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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. | | Statistics |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | AMPAR_traff_
model1 | 60 | Network |
Shared_Object_AMPAR_traff_model1, CaMKII, CaM,
PP1, PP2B, PP1_PSD,
PKA, AC, AMPAR,
AMPAR_memb | | This is the basic model of AMPAR trafficking bistability. It is based on Hayer and Bhalla, PLoS Comput. Biol. 2005. It includes the degradation and turnover of AMPARs. The CaMKII portion of the model is not bistable. |
I1 acting as a Molecule in AMPAR_traff_model1 Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | I1 | AMPAR_traff_
model1
Accession No. : 60 | PP1
Pathway No. : 247 | 1.8 | 0.09 | No | | I1 is a 'mixed' inhibitor, but at high enz concs it looks like a non-compet inhibitor (Foulkes et al Eur J Biochem 132 309-313 9183). We treat it as non-compet, so it just turns the enz off without interacting with the binding site. Cohen et al ann rev bioch refer to results where conc is 1.5 to 1.8 uM. In order to get complete inhib of PP1, which is at 1.8 uM, we need >= 1.8 uM. | | I1 | AMPAR_traff_
model1
Accession No. : 60 | PP1_PSD
Pathway No. : 249 | 4 | 0.01 | No | | I1 is a 'mixed' inhibitor, but at high enz concs it looks like a non-compet inhibitor (Foulkes et al Eur J Biochem 132 309-313 9183). We treat it as non-compet, so it just turns the enz off without interacting with the binding site. Cohen et al ann rev bioch refer to results where conc is 1.5 to 1.8 uM. In order to get complete inhib of PP1, which is at 1.8 uM, we need >= 1.8 uM. |
I1 acting as a Substrate for an Enzyme in AMPAR_traff_model1 Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | PKA-active /
PKA-phosph-I1 | AMPAR_traff_
model1
Accession No. : 60 | PKA
Pathway No. : 250 | 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 /
PKA-phosph-I1_
PSD
| AMPAR_traff_
model1
Accession No. : 60 | PKA
Pathway No. : 250 | 7.50008 | 9 | 4 | explicit E-S complex | Substrate
I1
Product
I1*
|
I1 acting as a Product of an Enzyme in AMPAR_traff_model1 Network
| | Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | | 1 | PP2A /
PP2A-dephosph-I1
| AMPAR_traff_
model1
Accession No. : 60 | PP1
Pathway No. : 247 | 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
| AMPAR_traff_
model1
Accession No. : 60 | PP1
Pathway No. : 247 | 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 /
dephosph_
inhib1_noCaM
| AMPAR_traff_
model1
Accession No. : 60 | PP2B
Pathway No. : 248 | 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 /
dephosph_
inhib1_noCaM_
PSD
| AMPAR_traff_
model1
Accession No. : 60 | PP2B
Pathway No. : 248 | 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 | AMPAR_traff_
model1
Accession No. : 60 | PP2B
Pathway No. : 248 | 4.97079 | 0.34 | 4 | explicit E-S complex | Substrate
I1*
Product
I1
| | 6 | CaM_Ca_n-CaNAB /
dephosph_
inhib1_PSD
| AMPAR_traff_
model1
Accession No. : 60 | PP2B
Pathway No. : 248 | 4.97071 | 0.34 | 4 | explicit E-S complex | Substrate
I1*
Product
I1
|
I1 acting as a Product in a reaction in AMPAR_traff_model1 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 | dissoc-PP1-I1 | AMPAR_traff_
model1
Accession No. : 60 | PP1
Pathway No. : 247 | 1
(s^-1) | 0
(uM^-1 s^-1) | - | - | Substrate
PP1-I1
Product
I1
PP1-active
| | | Let us assume that the equil in this case is very far over to the right. This is probably safe. | | 2 | dissoc-PP1-I1 | AMPAR_traff_
model1
Accession No. : 60 | PP1_PSD
Pathway No. : 249 | 1
(s^-1) | 0
(uM^-1 s^-1) | - | - | Substrate
PP1-I1
Product
I1
PP1-active_PSD
| | | Let us assume that the equil in this case is very far over to the right. This is probably safe. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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