| Molecule Name/ Site Name | Km (uM) | kcat (1/s) | Ratio (k2/k3) | Enzyme Type | Substrate | Product |
1 |
Enzyme Activity: auton-286-PSD
Enzyme Molecule: tot-auto-PSD | 500.002 | 0.5 | 4 | explicit E-S complex | CaMKII-CaM-PSD
| CaMKII-thr286-Ca M-PSD
|
2 |
Enzyme Activity: auton-305-PSD
Enzyme Molecule: tot-auto-PSD | 500 | 6 | 4 | explicit E-S complex | CaMKII-thr286-PS D
| CaMKII***-PSD
|
3 |
Enzyme Activity: auton-autoph
Enzyme Molecule: tot-auto-PSD | 500.005 | 2 | 4 | explicit E-S complex | CaMKII-PSD
| CaMKII-thr286-PS D
|
4 |
Enzyme Activity: CaM-act-286-PSD
Enzyme Molecule: tot-CaM-CaMKII-P SD | 319.996 | 0.5 | 4 | explicit E-S complex | CaMKII-CaM-PSD
| CaMKII-thr286-Ca M-PSD
|
5 |
Enzyme Activity: CaM-act-305-PSD
Enzyme Molecule: tot-CaM-CaMKII-P SD | 320 | 6 | 4 | explicit E-S complex | CaMKII-thr286-PS D
| CaMKII***-PSD
|
6 |
Enzyme Activity: CaM_act_autoph
Enzyme Molecule: tot-CaM-CaMKII-P SD | 320.002 | 2 | 4 | explicit E-S complex | CaMKII-PSD
| CaMKII-thr286-PS D
|
7 |
Enzyme Activity: Deph-thr286
Enzyme Molecule: PP1-active | 5.09905 | 2.5 | 4 | explicit E-S complex | CaMKII-thr286*-C aM
| CaMKII-CaM
|
8 |
Enzyme Activity: Deph-thr286
Enzyme Molecule: PP1-active_PSD | 2.00001 | 0.2 | 4 | explicit E-S complex | CaMKII-thr286-Ca M-PSD
| CaMKII-CaM-PSD
|
9 |
Enzyme Activity: Deph-thr286b
Enzyme Molecule: PP1-active | 5.09905 | 2.5 | 4 | explicit E-S complex | CaMKII-thr286
| CaMKII
|
10 |
Enzyme Activity: Deph-thr286b
Enzyme Molecule: PP1-active_PSD | 2.00001 | 0.2 | 4 | explicit E-S complex | CaMKII-thr286-PS D
| CaMKII-PSD
|
11 |
Enzyme Activity: Deph-thr286c
Enzyme Molecule: PP1-active | 5.09905 | 2.5 | 4 | explicit E-S complex | CaMKII***
| CaMK-thr305
|
12 |
Enzyme Activity: Deph-thr286c
Enzyme Molecule: PP1-active_PSD | 2.00001 | 0.2 | 4 | explicit E-S complex | CaMKII***-PSD
| CaMKII-thr305-PS D
|
13 |
Enzyme Activity: Deph-thr305
Enzyme Molecule: PP1-active | 5.09905 | 2.5 | 4 | explicit E-S complex | CaMKII***
| CaMKII-thr286
|
14 |
Enzyme Activity: Deph-thr305
Enzyme Molecule: PP1-active_PSD | 2.00001 | 0.2 | 4 | explicit E-S complex | CaMKII***-PSD
| CaMKII-thr286-PS D
|
15 |
Enzyme Activity: Deph-thr305a
Enzyme Molecule: PP1-active | 5.09905 | 2.5 | 4 | explicit E-S complex | CaMK-thr305
| CaMKII
|
16 |
Enzyme Activity: Deph-thr305a
Enzyme Molecule: PP1-active_PSD | 2.00001 | 0.2 | 4 | explicit E-S complex | CaMKII-thr305-PS D
| CaMKII-PSD
|
17 |
Enzyme Activity: dephosph-PP1-I*
Enzyme Molecule: CaM_Ca_n-CaNAB | 4.97079 | 0.34 | 4 | explicit E-S complex | PP1-I1*
| PP1-I1
|
18 |
Enzyme Activity:
dephosph-PP1-I*_ PSD
Enzyme Molecule: CaM_Ca_n-CaNAB | 4.97071 | 0.34 | 4 | explicit E-S complex | PP1-I1*
| PP1-I1
|
19 |
Enzyme Activity: dephosph_inhib1
Enzyme Molecule: CaM_Ca_n-CaNAB | 4.97079 | 0.34 | 4 | explicit E-S complex | I1*
| I1
|
20 |
Enzyme Activity: dephosph_ inhib1_noCaM
Enzyme Molecule: CaNAB-Ca4 | 4.97079 | 0.034 | 4 | explicit E-S complex | I1*
