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Molecule Parameter List for AC2-Gs

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

AC2-Gs 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
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

AC2-Gs acting as a Molecule in  Synaptic_Network Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
AC2-Gs	Synaptic_ Network Accession No. : 16	AC Pathway No. : 85	0	1000	No
This is the generic Gs-Stimulated form of AC2

AC2-Gs 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
AC2-Gs / 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 for AC1. This is consistent since there is a good match between the mixture of ACs tested by 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 for AC1. 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.

AC2-Gs 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
Gs-bind-AC2	Synaptic_ Network Accession No. : 16	AC Pathway No. : 85	499.998 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 0.002(uM)	-	Substrate AC2 Gs-alpha Product AC2-Gs
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's thesis data indicates it is more like 2 nM. Jacobowitz, PhD Thesis, Mount Sinai School of Medicine.