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Molecule Parameter List for Gbg

The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network. The text color of a molecule is highlighted by color.

Statistics

Gbg participated as	Molecule	Sum total of	Enzyme	Substrate of an enzyme	Product of an enzyme	Substrate in Reaction	Product in Reaction
No. of occurrences	1	0	0	0	0	1	1

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
cAMP_pathway	25	Network	Shared_Object_cAMP_pathway,  PKA,  AC,   Gs
This is a model of the canonical cAMP signaling pathway: Ligand->Receptor->G-protein->Cyclase->cAMP->PKA. It also includes phosphodiesterases to balance out cAMP formation.Bhalla US Methods Enzymol. 2002;345:3-23

Gbg acting as a Molecule in  cAMP_pathway Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
Gbg	cAMP_pathway Accession No. : 25	Gs Pathway No. : 137	0	1000	No
The Gbetagamma dimer.

Gbg acting as a Substrate in a reaction in  cAMP_pathway Network

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 reaction are not consider.

Name	Accession Name	Pathway Name	Kf	Kb	Kd	tau	Reagents
Trimerize-Gs	cAMP_pathway Accession No. : 25	Gs Pathway No. : 137	6 (uM^-1 s^-1)	0 (s^-1)	-	-	Substrate GDP.Ga Gbg Product GDP.Gabc
Negligible back-reaction.

Gbg acting as a Product in a reaction in  cAMP_pathway Network

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 reaction are not consider.

Name	Accession Name	Pathway Name	Kf	Kb	Kd	tau	Reagents
Activate-Gs	cAMP_pathway Accession No. : 25	Gs Pathway No. : 137	0.025 (s^-1)	0 (uM^-2 s^-1)	-	-	Substrate L.R.GDP.Gabc Product GTP.Ga Gbg L.R
This step combines several stages in GTP.Galpha release. From Berstein et al activation is at .35 - 0.7/min From Fay et al Biochem 30 5066-5075 1991 kf = .01/sec. From Brandt and Ross JBC 261(4):1656-1664 (1986) and Ransan et al Biochem J 283(2):519-524 (1992) rates around 2.5/min to 1.5/min are better.