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Molecule Parameter List for CaMKII-CaM

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-CaM 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	1	0	1

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-CaM acting as a Molecule in  Synaptic_Network Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
CaMKII-CaM	Synaptic_ Network Accession No. : 16	CaMKII Pathway No. : 80	0	1000	No
This is the regular, CaM-activated form of CaMKII. See the review Hanson and Schulman 1992 Ann. Rev. Biochem 60:559-601

CaMKII-CaM 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_CaM_CaMKII	CaMKII-CaM CaMKII-thr286*-C aM
This pool sums the levels of the CaM-bound forms of CaMKII: CaMKII-CaM + CaMKII-thr286*-CaM. Although their phosphorylation states are different, the level of activity is about the same so it makes sense to sum the levels. Hanson et al 1994 Neuron 12:943-956

CaMKII-CaM 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	tot_CaM_CaMKII  / CaM_act_286	Synaptic_ Network Accession No. : 16	CaMKII Pathway No. : 80	0.00000270563	0.5	4	explicit E-S complex	Substrate CaMKII-CaM Product CaMKII-thr286*-C aM
	See Hanson and Schulman 1992 JBC 267(24):17216-17224
2	tot_autonomous_ CaMKII  / auton_286	Synaptic_ Network Accession No. : 16	CaMKII Pathway No. : 80	0.00000416667	0.5	4	explicit E-S complex	Substrate CaMKII-CaM Product CaMKII-thr286*-C aM
	The autonomous rate has a slightly higher Km than the CaM-bound rate, but Vmax is the same. Hanson and Schulman 1992 Ann Rev Biochem 61:559-601 and Hanson and Schulman 1992 JBC 267(24):17216-17224

CaMKII-CaM 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
PP1-active  / Deph-thr286	Synaptic_ Network Accession No. : 16	Shared_Object_ Synaptic_ Network Pathway No. : 70	5.09907	0.35	4	explicit E-S complex	Substrate CaMKII-thr286*-C aM Product CaMKII-CaM
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-CaM acting as a Product in a reaction in  Synaptic_Network 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
CaMKII-bind-CaM	Synaptic_ Network Accession No. : 16	CaMKII Pathway No. : 80	49.9998 (uM^-1 s^-1)	5 (s^-1)	Kd(bf) = 0.1(uM)	-	Substrate CaM-Ca4 CaMKII Product CaMKII-CaM
This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kd = 0.1 uM. Rate is fast (see Hanson et al Neuron 12 943-956 1994) Hanson and Schulman 1992 AnnRev Biochem 61:559-601 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol.