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Enzyme List for pathway CaMKII (Pathway Number 159)

 Molecule Name/
Site Name 		Km (uM) kcat (1/s)Ratio
(k2/k3)		Enzyme TypeSubstrate Product
1 Enzyme Activity:
auton_286

Enzyme Molecule:
tot_autonomous_
CaMKII		00.54explicit E-S complexCaMKII-CaM
  • 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
    2 Enzyme Activity:
    auton_305

    Enzyme Molecule:
    tot_autonomous_
    CaMKII    		064explicit E-S complexCaMKII-thr286
    		CaMKII***
      See Hanson and Schulman 1992 JBC 267(24):17216-17224 for afterburst rates of phosphorylation
    3 Enzyme Activity:
    CaM-CaMK-phos

    Enzyme Molecule:
    tot_CaM_CaMKII    		1.60.54explicit E-S complexIP3_3K
    		IP3_3K*
      rates referred from standard CaM-CaMKII phosphorylation rates
    4 Enzyme Activity:
    CaM-CaMK-phos1

    Enzyme Molecule:
    tot_CaM_CaMKII    		1.60.54explicit E-S complexIP3_3K_CaM
    		IP3_3K_CaM*
      rates referred from standard CaM-CaMKII phosphorylation rates
    5 Enzyme Activity:
    CaMK-phos

    Enzyme Molecule:
    tot_autonomous_
    CaMKII    		2.50.54explicit E-S complexIP3_3K
    		IP3_3K*
      rates referred from standard CaMKII phosphorylation rates
    6 Enzyme Activity:
    CaMK-phos1

    Enzyme Molecule:
    tot_autonomous_
    CaMKII    		2.50.54explicit E-S complexIP3_3K_CaM
    		IP3_3K_CaM*
      rates referred from standard CaMKII phosphorylation rates
    7 Enzyme Activity:
    CaM_act_286

    Enzyme Molecule:
    tot_CaM_CaMKII    		00.54explicit E-S complexCaMKII-CaM
  • CaMKII-thr286*-C
    aM
    •   See Hanson and Schulman 1992 JBC 267(24):17216-17224
    8 Enzyme Activity:
    CaM_act_305

    Enzyme Molecule:
    tot_CaM_CaMKII    		064explicit E-S complexCaMKII-thr286
    		CaMKII***
      Rates from autocamtide phosphorylation, from Hanson and Schulman JBC 267:24 17216-17224 1992. See especially Fig 5.
    9 Enzyme Activity:
    Deph-thr286

    Enzyme Molecule:
    PP1-active    		5.09910.354explicit E-S complex
  • CaMKII-thr286*-C
    aM
    		• 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 Enzyme Activity:
    Deph-thr286c

    Enzyme Molecule:
    PP1-active    		5.09910.354explicit E-S complexCaMKII***
    		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.
    11 Enzyme Activity:
    Deph-thr305

    Enzyme Molecule:
    PP1-active    		5.09910.354explicit E-S complexCaMKII***
    		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.
    12 Enzyme Activity:
    Deph-thr306

    Enzyme Molecule:
    PP1-active    		5.09910.354explicit E-S complexCaMK-thr306
    		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.
    13 Enzyme Activity:
    Deph_thr286b

    Enzyme Molecule:
    PP1-active    		5.09910.354explicit E-S complexCaMKII-thr286
    		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.
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