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Molecule Parameter List for I1* | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network. The text color of a molecule is highlighted by color. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| I1* participated as | Molecule | Sum total of | Enzyme | Substrate of an enzyme | Product of an enzyme | Substrate in Reaction | Product in Reaction |
| No. of occurrences | 2 | 0 | 0 | 6 | 2 | 2 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
model0 | 59 | Network | Shared_Object_AMPAR_traff_model0, CaMKII, CaM, PP1, PP2B, PP1_PSD, PKA, AC, AMPAR, AMPAR_memb |
| This is model 0 from Hayer and Bhalla, PLoS Comput Biol 2005. It has a bistable model of AMPAR traffick, plus a non-bistable model of CaMKII. This differs from the reference model (model 1) in that model0 lacks degradation and turno ver reactions for AMPAR. | |||
I1* acting as a Molecule in AMPAR_traff_model0 Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| I1* | model0 Accession No. : 59 | PP1 Pathway No. : 237 | 0 | 0.09 | No | |
| Dephosph is mainly by PP2B | ||||||
| I1* | model0 Accession No. : 59 | PP1_PSD Pathway No. : 239 | 0 | 0.01 | No | |
| Dephosph is mainly by PP2B | ||||||
I1* acting as a Substrate for an Enzyme in AMPAR_traff_model0 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | PP2A / | model0 Accession No. : 59 | PP1 Pathway No. : 237 | 15.9999 | 2 | 4.1667 | explicit E-S complex | Substrate I1* Product 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 | ||||||||
| 2 | PP2A / PP2A-dephosph-I1 _ PSD | model0 Accession No. : 59 | PP1 Pathway No. : 237 | 15.9999 | 2 | 4.1667 | explicit E-S complex | Substrate I1* Product 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 | ||||||||
| 3 | CaNAB-Ca4 / inhib1_noCaM | model0 Accession No. : 59 | PP2B Pathway No. : 238 | 4.97079 | 0.034 | 4 | explicit E-S complex | Substrate I1* Product 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 | ||||||||
| 4 | CaNAB-Ca4 / inhib1_noCaM_ PSD | model0 Accession No. : 59 | PP2B Pathway No. : 238 | 4.97071 | 0.034 | 4 | explicit E-S complex | Substrate I1* Product 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 | ||||||||
| 5 | CaM_Ca_n-CaNAB / dephosph_inhib1 | model0 Accession No. : 59 | PP2B Pathway No. : 238 | 4.97079 | 0.34 | 4 | explicit E-S complex | Substrate I1* Product I1 |
| 6 | CaM_Ca_n-CaNAB / inhib1_PSD | model0 Accession No. : 59 | PP2B Pathway No. : 238 | 4.97071 | 0.34 | 4 | explicit E-S complex | Substrate I1* Product I1 |
I1* acting as a Product of an Enzyme in AMPAR_traff_model0 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | PKA-active / PKA-phosph-I1 | model0 Accession No. : 59 | PKA Pathway No. : 240 | 7.50008 | 9 | 4 | explicit E-S complex | Substrate I1 Product 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. | ||||||||
| 2 | PKA-active / PSD | model0 Accession No. : 59 | PKA Pathway No. : 240 | 7.50008 | 9 | 4 | explicit E-S complex | Substrate I1 Product I1* |
I1* acting as a Substrate in a reaction in AMPAR_traff_model0 Network
| Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated. Kd for higher order reaction are not consider. |
| Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | |
| 1 | Inact-PP1 | model0 Accession No. : 59 | PP1 Pathway No. : 237 | 499.981 (uM^-1 s^-1) | 0.1 (s^-1) | Kd(bf) = 0.0002(uM) | - | Substrate I1* PP1-active Product PP1-I1* |
| K inhib = 1nM from Cohen Ann Rev Bioch 1989, 4 nM from Foukes et al Assume 2 nM. kf /kb = 8.333e-4 | ||||||||
| 2 | Inact-PP1 | model0 Accession No. : 59 | PP1_PSD Pathway No. : 239 | 499.98 (uM^-1 s^-1) | 0.1 (s^-1) | Kd(bf) = 0.0002(uM) | - | Substrate I1* PP1-active_PSD Product PP1-I1* |
| K inhib = 1nM from Cohen Ann Rev Bioch 1989, 4 nM from Foukes et al Assume 2 nM. kf /kb = 8.333e-4 | ||||||||
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