|
Enter a Search String | | Special character and space not allowed in the query term.
Search string should be at least 2 characters long. |
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 | 0 | 0.09 | No | | Dephosph is mainly by PP2B | | I1* | AMPAR_traff_
model1
Accession No. : 60 | PP1_PSD
Pathway No. : 249 | 0 | 0.01 | No | | Dephosph is mainly by PP2B |
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 | 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 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 | 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 Substrate 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 | Inact-PP1 | AMPAR_traff_
model1
Accession No. : 60 | PP1
Pathway No. : 247 | 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 | AMPAR_traff_
model1
Accession No. : 60 | PP1_PSD
Pathway No. : 249 | 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 |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
|
