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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 asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000011

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
cAMP_pathway25Network
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
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
GbgcAMP_pathway
Accession No. : 25
Gs
Pathway No. : 137
01000No
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.
NameAccession NamePathway NameKfKbKdtauReagents
Trimerize-GscAMP_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.
NameAccession NamePathway NameKfKbKdtauReagents
Activate-GscAMP_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.



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