Table 1 Steady-state kinetic constants of cytidylyltransferasesa
From: The predominance of nucleotidyl activation in bacterial phosphonate biosynthesis
Enzyme | Substrate | kcat (s−1) | KM (mM) | kcat/KM (M−1 s−1) | Specificityb | Ref. |
|---|---|---|---|---|---|---|
Ari-PntC | AEP | 3.7 ± 0.1 | 0.012 ± 0.001 | 3.2 × 105 | 0.0023 | This work |
ChoPc | 0.7 ± 0.3 | 1.0 ± 0.8 | 7.2 × 102 | |||
Spn-LicC | AEP | 0.72 ± 0.05 | 0.3 ± 0.1 | 2.3 × 103 | 200 | This work |
ChoPd | 1.06 ± 0.04 | 2.4( ± 0.6)x10−3 | 4.5 × 105 | |||
ChoP | 3.6 | 0.060 | 6.0 × 104 | 2700 | ||
PEtn | 0.031 | 1.43 | 22 | |||
ChoP | 17.5 | 0.39 | 4.5 × 104 | |||
ChoP | 37 | 0.066 | 5.6 × 105 | |||
Tde-PntC | AEP | 1.05 ± 0.05 | 0.016 ± 0.005 | 6.8 × 104 | ND | This work |
ChoP | NDe | ND | ND |
