-fold decrease | |||
h-FUMP d | 0.044 | 9.3 × 10−6 | 1.1 × 10−4 | 5.0 × 10−3 | 400 | 1.9 × 10−3 |
Effect of mutation | 4700-fold decrease | 45-fold increase | 210000-fold decrease |
The kinetic parameters kcat and Km, and kex and Kd, respectively, are used for the ScOMPDC-catalyzed decarboxylation and deuterium exchange reactions.
At pH 7.1 (30 mM MOPS) 25 °C, and I = 0.10 (NaCl). Data for wildtype ScOMPDC is from Ref. 38.
At pH 7.1 (10 mM MOPS) 25 °C, and I = 0.10 (NaCl). Data for wildtype ScOMPDC is from Ref. 39.
At pD 8.15 (20 mM GlyGly, 20% free base), and I = 0.14 (NaCl). Data for wildtype ScOMPDC is from Ref. 13.