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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 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 | 0 |
Accession and Pathway Details | |
AC acting as a Molecule in cAMP_pathway Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | AC | cAMP_pathway
Accession No. : 25 | AC
Pathway No. : 136 | 0.015 | 1000 | No | | 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. |
| 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. |
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