Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.

Search in:

ALL Accession Pathway Molecule Enzyme Reaction Connected to

Search for

Match

Anything Exact Word Starting With

By

Name Notes Model

Molecule Parameter List for L.R.GDP.Gabc

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

L.R.GDP.Gabc 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	2

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

L.R.GDP.Gabc acting as a Molecule in  cAMP_pathway Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
L.R.GDP.Gabc	cAMP_pathway Accession No. : 25	Gs Pathway No. : 137	0	1000	No
This is the ternary complex, where all the action happens. There are actually a lot more steps here, including a final step where the GTP binds the L.R.Ga complex and causes the release of GTP.Ga from the L.R. For simplicity this is excluded.

L.R.GDP.Gabc 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
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.

L.R.GDP.Gabc 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
1	L-bind-R.Gabc	cAMP_pathway Accession No. : 25	Gs Pathway No. : 137	5 (uM^-1 s^-1)	0.1 (s^-1)	Kd(bf) = 0.02(uM)	-	Substrate L R.GDP.Gabc Product L.R.GDP.Gabc
	From Seifert et al Mol. Pharmacol 56:348-358 (1999) The EC50 for ISO is about 20 nM.
2	L.R-bind-Gabc	cAMP_pathway Accession No. : 25	Gs Pathway No. : 137	10.0002 (uM^-1 s^-1)	0.1 (s^-1)	Kd(bf) = 0.01(uM)	-	Substrate GDP.Gabc L.R Product L.R.GDP.Gabc
	See Fay et al Biochem 30 5066-5075 1991. kf is 0.01/sec but does not account for Gs levels. kb is 0.0001/sec. The fraction of RG is about 50%, so we can estimate Kd at about the same as for Gs basal levels. This rate has to be faster since it has to feed GTP.Ga into the system faster than the GTPase. Waldhoer et al Mol Pharmacol 53:808-818 1988 say affinity for A1adenosine/Gi is 10 nM.