TABLE 1.
Enzyme | Substrate | Michaelian parameter
|
Non-Michaelian parametere
|
||||
---|---|---|---|---|---|---|---|
Km (μM) | kcat (s−1) | kcat/Km (s−1·M−1) | S50 (μM) | Vmax (s−1) | n | ||
DAPDH | NAD+a | 16 ± 1 | 34 ± 0.7 | 2.1 106 | |||
NADP+a | 2,560 ± 280 | 5 ± 0.5 | 2.0 103 | ||||
(2R,4S)-DAPb | 109 ± 4 | 51.6 ± 0.6 | 1.24 ± 0.04 | ||||
(2R,4R)-DAPb | 1,800 ± 200 | 2.8 ± 0.1 | 1.77 ± 0.25 | ||||
OR | l-Ornithine | 520 ± 20 | 1,660 ± 30 | 3.2 106 | |||
AKPT | CoA-SHc | 18 ± 3 | 3.5 ± 0.2 | 1.9 105 | |||
AKPd | 35 ± 6 | 3.4 ± 0.2 | 9.7 104 |
The (2R,4S)-DAP concentration was 800 μM.
The NAD+ concentration was 2 mM.
The AKP concentration was 350 μM.
The CoA-SH concentration was 80 μM.
S50 is the substrate concentration showing half-maximal velocity, n is the Hill coefficient, and Vmax is the maximal velocity.