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Accession Type:
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fig3_CaMKII
Shared_Object_
fig3_CaMKII
CaMKII
CaM
PP1
PP2B
PKA
 Molecule
 Reaction
AC

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Reaction List for pathway PKA (Pathway Number 17)

Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated. Kd for higher order reactions is not considered.
  Name KfKbKdtauSubstrateProduct
1 cAMP-bind-site-A
1
kf
(uM^-1 s^-1)
110
(s^-1)
Kd(bf) = 1.4667(uM)-R2C2-cAMP2
cAMP
R2C2-cAMP3
  Kf = 75 /sec/uM, Kb = 110 /sec; This site has higher Kd for cAMP (kinetics within bovine myocardium)
Dagfinn Ogreid and Stein Ove Doskeland (1981) FEBS Lett. 129(2):287-292
2 cAMP-bind-site-A
2
kf
(uM^-1 s^-1)
32.5
(s^-1)
Kd(bf) = 0.4333(uM)-cAMP
R2C2-cAMP3
R2C2-cAMP4
  Now cAMP shows effects of cooperativity and PKA has a low Kd for cAMP.
3 cAMP-bind-site-B
1
kf
(uM^-1 s^-1)
33
(s^-1)
Kd(bf) = 0.6111(uM)-R2C2
cAMP
R2C2-cAMP
  Kf = 54 /sec/uM, Kb = 33 /sec; PKA in normal human T lymphocytes. Hasler et al (1992) FASEB J 6:2735-2741
Kd =1e-07 M for type II, 5.6e-08 M for type I; Stephen B. Smith et al (1981) PNAS, USA 78: 1591-1595
Ka1 = 2.1e+07 /M which gives Kd = 47 nM, Kan = 5e+08 /M or Kd of 2nM from Fig.7
4 cAMP-bind-site-B
2
kf
(uM^-1 s^-1)
33
(s^-1)
Kd(bf) = 0.6111(uM)-R2C2-cAMP
cAMP
R2C2-cAMP2
  Kf = 54 /sec/uM, Kb = 33 /sec; Same Km (1e-07M) assumed as site B1.
kf/kb = 0.7e-07M*1e06/(6e05^02) = 2e-13:2.77e-12
5 inhib-PKAkf
(uM^-1 s^-1)
1
(s^-1)
Kd(bf) = 0.0167(uM)-PKA-active
PKA-inhibitor
inhibited-PKA
6 Release-C1kf
(s^-1)
18
(uM^-1 s^-1)
Kd(cb) = 0.3(uM)-R2C2-cAMP4
PKA-active
R2C-cAMP4
  The complex starts to dissociate and release catalytic subunit C. This has to be fast, as the activation of PKA by cAMP is also fast.
7 Release-C2kf
(s^-1)
18
(uM^-1 s^-1)
Kd(cb) = 0.3(uM)-R2C-cAMP4
PKA-active
R2-cAMP4


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