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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

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
AMPAR_CaMKII_ strong_coupling	64	Network	Shared_Object_AMPAR_CaMKII_strong_coupling, CaMKII, CaM, PP1, AMPAR_memb, PP2B, PKA, AC, PP1_PSD, AMPAR
This is a model of tight coupling between the AMPAR trafficking bistability, and the CaMKII autophosphorylation bistability. In this model, the CaMKII activity is self sustaining only when AMPAR is turned on. Further, CaMKII turns on when AMPAR is turned on.

I1* acting as a Molecule in AMPAR_CaMKII_strong_coupling Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
I1*	AMPAR_CaMKII_ strong_coupling Accession No. : 64	PP1 Pathway No. : 274	0	0.09	No
Dephosph is mainly by PP2B
I1*	AMPAR_CaMKII_ strong_coupling Accession No. : 64	PP1_PSD Pathway No. : 279	0	0.01	No
Dephosph is mainly by PP2B

I1* acting as a Substrate for an Enzyme in AMPAR_CaMKII_strong_coupling Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	PP2A / PP2A-dephosph-I1	AMPAR_CaMKII_ strong_coupling Accession No. : 64	Shared_Object_ AMPAR_CaMKII_ strong_coupling Pathway No. : 271	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_CaMKII_ strong_coupling Accession No. : 64	Shared_Object_ AMPAR_CaMKII_ strong_coupling Pathway No. : 271	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_CaMKII_ strong_coupling Accession No. : 64	Shared_Object_ AMPAR_CaMKII_ strong_coupling Pathway No. : 271	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_CaMKII_ strong_coupling Accession No. : 64	Shared_Object_ AMPAR_CaMKII_ strong_coupling Pathway No. : 271	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_CaMKII_ strong_coupling Accession No. : 64	Shared_Object_ AMPAR_CaMKII_ strong_coupling Pathway No. : 271	4.97079	0.34	4	explicit E-S complex	Substrate I1* Product I1
6	CaM_Ca_n-CaNAB / dephosph_ inhib1_PSD	AMPAR_CaMKII_ strong_coupling Accession No. : 64	Shared_Object_ AMPAR_CaMKII_ strong_coupling Pathway No. : 271	4.97071	0.34	4	explicit E-S complex	Substrate I1* Product I1

I1* acting as a Product of an Enzyme in AMPAR_CaMKII_strong_coupling 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_CaMKII_ strong_coupling Accession No. : 64	Shared_Object_ AMPAR_CaMKII_ strong_coupling Pathway No. : 271	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_CaMKII_ strong_coupling Accession No. : 64	Shared_Object_ AMPAR_CaMKII_ strong_coupling Pathway No. : 271	7.50008	9	4	explicit E-S complex	Substrate I1 Product I1*

I1* acting as a Substrate in a reaction in AMPAR_CaMKII_strong_coupling 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_CaMKII_ strong_coupling Accession No. : 64	PP1 Pathway No. : 274	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_CaMKII_ strong_coupling Accession No. : 64	Shared_Object_ AMPAR_CaMKII_ strong_coupling Pathway No. : 271	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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