Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.

Search in:

ALL Accession Pathway Molecule Enzyme Reaction Connected to

Search for

Match

Anything Exact Word Starting With

By

Name Notes Model

Molecule Parameter List for AC1-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

AC1-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

AC1-Gs acting as a Molecule in  Synaptic_Network Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
AC1-Gs	Synaptic_ Network Accession No. : 16	AC Pathway No. : 85	0	1000	No
This is the generic Gs-Stimulated state of AC1. Note that the enzyme is normally saturated, so all reactions involving AC1-Gs actually relate to the enzyme-substrate complex.

AC1-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
AC1-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 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-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-AC1	Synaptic_ Network Accession No. : 16	AC Pathway No. : 85	126 (uM^-1 s^-1)	1 (s^-1)	Kd(bf) = 0.0079(uM)	-	Substrate AC1 Gs-alpha Product AC1-Gs
Half-max 8nM from Tang et al JBC266:13 8595-8603 kb/kf = 8 nM = 4800#/cell Also assume rapid binding of 1/sec.