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Enzyme List for pathway Shared_Object_CaMKII_2003 (Pathway Number 201)

 Molecule Name/
Site Name 		Km (uM) kcat (1/s)Ratio
(k2/k3)		Enzyme TypeSubstrate Product
1 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
    2 Enzyme Activity:
    Deph-thr286c

    Enzyme Molecule:
    PP1-active    		5.09910.354explicit E-S complexCaMKII***
    		CaMK-thr306
    3 Enzyme Activity:
    Deph-thr305

    Enzyme Molecule:
    PP1-active    		5.09910.354explicit E-S complexCaMKII***
    		CaMKII-thr286
    4 Enzyme Activity:
    Deph-thr306

    Enzyme Molecule:
    PP1-active    		5.09910.354explicit E-S complexCaMK-thr306
    		CaMKII
      See Cohen et al
    5 Enzyme Activity:
    dephosph-PP1-I*

    Enzyme Molecule:
    CaM(Ca)n-CaNAB    		4.97080.344explicit E-S complexPP1-I1*
    		PP1-I1
    6 Enzyme Activity:
    dephosph_inhib1

    Enzyme Molecule:
    CaM(Ca)n-CaNAB    		4.97080.344explicit E-S complexI1*
    		I1
    7 Enzyme Activity:
    dephosph_
    inhib1_noCaM

    Enzyme Molecule:
    CaNAB-Ca4    		4.97080.0344explicit E-S complexI1*
    		I1
      The rates here are so slow I do not know if we should even bother with this enz reacn. These numbers are from Liu and Storm. Other refs suggest that the Km stays the same but the Vmax goes to 10% of the CaM stim levels. Prev: k1=2.2e-9, k2 = 0.0052, k3 = 0.0013 New : k1=5.7e-8, k2=.136, k3=.034
    8 Enzyme Activity:
    dephosph_
    neurogranin

    Enzyme Molecule:
    CaM(Ca)n-CaNAB    		10.0120.673.98507explicit E-S complexneurogranin*
    		neurogranin
      From Seki et al ABB 316(2):673-679
    9 Enzyme Activity:
    Deph_thr286b

    Enzyme Molecule:
    PP1-active    		5.09910.354explicit E-S complexCaMKII-thr286
    		CaMKII
    10 Enzyme Activity:
    PKA-phosph-I1

    Enzyme Molecule:
    PKA-active    		7.594explicit E-S complexI1
    		I1*
      #s from Bramson et al CRC crit rev Biochem 15:2 93-124. They have a huge list of peptide substrates and I have chosen high-ish rates. These consts give too much PKA activity, so lower Vmax 1/3. Now, k1 = 3e-5, k2 = 36, k3 = 9 (still pretty fast). Also lower Km 1/3 so k1 = 1e-5 Cohen et al FEBS Lett 76:182-86 1977 say rate =30% PKA act on phosphokinase beta.
    11 Enzyme Activity:
    PKC-phosph-neuro
    granin

    Enzyme Molecule:
    PKC-active    		28.62750.584.03448explicit E-S complexneurogranin
    		neurogranin*
      Rates from Huang et al ABB 305:2 570-580 1993
    12 Enzyme Activity:
    PKC-phosph-ng-Ca
    M

    Enzyme Molecule:
    PKC-active    		28.59480.354explicit E-S complexneurogranin-CaM
    		CaM
    neurogranin*
      Rates are 60% those of PKC-phosph-neurogranin. See Huang et al ABB 305:2 570-580 1993
    13 Enzyme Activity:
    PP2A-dephosph-I1

    Enzyme Molecule:
    PP2A    		7.828364.16667explicit E-S complexI1*
    		I1
      PP2A does most of the dephosph of I1 at basal Ca levels. See the review by Cohen in Ann Rev Biochem 1989. For now, lets halve Km. k1 was 3.3e-6, now 6.6e-6
    14 Enzyme Activity:
    PP2A-dephosph-PP
    1-I*

    Enzyme Molecule:
    PP2A    		7.828364.16667explicit E-S complexPP1-I1*
    		PP1-I1
      k1 changed from 3.3e-6 to 6.6e-6
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