| | Molecule Name/
Site Name | Km (uM) | kcat (1/s) | Ratio
(k2/k3) | Enzyme Type | Substrate | Product |
| 1 |
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 |
| 2 |
Enzyme Activity:
Deph-thr286c
Enzyme Molecule:
PP1-active | 5.09907 | 0.35 | 4 | explicit E-S complex | CaMKII***
| CaMK-thr306
|
| 3 |
Enzyme Activity:
Deph-thr305
Enzyme Molecule:
PP1-active | 5.09907 | 0.35 | 4 | explicit E-S complex | CaMKII***
| CaMKII-thr286
|
| 4 |
Enzyme Activity:
Deph-thr306
Enzyme Molecule:
PP1-active | 5.09907 | 0.35 | 4 | explicit E-S complex | CaMK-thr306
| CaMKII
|
| | See Cohen et al |
| 5 |
Enzyme Activity:
dephosph-PP1-I*
Enzyme Molecule:
CaM(Ca)n-CaNAB | 4.97076 | 0.34 | 4 | explicit E-S complex | PP1-I1*
| PP1-I1
|
| 6 |
Enzyme Activity:
dephosph_inhib1
Enzyme Molecule:
CaM(Ca)n-CaNAB | 4.97076 | 0.34 | 4 | explicit E-S complex | I1*
| I1
|
| 7 |
Enzyme Activity:
dephosph_
inhib1_noCaM
Enzyme Molecule:
CaNAB-Ca4 | 4.97076 | 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 |
| 8 |
Enzyme Activity:
dephosph_
neurogranin
Enzyme Molecule:
CaM(Ca)n-CaNAB | 10.012 | 0.67 | 3.98507 | explicit E-S complex | neurogranin*
| neurogranin
|
| | From Seki et al ABB 316(2):673-679 |
| 9 |
Enzyme Activity:
Deph_thr286b
Enzyme Molecule:
PP1-active | 5.09907 | 0.35 | 4 | explicit E-S complex | CaMKII-thr286
| CaMKII
|
| 10 |
Enzyme Activity:
PKA-phosph-I1
Enzyme Molecule:
PKA-active | 7.5 | 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. |
| 11 |
Enzyme Activity:
PKC-phosph-neuro
granin
Enzyme Molecule:
PKC-active | 28.6275 | 0.58 | 4.03448 | explicit E-S complex | neurogranin
| neurogranin*
|
| | Rates from Huang et al ABB 305:2 570-580 1993 |
| 12 |
Enzyme Activity:
PKC-phosph-ng-Ca
M
Enzyme Molecule:
PKC-active | 28.5948 | 0.35 | 4 | explicit E-S complex | neurogranin-CaM
| CaM
neurogranin*
|
| | Rates are 60% those of PKC-phosph-neurogranin. See Huang et al ABB 305:2 570-580 1993 |
| 13 |
Enzyme Activity:
PP2A-dephosph-I1
Enzyme Molecule:
PP2A | 7.82828 | 6 | 4.16667 | 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 |
| 14 |
Enzyme Activity:
PP2A-dephosph-PP
1-I*
Enzyme Molecule:
PP2A | 7.82828 | 6 | 4.16667 | explicit E-S complex | PP1-I1*
| PP1-I1
|
| | k1 changed from 3.3e-6 to 6.6e-6 |
