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Result: 1 - 13 of 13 rows are displayed

Enzyme List for pathway CaMKII (Pathway Number 121) in Accession Osc_Ca_IP3metabolism (Accession Number 24)

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  Enzyme Molecule /

 Enzyme Activity
Pathway Name / 
Pathway No.
Km
(uM)
kcat
(s^-1)
Ratio
(k2/k3)
Enzyme TypeReagents
1 tot_CaM_CaMKII /
CaM_act_305
CaMKII

Pathway No. 121
2.70563e-0664explicit 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.
2 tot_CaM_CaMKII /
CaM_act_286
CaMKII

Pathway No. 121
2.70563e-060.54explicit E-S complexSubstrate: 
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. 121
1.600010.54explicit E-S complexSubstrate: 
IP3_3K
Product : 
IP3_3K*
  rates referred from standard CaM-CaMKII phosphorylation rates
4 tot_CaM_CaMKII /
CaM-CaMK-phos1
CaMKII

Pathway No. 121
1.599980.54explicit E-S complexSubstrate: 
IP3_3K_CaM
Product : 
IP3_3K_CaM*
  rates referred from standard CaM-CaMKII phosphorylation rates
5 
  • tot_autonomous_
    CaMKII
    /
    auton_305
  • CaMKII

    Pathway No. 121
    4.16667e-0664explicit E-S complexSubstrate: 
    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. 121
    4.16667e-060.54explicit 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
    7 
  • tot_autonomous_
    CaMKII
    /
    CaMK-phos
  • CaMKII

    Pathway No. 121
    2.499990.54explicit E-S complexSubstrate: 
    IP3_3K
    Product : 
    IP3_3K*
      rates referred from standard CaMKII phosphorylation rates
    8 
  • tot_autonomous_
    CaMKII
    /
    CaMK-phos1
  • CaMKII

    Pathway No. 121
    2.499950.54explicit E-S complexSubstrate: 
    IP3_3K_CaM
    Product : 
    IP3_3K_CaM*
      rates referred from standard CaMKII phosphorylation rates
    9 PP1-active /
    Deph-thr286
    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.
    10 PP1-active /
    Deph-thr305
    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.
    11 PP1-active /
    Deph-thr306
    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.
    12 PP1-active /
    Deph-thr286c
    CaMKII

    Pathway No. 121
    5.099070.354explicit E-S complexSubstrate: 
    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. 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: 1 - 13 of 13 rows are displayed



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