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Molecule Parameter List for 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
AC participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000010

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

AC acting as a Molecule in  
cAMP_pathway Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
ACcAMP_pathway
Accession No. : 25
AC
Pathway No. : 136
0.0151000No
AC is present at rather low levels. Here we use 0.015 uM which is meant to lump various isoforms. None of the isoforms nor the other specific regulators are included here. Jacobowitz, PhD thesis.

AC 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
Gs-bind-ACcAMP_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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