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Enzyme List for CamKII acting as a Product

Entries are grouped according to Pathway Number and they are alternately color coded using  and   color.
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  Enzyme Molecule /

 Enzyme Activity		Accession Name / 
Accession No.		Pathway Name / 
Pathway No.		Km
(uM)		kcat
(s^-1)		Ratio
(k2/k3)		Enzyme TypeReagents
21 tot_CaM_CaMKII  /
CaM_act_305
  • Synaptic_
    Network
    Accession No. 16
    		• CaMKII

    Pathway No. 80    		0.0000027056364explicit E-S complexSubstrate: 
    CaMKII-thr286
    Product : 
    CaMKII***
      Rates from autocamtide phosphorylation, from Hanson and Schulman JBC 267:24 17216-17224 1992. See especially Fig 5.
    22 tot_CaM_CaMKII  /
    CaM_act_286
  • Synaptic_
    Network
    Accession No. 16
    		• CaMKII

    Pathway No. 80    		0.000002705630.54explicit E-S complexSubstrate: 
    CaMKII-CaM
    Product : 
  • CaMKII-thr286*-C
    aM
    •   See Hanson and Schulman 1992 JBC 267(24):17216-17224
    23 
  • tot_autonomous_
    CaMKII      /
    auton_305
  • Synaptic_
    Network
    Accession No. 16
    		• CaMKII

    Pathway No. 80    		0.0000041666764explicit E-S complexSubstrate: 
    CaMKII-thr286
    Product : 
    CaMKII***
      See Hanson and Schulman 1992 JBC 267(24):17216-17224 for afterburst rates of phosphorylation
    24 
  • tot_autonomous_
    CaMKII      /
    auton_286
  • Synaptic_
    Network
    Accession No. 16
    		• CaMKII

    Pathway No. 80    		0.000004166670.54explicit E-S complexSubstrate: 
    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
    25 tot_CaM_CaMKII  /
    CaM_act_305
  • NonOsc_Ca_
    IP3metabolism
    Accession No. 23
    		• CaMKII

    Pathway No. 106    		0.0000027056364explicit E-S complexSubstrate: 
    CaMKII-thr286
    Product : 
    CaMKII***
      Rates from autocamtide phosphorylation, from Hanson and Schulman JBC 267:24 17216-17224 1992. See especially Fig 5.
    26 tot_CaM_CaMKII  /
    CaM_act_286
  • NonOsc_Ca_
    IP3metabolism
    Accession No. 23
    		• CaMKII

    Pathway No. 106    		0.000002705630.54explicit E-S complexSubstrate: 
    CaMKII-CaM
    Product : 
  • CaMKII-thr286*-C
    aM
    •   See Hanson and Schulman 1992 JBC 267(24):17216-17224
    27 
  • tot_autonomous_
    CaMKII      /
    auton_305
  • NonOsc_Ca_
    IP3metabolism
    Accession No. 23
    		• CaMKII

    Pathway No. 106    		0.0000041666764explicit E-S complexSubstrate: 
    CaMKII-thr286
    Product : 
    CaMKII***
      See Hanson and Schulman 1992 JBC 267(24):17216-17224 for afterburst rates of phosphorylation
    28 
  • tot_autonomous_
    CaMKII      /
    auton_286
  • NonOsc_Ca_
    IP3metabolism
    Accession No. 23
    		• CaMKII

    Pathway No. 106    		0.000004166670.54explicit E-S complexSubstrate: 
    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
    29 PP1-active  /
    Deph-thr286
  • NonOsc_Ca_
    IP3metabolism
    Accession No. 23
    		• CaMKII

    Pathway No. 106    		5.099070.354explicit E-S complexSubstrate: 
  • 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.
    30 PP1-active  /
    Deph-thr305
  • NonOsc_Ca_
    IP3metabolism
    Accession No. 23
    		• CaMKII

    Pathway No. 106    		5.099070.354explicit E-S complexSubstrate: 
    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.
    31 PP1-active  /
    Deph-thr306
  • NonOsc_Ca_
    IP3metabolism
    Accession No. 23
    		• CaMKII

    Pathway No. 106    		5.099070.354explicit E-S complexSubstrate: 
    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.
    32 PP1-active  /
    Deph_thr286b
  • NonOsc_Ca_
    IP3metabolism
    Accession No. 23
    		• CaMKII

    Pathway No. 106    		5.099070.354explicit E-S complexSubstrate: 
    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.
    33 tot_CaM_CaMKII  /
    CaM_act_305
  • Osc_Ca_
    IP3metabolism
    Accession No. 24
    		• CaMKII

    Pathway No. 121    		0.0000027056364explicit E-S complexSubstrate: 
    CaMKII-thr286
    Product : 
    CaMKII***
      Rates from autocamtide phosphorylation, from Hanson and Schulman JBC 267:24 17216-17224 1992. See especially Fig 5.
    34 tot_CaM_CaMKII  /
    CaM_act_286
  • Osc_Ca_
    IP3metabolism
    Accession No. 24
    		• CaMKII

    Pathway No. 121    		0.000002705630.54explicit E-S complexSubstrate: 
    CaMKII-CaM
    Product : 
  • CaMKII-thr286*-C
    aM
    •   See Hanson and Schulman 1992 JBC 267(24):17216-17224
    35 
  • tot_autonomous_
    CaMKII      /
    auton_305
  • Osc_Ca_
    IP3metabolism
    Accession No. 24
    		• CaMKII

    Pathway No. 121    		0.0000041666764explicit E-S complexSubstrate: 
    CaMKII-thr286
    Product : 
    CaMKII***
      See Hanson and Schulman 1992 JBC 267(24):17216-17224 for afterburst rates of phosphorylation
    36 
  • tot_autonomous_
    CaMKII      /
    auton_286
  • Osc_Ca_
    IP3metabolism
    Accession No. 24
    		• CaMKII

    Pathway No. 121    		0.000004166670.54explicit E-S complexSubstrate: 
    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
    37 PP1-active  /
    Deph-thr286
  • Osc_Ca_
    IP3metabolism
    Accession No. 24
    		• CaMKII

    Pathway No. 121    		5.099070.354explicit E-S complexSubstrate: 
  • 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.
    38 PP1-active  /
    Deph-thr305
  • Osc_Ca_
    IP3metabolism
    Accession No. 24
    		• CaMKII

    Pathway No. 121    		5.099070.354explicit E-S complexSubstrate: 
    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.
    39 PP1-active  /
    Deph-thr306
  • Osc_Ca_
    IP3metabolism
    Accession No. 24
    		• CaMKII

    Pathway No. 121    		5.099070.354explicit E-S complexSubstrate: 
    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.
    40 PP1-active  /
    Deph_thr286b
  • Osc_Ca_
    IP3metabolism
    Accession No. 24
    		• CaMKII

    Pathway No. 121    		5.099070.354explicit E-S complexSubstrate: 
    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.
    Result: 21 - 40 of 208 rows are displayed Previous of 11  Next


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