| | Molecule Name/
Site Name | Km (uM) | kcat (1/s) | Ratio
(k2/k3) | Enzyme Type | Substrate | Product |
| 1 |
Enzyme Activity:
PIP2_hydrolysis
Enzyme Molecule:
Ca.PLC_g | 97.2222 | 14 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | PIP2
| DAG
IP3
|
| | Mainly Homma et al JBC 263:14 1988 pp 6592, but these parms are the Ca-stimulated form. It is not clear whether the enzyme is activated by tyrosine phosphorylation at this point or not. Wahl et al JBC 267:15 10447-10456 1992 say that the Ca_stim and phosph form has 7X higher affinity for substrate than control. This is close to Wahl's figure 7, which I am using as reference. |
| 2 |
Enzyme Activity:
PIP2_hydrolysis
Enzyme Molecule:
Ca.PLC_g* | 19.7917 | 57 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | PIP2
| DAG
IP3
|
| | Mainly Homma et al JBC 263:14 1988 pp 6592, but these parms are the Ca-stimulated form. It is not clear whether the enzyme is activated by tyrosine phosphorylation at this point or not. Wahl et al JBC 267:15 10447-10456 1992 say that this has 7X higher affinity for substrate than control. |