| I1
|
| The rates here are so slow I do not know if we should even bother with this enz reacn. These numbers are from Liu and Storm. Other refs suggest that the Km stays the same but the Vmax goes to 10% of the CaM stim levels. Prev: k1=2.2e-9, k2 = 0.0052, k3 = 0.0013 New : k1=5.7e-8, k2=.136, k3=.034 |
21 |
Enzyme Activity: dephosph_ inhib1_noCaM_ PSD
Enzyme Molecule: CaNAB-Ca4 | 4.97071 | 0.034 | 4 | explicit E-S complex | I1*
| I1
|
| The rates here are so slow I do not know if we should even bother with this enz reacn. These numbers are from Liu and Storm. Other refs suggest that the Km stays the same but the Vmax goes to 10% of the CaM stim levels. Prev: k1=2.2e-9, k2 = 0.0052, k3 = 0.0013 New : k1=5.7e-8, k2=.136, k3=.034 |
22 |
Enzyme Activity: dephosph_ inhib1_PSD
Enzyme Molecule: CaM_Ca_n-CaNAB | 4.97071 | 0.34 | 4 | explicit E-S complex | I1*
| I1
|
23 |
Enzyme Activity: phosph-AC2
Enzyme Molecule: PKC-active | 33.3337 | 4 | 4 | explicit E-S complex | AC2
| AC2*
|
| Phorbol esters have little effect on AC1 or on the Gs-stimulation of AC2. So in this model we are only dealing with the increase in basal activation of AC2 induced by PKC k1 = 1.66e-6 k2 = 16 k3 =4 |
24 |
Enzyme Activity: phosph-PDE
Enzyme Molecule: PKA-active | 7.50008 | 9 | 4 | explicit E-S complex | cAMP-PDE
| cAMP-PDE*
|
| Same rates as PKA-phosph-I1 |
25 |
Enzyme Activity: PKA-phosph-I1
Enzyme Molecule: PKA-active | 7.50008 | 9 | 4 | explicit E-S complex | I1
| I1*
|
| #s from Bramson et al CRC crit rev Biochem 15:2 93-124. They have a huge list of peptide substrates and I have chosen high-ish rates. These consts give too much PKA activity, so lower Vmax 1/3. Now, k1 = 3e-5, k2 = 36, k3 = 9 (still pretty fast). Also lower Km 1/3 so k1 = 1e-5 Cohen et al FEBS Lett 76:182-86 1977 say rate =30% PKA act on phosphokinase beta. |
26 |
Enzyme Activity: PKA-phosph-I1_ PSD
Enzyme Molecule: PKA-active | 7.50008 | 9 | 4 | explicit E-S complex | I1
| I1*
|
27 |
Enzyme Activity: PP2A-dephosph-I1
Enzyme Molecule: PP2A | 15.9999 | 2 | 4.1667 | explicit E-S complex | I1*
| I1
|
| PP2A does most of the dephosph of I1 at basal Ca levels. See the review by Cohen in Ann Rev Biochem 1989. For now, lets halve Km. k1 was 3.3e-6, now 6.6e-6 |
28 |
Enzyme Activity:
PP2A-dephosph-I1 _ PSD
Enzyme Molecule: PP2A | 15.9999 | 2 | 4.1667 | explicit E-S complex | I1*
| I1
|
| PP2A does most of the dephosph of I1 at basal Ca levels. See the review by Cohen in Ann Rev Biochem 1989. For now, lets halve Km. k1 was 3.3e-6, now 6.6e-6 |
29 |
Enzyme Activity: PP2A-dephosph-PP 1-I*
Enzyme Molecule: PP2A | 15.9999 | 2 | 4.1667 | explicit E-S complex | PP1-I1*
| PP1-I1
|
| k1 changed from 3.3e-6 to 6.6e-6 |
30 |
Enzyme Activity:
PP2A-dephosph-PP 1-I*_ PSD
Enzyme Molecule: PP2A | 15.9999 | 2 | 4.1667 | explicit E-S complex | PP1-I1*
| PP1-I1
|
| k1 changed from 3.3e-6 to 6.6e-6 |