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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	1	0	0	3	1	1	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
Ajay_Bhalla_ 2004_PKM_Tuning	76	Network	PKC, Shared_Object_Ajay_Bhalla_2004_PKM_tuning, PLA2, PLCbeta, Gq, MAPK, Ras, EGFR, Sos, PLC_g, CaMKII, CaM, PP1, PP2B, PKA, AC, PKM
This model is taken from the Ajay SM, Bhalla US. Eur J Neurosci. 2004 Nov;20(10):2671-80. This is the reference feedforward model from Figure 8a.

I1* acting as a Molecule in Ajay_Bhalla_2004_PKM_Tuning Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
I1*	Ajay_Bhalla_ 2004_PKM_Tuning Accession No. : 76	PP1 Pathway No. : 324	0.001	1.5	No
Dephosph is mainly by PP2B

I1* acting as a Substrate for an Enzyme in Ajay_Bhalla_2004_PKM_Tuning Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	CaM(Ca)n-CaNAB / dephosph_inhib1	Ajay_Bhalla_ 2004_PKM_Tuning Accession No. : 76	Shared_Object_ Ajay_Bhalla_ 2004_PKM_tuning Pathway No. : 312	4.97076	0.34	4	explicit E-S complex	Substrate I1* Product I1

2	PP2A / PP2A-dephosph-I1	Ajay_Bhalla_ 2004_PKM_Tuning Accession No. : 76	Shared_Object_ Ajay_Bhalla_ 2004_PKM_tuning Pathway No. : 312	7.82828	6	4.16667	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	Ajay_Bhalla_ 2004_PKM_Tuning Accession No. : 76	Shared_Object_ Ajay_Bhalla_ 2004_PKM_tuning Pathway No. : 312	4.97076	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

I1* acting as a Product of an Enzyme in Ajay_Bhalla_2004_PKM_Tuning Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
PKA-active / PKA-phosph-I1	Ajay_Bhalla_ 2004_PKM_Tuning Accession No. : 76	Shared_Object_ Ajay_Bhalla_ 2004_PKM_tuning Pathway No. : 312	7.49996	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.

I1* acting as a Substrate in a reaction in Ajay_Bhalla_2004_PKM_Tuning 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
Inact-PP1	Ajay_Bhalla_ 2004_PKM_Tuning Accession No. : 76	PP1 Pathway No. : 324	499.977 (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

Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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