Table 2.
Steady-state kinetic parametersa of BphAEB356, BphAELB400, and BphAEp4 toward diphenylmethane and benzophenone
| Substrate and enzyme | Km (mM) | kcat (s−1) | kcat/Km (103 · M−1 · s−1) |
|---|---|---|---|
| Diphenylmethane | |||
| BphAEB356 | 63.0 (5.6) | 8.9 (0.3) | 141.3 (7.5) |
| BphAELB400 | 15.4 (1.1) | 1.0 (0.1) | 64.9 (2.7) |
| BphAEp4 | 17.9 (2.2) | 1.6 (0.1) | 89.4 (5.5) |
| Benzophenone | |||
| BphAEB356 | 65.3 (8.5) | 1.2 (0.2) | 18.4 (0.6) |
| BphAELB400 | NDb | ND | ND |
| BphAEp4 | 9.1 (2.1) | 0.1 (0.0) | 11.0 (1.6) |
a
The steady-states kinetics were determined from the oxygen consumption rates as described in Materials and Methods. The values are results ± standard deviations from three independently produced enzyme preparations.
b
ND, not determined; metabolism was too slow to determine values accurately.