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Enzyme List for pathway CaMKII (Pathway Number 145) in Accession NonOsc_Ca_IP3metabolism (Accession Number 31)

Entries are grouped according to Pathway Number and they are alternately color coded using

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	Enzyme Molecule / Enzyme Activity	Pathway Name / Pathway No.	Km (uM)	kcat (s^-1)	Ratio (k2/k3)	Enzyme Type	Reagents
1	tot_CaM_CaMKII / CaM_act_305	CaMKII Pathway No. 145	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_CaM_CaMKII / CaM_act_286	CaMKII Pathway No. 145	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
3	tot_CaM_CaMKII / CaM-CaMK-phos	CaMKII Pathway No. 145	1.60001	0.5	4	explicit E-S complex	Substrate: IP3_3K Product : IP3_3K*
	rates referred from standard CaM-CaMKII phosphorylation rates
4	tot_CaM_CaMKII / CaM-CaMK-phos1	CaMKII Pathway No. 145	1.59998	0.5	4	explicit E-S complex	Substrate: IP3_3K_CaM Product : IP3_3K_CaM*
	rates referred from standard CaM-CaMKII phosphorylation rates
5	tot_autonomous_ CaMKII / auton_305	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
6	tot_autonomous_ CaMKII / auton_286	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
7	tot_autonomous_ CaMKII / CaMK-phos	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
8	tot_autonomous_ CaMKII / CaMK-phos1	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
9	PP1-active / Deph-thr286	CaMKII Pathway No. 145	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.
10	PP1-active / Deph-thr305	CaMKII Pathway No. 145	5.09907	0.35	4	explicit E-S complex	Substrate: CaMKII* Product :** CaMKII-thr286
	Dephosphorylation tempkin 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.
11	PP1-active / Deph-thr306	CaMKII Pathway No. 145	5.09907	0.35	4	explicit E-S complex	Substrate: CaMK-thr306 Product : CaMKII
	Dephosphorylation tempkin 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.
12	PP1-active / Deph-thr286c	CaMKII Pathway No. 145	5.09907	0.35	4	explicit E-S complex	Substrate: CaMKII* Product :** CaMK-thr306
	Dephosphorylation tempkin 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.
13	PP1-active / Deph_thr286b	CaMKII Pathway No. 145	5.09907	0.35	4	explicit E-S complex	Substrate: CaMKII-thr286 Product : CaMKII
	Rates 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.