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Molecule Parameter List for CaMKII***

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

CaMKII*** 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	1	0	2	2	0	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
Synaptic_ Network	16	Network	Shared_Object_Synaptic_Network,  PKC,  PLA2,   PLCbeta,  Gq,  MAPK,   Ras,  EGFR,  Sos,   PLC_g,  CaMKII,  CaM,   PP1,  PP2B,  PKA,   AC,  CaRegulation
This model is an annotated version of the synaptic signaling network. The primary reference is Bhalla US and Iyengar R. Science (1999) 283(5400):381-7 but several of the model pathways have been updated. Bhalla US Biophys J. 2002 Aug;83(2):740-52 Bhalla US J Comput Neurosci. 2002 Jul-Aug;13(1):49-62

CaMKII*** acting as a Molecule in  Synaptic_Network Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
CaMKII***	Synaptic_ Network Accession No. : 16	CaMKII Pathway No. : 80	0	1000	No
From Hanson and Schulman, the CaMKII does a lot of autophosphorylation just after the CaM is released. This prevents further CaM binding and renders the enzyme quite independent of Ca.

CaMKII*** acting as a Summed Molecule in  Synaptic_Network Network

Accession Name	Pathway Name	Target	Input
Synaptic_ Network Accession No. : 16	CaMKII Pathway No. : 80	tot_autonomous_CaMKII	CaMKII-thr286 CaMKII***
This is the sum total of the various CaM-independent forms of the kinase. There are actually several possible states here, but I only consider the forms thr-286 phosphorylated form and the doubly/triply phosphorylated form including the thr305/306, represented here as CaMKII***

CaMKII*** acting as a Substrate for an Enzyme in  Synaptic_Network Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	PP1-active  / Deph-thr305	Synaptic_ Network Accession No. : 16	Shared_Object_ Synaptic_ Network Pathway No. : 70	5.09907	0.35	4	explicit E-S complex	Substrate CaMKII*** Product CaMKII-thr286
	Dephosphorylation kinetics are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec.
2	PP1-active  / Deph-thr286c	Synaptic_ Network Accession No. : 16	Shared_Object_ Synaptic_ Network Pathway No. : 70	5.09907	0.35	4	explicit E-S complex	Substrate CaMKII*** Product CaMK-thr306
	Dephosphorylation kinetics are assumed to be the same for all phosphorylation sites on CaMKII. The rates are from Stralfors et al Eur J Biochem 149 295-303 giving Vmax = 5.7 umol/min giving k3 = 3.5/sec and k2 = 14. Foulkes et al Eur J Biochem 132 309-313 1983 give Km = 5.1 uM so k1 becomes 5.72e-6 Simonelli 1984 (Grad Thesis, CUNY) showed that other substrates are about 1/10 rate of phosphorylase a, so we reduce k1,k2,k3 by 10 to 5.72e-7, 1.4, 0.35. This gives the final Km of 5.1, and Vmax of 0.35/sec.

CaMKII*** acting as a Product of an Enzyme in  Synaptic_Network Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	tot_CaM_CaMKII  / CaM_act_305	Synaptic_ Network Accession No. : 16	CaMKII Pathway No. : 80	0.00000270563	6	4	explicit E-S complex	Substrate CaMKII-thr286 Product CaMKII***
	Rates from autocamtide phosphorylation, from Hanson and Schulman JBC 267:24 17216-17224 1992. See especially Fig 5.
2	tot_autonomous_ CaMKII  / auton_305	Synaptic_ Network Accession No. : 16	CaMKII Pathway No. : 80	0.00000416667	6	4	explicit E-S complex	Substrate CaMKII-thr286 Product CaMKII***
	See Hanson and Schulman 1992 JBC 267(24):17216-17224 for afterburst rates of phosphorylation