Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.

Search in:

ALL Accession Pathway Molecule Enzyme Reaction Connected to

Search for

Match

Anything Exact Word Starting With

By

Name Notes Model

Molecule Parameter List for CaMKII-thr286*-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-thr286*-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	1	2	0	1

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
CaMKII_2003	49	Network	Shared_Object_CaMKII_2003,  CaMKII,  CaM,   PP1,  PP2B
Model of regulation of CaMKII by Calcium, including parallel excitatory input from CaM and inhibitory input from PP1 as regulated by Calcineurin and PKA. Cell type: neuronal. Bhalla US. Biophys J. 2004 Aug;87(2):733-44.

CaMKII-thr286*-CaM acting as a Molecule in  CaMKII_2003 Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
CaMKII-thr286*-CaM	CaMKII_2003 Accession No. : 49	CaMKII Pathway No. : 202	0	1000	No
From Hanson and Schulman, the thr286 is responsible for autonomous activation of CaMKII.

CaMKII-thr286*-CaM acting as a Summed Molecule in  CaMKII_2003 Network

Accession Name	Pathway Name	Target	Input
CaMKII_2003 Accession No. : 49	CaMKII Pathway No. : 202	tot_CaM_CaMKII	CaMKII-CaM CaMKII-thr286*-C aM

CaMKII-thr286*-CaM acting as a Substrate for an Enzyme in  CaMKII_2003 Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
PP1-active  / Deph-thr286	CaMKII_2003 Accession No. : 49	Shared_Object_ CaMKII_2003 Pathway No. : 201	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

CaMKII-thr286*-CaM acting as a Product of an Enzyme in  CaMKII_2003 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	CaMKII_2003 Accession No. : 49	CaMKII Pathway No. : 202	113.601	0.5	4	explicit E-S complex	Substrate CaMKII-CaM Product CaMKII-thr286*-C aM
2	tot_autonomous_ CaMKII  / auton_286	CaMKII_2003 Accession No. : 49	CaMKII Pathway No. : 202	174.997	0.5	4	explicit E-S complex	Substrate CaMKII-CaM Product CaMKII-thr286*-C aM

CaMKII-thr286*-CaM acting as a Product in a reaction in  CaMKII_2003 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
CaMK-thr286-bind -CaM	CaMKII_2003 Accession No. : 49	CaMKII Pathway No. : 202	1000.2 (uM^-1 s^-1)	0.1 (s^-1)	Kd(bf) = 0.0001(uM)	-	Substrate CaM-Ca4 CaMKII-thr286 Product CaMKII-thr286*-C aM
Affinity is up 1000X. Time to release is about 20 sec, so the kb is OK at 0.1 This makes Kf around 1.6666e-3