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Enzyme Molecule /
Enzyme Activity | Accession Name / Accession No. | Pathway Name / Pathway No. | Km (uM) | kcat (s^-1) | Ratio (k2/k3) | Enzyme Type | Reagents |
1 | PP1-active / Deph-thr286 | fig3_CaMKII
Accession No. 2 | Shared_Object_ fig3_CaMKII Pathway No. 12 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII-thr286*-C aM Product : CaMKII-CaM
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2 | PP1-active / Deph-thr305 | fig3_CaMKII
Accession No. 2 | Shared_Object_ fig3_CaMKII Pathway No. 12 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII*** Product : CaMKII-thr286
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3 | PP1-active / Deph-thr286c | fig3_CaMKII
Accession No. 2 | Shared_Object_ fig3_CaMKII Pathway No. 12 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII*** Product : CaMK-thr306
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4 | PP1-active / Deph_thr286b | fig3_CaMKII
Accession No. 2 | Shared_Object_ fig3_CaMKII Pathway No. 12 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII-thr286 Product : CaMKII
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5 | tot_CaM_CaMKII / CaM_act_305 | fig3_CaMKII
Accession No. 2 | CaMKII
Pathway No. 13 | 0.00000270563 | 6 | 4 | explicit E-S complex | Substrate: CaMKII-thr286 Product : CaMKII***
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6 | tot_CaM_CaMKII / CaM_act_286 | fig3_CaMKII
Accession No. 2 | CaMKII
Pathway No. 13 | 0.00000270563 | 0.5 | 4 | explicit E-S complex | Substrate: CaMKII-CaM Product : CaMKII-thr286*-C aM
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7 | tot_autonomous_ CaMKII / auton_305 | fig3_CaMKII
Accession No. 2 | CaMKII
Pathway No. 13 | 0.00000416667 | 6 | 4 | explicit E-S complex | Substrate: CaMKII-thr286 Product : CaMKII***
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8 | tot_autonomous_ CaMKII / auton_286 | fig3_CaMKII
Accession No. 2 | CaMKII
Pathway No. 13 | 0.00000416667 | 0.5 | 4 | explicit E-S complex | Substrate: CaMKII-CaM Product : CaMKII-thr286*-C aM
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9 | PP1-active / Deph-thr286 | fig4_synapse
Accession No. 3 | Shared_Object_ fig4_synapse Pathway No. 19 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII-thr286*-C aM Product : CaMKII-CaM
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10 | PP1-active / Deph-thr305 | fig4_synapse
Accession No. 3 | Shared_Object_ fig4_synapse Pathway No. 19 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII*** Product : CaMKII-thr286
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11 | PP1-active / Deph-thr286c | fig4_synapse
Accession No. 3 | Shared_Object_ fig4_synapse Pathway No. 19 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII*** Product : CaMK-thr306
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12 | PP1-active / Deph_thr286b | fig4_synapse
Accession No. 3 | Shared_Object_ fig4_synapse Pathway No. 19 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII-thr286 Product : CaMKII
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13 | tot_CaM_CaMKII / CaM_act_305 | fig4_synapse
Accession No. 3 | CaMKII
Pathway No. 26 | 0.00000270563 | 6 | 4 | explicit E-S complex | Substrate: CaMKII-thr286 Product : CaMKII***
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14 | tot_CaM_CaMKII / CaM_act_286 | fig4_synapse
Accession No. 3 | CaMKII
Pathway No. 26 | 0.00000270563 | 0.5 | 4 | explicit E-S complex | Substrate: CaMKII-CaM Product : CaMKII-thr286*-C aM
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15 | tot_autonomous_ CaMKII / auton_305 | fig4_synapse
Accession No. 3 | CaMKII
Pathway No. 26 | 0.00000416667 | 6 | 4 | explicit E-S complex | Substrate: CaMKII-thr286 Product : CaMKII***
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16 | tot_autonomous_ CaMKII / auton_286 | fig4_synapse
Accession No. 3 | CaMKII
Pathway No. 26 | 0.00000416667 | 0.5 | 4 | explicit E-S complex | Substrate: CaMKII-CaM Product : CaMKII-thr286*-C aM
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17 | PP1-active / Deph-thr286 | Synaptic_ Network Accession No. 16 | Shared_Object_ Synaptic_ Network Pathway No. 70 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII-thr286*-C aM Product : CaMKII-CaM
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| 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. |
18 | PP1-active / Deph-thr305 | Synaptic_ Network Accession No. 16 | Shared_Object_ Synaptic_ Network Pathway No. 70 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII*** Product : CaMKII-thr286
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| Dephosphorylation kinetics 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. |
19 | PP1-active / Deph-thr286c | Synaptic_ Network Accession No. 16 | Shared_Object_ Synaptic_ Network Pathway No. 70 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII*** Product : CaMK-thr306
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| Dephosphorylation kinetics 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. |
20 | PP1-active / Deph_thr286b | Synaptic_ Network Accession No. 16 | Shared_Object_ Synaptic_ Network Pathway No. 70 | 5.09907 | 0.35 | 4 | explicit E-S complex | Substrate: CaMKII-thr286 Product : CaMKII
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| 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. |