DOQCS database

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	CaM-bind-GEF	199.995 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 0.005(uM)	-	inact-GEF CaM-Ca4	CaM-GEF
	We have no numbers for this. It is probably between the two extremes represented by the CaMKII phosph states, and I have used guesses based on this. kf=1e-4 kb=1 The reaction is based on Farnsworth et al Nature 376 524-527 1995 28 Feb 2006: Increased affinity 36-fold to account for Ca input to MAPK cascade, possibly folding in other pathway inputs. 21 April 2006: Altered affinity to same level as pkm_mapk21.g model to prevent spontaneous turnon. Kf = 200, Kb = 1.
2	dephosph-GAP	0.1 (s^-1)	0 (s^-1)	-	-	GAP*	GAP
	Assume a reasonably good rate for dephosphorylating it, 1/sec
3	dephosph-GEF	1 (s^-1)	0 (s^-1)	-	-	GEF*	inact-GEF
4	Ras-intrinsic-GT Pase	0.0001 (s^-1)	0 (s^-1)	-	-	GTP-Ras	GDP-Ras
	This is extremely slow (1e-4), but it is significant as so little GAP actually gets complexed with it that the total GTP turnover rises only by 2-3 X (see Gibbs et al, JBC 265(33) 20437-20422) and Eccleston et al JBC 268(36) 27012-27019 kf = 1e-4

Pathway Details Molecule List Enzyme List Reaction List

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