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Molecule Parameter List for tot_autonomous_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

tot_autonomous_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	4	0	0	0	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
NonOsc_Ca_ IP3metabolism	31	Network	MIPP,  CaMKII,  CaM,   PKC,  IP3-3K,  CaRegulation,   Gq,  PLCbeta,  134_dephos,   145_dephos,  IP4-system,  IHP-system,   1345_dephos
This network models detailed metabolism of Ins(145)P3, integrated with GPCR mediated PLCbeta activation and Ca release by the InsP3 receptor in the neuron. It is similar to the NonOsc_Ca_IP3metab model (accession 23) except that some enzymes have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. These modified enzymes belong to the groups: IP4-system, IP3-3K, 145_dephos and 134_dephos. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316.

tot_autonomous_CaMKII acting as a Molecule in  NonOsc_Ca_IP3metabolism Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
tot_autonomous_CaMKII	NonOsc_Ca_ IP3metabolism Accession No. : 31	CaMKII Pathway No. : 145	0	1000	No
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***

tot_autonomous_CaMKII acting as a Summed Molecule in  NonOsc_Ca_IP3metabolism Network

Accession Name	Pathway Name	Target	Input
NonOsc_Ca_ IP3metabolism Accession No. : 31	CaMKII Pathway No. : 145	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***

tot_autonomous_CaMKII acting as an Enzyme in  NonOsc_Ca_IP3metabolism Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	tot_autonomous_ CaMKII / auton_305	NonOsc_Ca_ IP3metabolism Accession No. : 31	CaMKII Pathway No. : 145	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
2	tot_autonomous_ CaMKII / auton_286	NonOsc_Ca_ IP3metabolism Accession No. : 31	CaMKII Pathway No. : 145	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
3	tot_autonomous_ CaMKII / CaMK-phos	NonOsc_Ca_ IP3metabolism Accession No. : 31	CaMKII Pathway No. : 145	2.49999	0.5	4	explicit E-S complex	Substrate IP3_3K Product IP3_3K*
	rates referred from standard CaMKII phosphorylation rates
4	tot_autonomous_ CaMKII / CaMK-phos1	NonOsc_Ca_ IP3metabolism Accession No. : 31	CaMKII Pathway No. : 145	2.49995	0.5	4	explicit E-S complex	Substrate IP3_3K_CaM Product IP3_3K_CaM*
	rates referred from standard CaMKII phosphorylation rates