| | Molecule Name/
Site Name | Km (uM) | kcat (1/s) | Ratio
(k2/k3) | Enzyme Type | Substrate | Product |
| 1 |
Enzyme Activity:
PLC
Enzyme Molecule:
PLC | 19.9994 | 2.5 | 4 | explicit E-S complex | PIP2
| IP3(145)
DAG
|
| | Smrcka et al; Science 251, 15.2.1991, pp804-807 |
| 2 |
Enzyme Activity:
PLC-Ca
Enzyme Molecule:
PLC-Ca | 19.8408 | 10 | 4 | explicit E-S complex | PIP2
| IP3(145)
DAG
|
| | From Sternweis et al Phil Trans R Soc Lond 1992, also matched by Homma et al. k1 = 1.5e-5, now 4.2e-6 k2 = 70/sec; now 40/sec k3 = 17.5/sec; now 10/sec Note that the wording in Sternweis et al is ambiguous re the Km. Also Smrcka et al; Science 251, 15.2.1991, pp804-807 |
| 3 |
Enzyme Activity:
PLC-Gq
Enzyme Molecule:
PLC-Gq | 5 | 75 | 4 | explicit E-S complex | PIP2
| IP3(145)
DAG
|
| | from Smrcka et al, 1991 Science 251: 804-807 |
| 4 |
Enzyme Activity:
PLCb-Ca-Gq
Enzyme Molecule:
PLC-Ca-Gq | 4.99994 | 160 | 4 | explicit E-S complex | PIP2
| IP3(145)
DAG
|
| | Km: Sternweis et al, Phil Trans R Soc Lond 1992 Vmax: Smrcka et al, Science 1991 |
