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Molecule Parameter List for AC1-CaM | 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 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | Synaptic_
Network | 16 | Network |
Shared_Object_Synaptic_Network, PKC, PLA2,
PLCbeta, Gq, MAPK,
Ras, EGFR, Sos,
PLC_g, CaMKII, CaM,
PP1, PP2B, PKA,
AC, CaRegulation | This model is an annotated version of the synaptic signaling network.
The primary reference is Bhalla US and Iyengar R. Science (1999) 283(5400):381-7 but several of the model pathways have been updated.
Bhalla US Biophys J. 2002 Aug;83(2):740-52
Bhalla US J Comput Neurosci. 2002 Jul-Aug;13(1):49-62 |
AC1-CaM acting as a Molecule in Synaptic_Network Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | AC1-CaM | Synaptic_
Network
Accession No. : 16 | AC
Pathway No. : 85 | 0 | 1000 | No | | This state of AC1 is bound to Calmodulin and therefore activated. Gs stimulates it but betagamma inhibits. |
AC1-CaM acting as an Enzyme in Synaptic_Network Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | AC1-CaM /
kenz
| Synaptic_
Network
Accession No. : 16 | AC
Pathway No. : 85 | 20 | 18 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | Substrate
ATP
Product
cAMP
| | Vmax is assumed to be the same as that for the Gs-stimulated form. The rates are from: Smigel 1986 JBC 261(4):1976-1982 who has 8.27 umol/min/mg with forskolin stimulated AC. Tang et al JBC 266(13):8595-8603 have an almost identical Vmax of 8 umol/min/mg. This comes to a Vmax of 18/sec. The Km is pretty immaterial since the vast excess of ATP means that the enzyme will normally be saturated. This is a pretty fast enzyme. Note that the saturation of the enzyme means that the regulatory reactions have to involve the complex rather than the free enzyme. |
AC1-CaM acting as a Product in a reaction in Synaptic_Network 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 | | CaM-bind-AC1 | Synaptic_
Network
Accession No. : 16 | AC
Pathway No. : 85 | 49.9998
(uM^-1 s^-1) | 1
(s^-1) | Kd(bf) = 0.02(uM) | - | Substrate
AC1
CaM-Ca4
Product
AC1-CaM
| | Half-max at 20 nM CaM (Tang et al JBC 266:13 8595-8603 1991 Assume a rapid CaM binding of 1/sec. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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