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Molecule Parameter List for PKA-active

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

PKA-active 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	3	0	0	1	2

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
CaMKII_model3	63	Network	Shared_Object_CaMKII_model3,  CaMKII,  CaM,   PP1,  PP2B,  PP1_PSD,   AC,  PKA
This is the complete model of CaMKII bistability, model 3. It exhibits bistability in CaMKII activation due to autophosphorylation at the PSD and local saturation of PP1. This version of model 3 includes PKA regulatory input. This has little effect on the deterministic calculations, but the PKA pathway introduces a lot of noise which causes a difference in stochastic runs.

PKA-active acting as a Molecule in  CaMKII_model3 Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
PKA-active	CaMKII_model3 Accession No. : 63	Shared_Object_ CaMKII_model3 Pathway No. : 263	0	0.09	No

PKA-active acting as an Enzyme in  CaMKII_model3 Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	PKA-active / PKA-phosph-I1	CaMKII_model3 Accession No. : 63	Shared_Object_ CaMKII_model3 Pathway No. : 263	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	CaMKII_model3 Accession No. : 63	Shared_Object_ CaMKII_model3 Pathway No. : 263	7.50008	9	4	explicit E-S complex	Substrate I1 Product I1*
3	PKA-active / phosph-PDE	CaMKII_model3 Accession No. : 63	Shared_Object_ CaMKII_model3 Pathway No. : 263	7.50008	9	4	explicit E-S complex	Substrate cAMP-PDE Product cAMP-PDE*
	Same rates as PKA-phosph-I1

PKA-active acting as a Substrate in a reaction in  CaMKII_model3 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
inhib-PKA	CaMKII_model3 Accession No. : 63	PKA Pathway No. : 270	59.9994 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 0.0167(uM)	-	Substrate PKA-active PKA-inhibitor Product inhibited-PKA
This has to be set to zero for matching the expts in vitro. In vivo we need to consider the inhibition though. kf = 1e-5 kb = 1

PKA-active acting as a Product in a reaction in  CaMKII_model3 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	Release-C1	CaMKII_model3 Accession No. : 63	PKA Pathway No. : 270	60 (s^-1)	17.9998 (uM^-1 s^-1)	Kd(cb) = 0.3(uM)	-	Substrate R2C2-cAMP4 Product PKA-active R2C-cAMP4
	This has to be fast, as the activation of PKA by cAMP is also fast. kf was 10
2	Release-C2	CaMKII_model3 Accession No. : 63	PKA Pathway No. : 270	60 (s^-1)	17.9998 (uM^-1 s^-1)	Kd(cb) = 0.3(uM)	-	Substrate R2C-cAMP4 Product PKA-active R2-cAMP4