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Accession Type:
Network

fig3_CaMKII

Shared_Object_
fig3_CaMKII

		PKA
		Molecule
		Reaction

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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	Kf	Kb	Kd	tau	Substrate	Product
1	cAMP-bind-site-A 1	75 (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	75 (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	54 (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	54 (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-PKA	60 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 0.0167(uM)	-	PKA-active PKA-inhibitor	inhibited-PKA
6	Release-C1	60 (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-C2	60 (s^-1)	18 (uM^-1 s^-1)	Kd(cb) = 0.3(uM)	-	R2C-cAMP4	PKA-active R2-cAMP4

Pathway Details Molecule List Enzyme List Reaction List

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