| | 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
|
| | Wahl et al JBC 267(15) 10447-10456 1992. Homma et al JBC 263:14 1988 pp 6592. These parms are the Ca-stimulated form. This is close to Wahl's figure 7, which I am using as reference. Also see Nakanishi et al Biochem J 256 453-459 1998, Nishibe et al Science 250 :1253-1256 This model uses a rather low PIP2 of 10 uM. |
| 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. These parms are the Ca-stimulated form. Wahl et al JBC 267:15 10447-10456 1992 say that the tyrosine phosphorylated form has 7X higher affinity for substrate than control. The PIP2 levels in this model are rather low, at 10 uM. |
