| | Molecule Name/
Site Name | Km (uM) | kcat (1/s) | Ratio
(k2/k3) | Enzyme Type | Substrate | Product |
| 1 |
Enzyme Activity:
Ca.PLCbeta
Enzyme Molecule:
Ca.PLCbeta | 10 | 7 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | PIP2
| DAG
IP3
|
| | 3 Nov 2001 Sternweis et al Phil Trans Soc R Lond B Biol Sci 1992 Apr 29; 336(1276);35-41;discussion 41-2. The Km and Vmax values according to Sternweis et al. The Km is fixed to 10uM since there is absence of Gq and so is the Vmax values which is fixed at 7uM since the Km obtained varies between 5 and 20uM and Vmax between 7 and 23umol/min/mg depending on the presence and absence of Gq. |
| 2 |
Enzyme Activity:
Gq.Ca.PLCbeta
Enzyme Molecule:
Gq.Ca.PLCbeta | 10 | 23 | 4 | explicit E-S complex | PIP2
| DAG
IP3
|
| | 3 Nov 2001 The Km and Vmax values are fixed accordingly from Sternweis et al Phil Trans R Soc Lond B Bio Sci 1992 Apr 29;336(1276):35-41;discussion 41-2 and Smrcka et al Science 251 804-807 1991 where Km varied between 5 and 20uM and Vmax between 7 and 23 umol/min/mg depending on the presenece and absence of Gq. |
| 3 |
Enzyme Activity:
PA.Ca.PLCbeta
Enzyme Molecule:
PA.Ca.PLCbeta | 10 | 38 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | PIP2
| DAG
IP3
|
| | 3 Nov 2001 The Km and Vmax were fixed relatively to the Km and Vmax values of Ca.PLCbeta and Gq.Ca.PLCbeta which were obtained from the works of Sternweis et al and Smrcka et al where the Km varied between 5 and 20uM and Vmax between 7 and 23 umol/min/mg depending on the presence and absence of Gq. |
