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Molecule Parameter List for Gs.AC

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

*Gs.AC* 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	1	0	0	0	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

Gs.AC acting as a Molecule in cAMP_pathway Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
Gs.AC	cAMP_pathway Accession No. : 25	AC Pathway No. : 136	0	1000	No
This is the active form of the cyclase.

Gs.AC acting as an Enzyme in cAMP_pathway Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
Gs.AC / cyclase	cAMP_pathway Accession No. : 25	AC Pathway No. : 136	20	18	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate ATP Product cAMP
See Feinstein et al PNAS 88:10173-10177, Jacobowitz et al JBC 286(6):3829-3832 Smigel, JBC 261(4):1976-1982 (1986)

Gs.AC 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
Gs-bind-AC	cAMP_pathway Accession No. : 25	AC Pathway No. : 136	499.998 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 0.002(uM)	-	Substrate AC GTP.Ga Product Gs.AC
Half-max at around 3nM = kb/kf from fig 5 in Feinstein et al PNAS USA 88 10173-10177 1991 kf = kb/1800 = 5.56e-4 kb Ofer Jacobowitz thesis (Mount Sinai 1995) data indicates it is more like 2 nM.

Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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