| | Molecule Name/
Site Name | Km (uM) | kcat (1/s) | Ratio
(k2/k3) | Enzyme Type | Substrate | Product |
| 1 |
Enzyme Activity:
auton_286
Enzyme Molecule:
tot_autonomous_
CaMKII | 0.00000416667 | 0.5 | 4 | explicit E-S complex | CaMKII-CaM
| CaMKII-thr286*-C
aM
|
| | The autonomous rate has a slightly higher Km than the CaM-bound rate, but Vmax is the same. Hanson and Schulman 1992 Ann Rev Biochem 61:559-601 and Hanson and Schulman 1992 JBC 267(24):17216-17224 |
| 2 |
Enzyme Activity:
auton_305
Enzyme Molecule:
tot_autonomous_
CaMKII | 0.00000416667 | 6 | 4 | explicit E-S complex | CaMKII-thr286
| CaMKII***
|
| | See Hanson and Schulman 1992 JBC 267(24):17216-17224 for afterburst rates of phosphorylation |
| 3 |
Enzyme Activity:
CaM-CaMK-phos
Enzyme Molecule:
tot_CaM_CaMKII | 1.60001 | 0.5 | 4 | explicit E-S complex | IP3_3K
| IP3_3K*
|
| | rates referred from standard CaM-CaMKII phosphorylation rates |
| 4 |
Enzyme Activity:
CaM-CaMK-phos1
Enzyme Molecule:
tot_CaM_CaMKII | 1.59998 | 0.5 | 4 | explicit E-S complex | IP3_3K_CaM
| IP3_3K_CaM*
|
| | rates referred from standard CaM-CaMKII phosphorylation rates |
| 5 |
Enzyme Activity:
CaMK-phos
Enzyme Molecule:
tot_autonomous_
CaMKII | 2.49999 | 0.5 | 4 | explicit E-S complex | IP3_3K
| IP3_3K*
|
| | rates referred from standard CaMKII phosphorylation rates |
| 6 |
Enzyme Activity:
CaMK-phos1
Enzyme Molecule:
tot_autonomous_
CaMKII | 2.49995 | 0.5 | 4 | explicit E-S complex | IP3_3K_CaM
| IP3_3K_CaM*
|
| | rates referred from standard CaMKII phosphorylation rates |
| 7 |
Enzyme Activity:
CaM_act_286
Enzyme Molecule:
tot_CaM_CaMKII | 0.00000270563 | 0.5 | 4 | explicit E-S complex | CaMKII-CaM
| CaMKII-thr286*-C
aM
|
| | See Hanson and Schulman 1992 JBC 267(24):17216-17224 |
| 8 |
Enzyme Activity:
CaM_act_305
Enzyme Molecule:
tot_CaM_CaMKII | 0.00000270563 | 6 | 4 | explicit E-S complex | CaMKII-thr286
| CaMKII***
|
| | Rates from autocamtide phosphorylation, from Hanson and Schulman JBC 267:24 17216-17224 1992. See especially Fig 5. |
| 9 |
Enzyme Activity:
Deph-thr286
Enzyme Molecule:
PP1-active | 5.09907 | 0.35 | 4 | explicit E-S complex | CaMKII-thr286*-C
aM
| CaMKII-CaM
|
| | The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec. |
| 10 |
Enzyme Activity:
Deph-thr286c
Enzyme Molecule:
PP1-active | 5.09907 | 0.35 | 4 | explicit E-S complex | CaMKII***
| CaMK-thr306
|
| | Dephosphorylation tempkin are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec. |
| 11 |
Enzyme Activity:
Deph-thr305
Enzyme Molecule:
PP1-active | 5.09907 | 0.35 | 4 | explicit E-S complex | CaMKII***
| CaMKII-thr286
|
| | Dephosphorylation tempkin are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec. |
| 12 |
Enzyme Activity:
Deph-thr306
Enzyme Molecule:
PP1-active | 5.09907 | 0.35 | 4 | explicit E-S complex | CaMK-thr306
| CaMKII
|
| | Dephosphorylation tempkin are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec. |
| 13 |
Enzyme Activity:
Deph_thr286b
Enzyme Molecule:
PP1-active | 5.09907 | 0.35 | 4 | explicit E-S complex | CaMKII-thr286
| CaMKII
|
| | Rates are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec. |
