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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

AC1-CaM 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
AMPAR_CaMKII_ weak_coupling	65	Network	Shared_Object_AMPAR_CaMKII_weak_coupling,  CaMKII,  CaM,   PP1,  PP2B,  PP1_PSD,   AMPAR,  PKA,  AC,   AMPAR_memb,  PP1_CaMKII_PSD,  CaMKII_PSD
This is a model of weak coupling between the AMPAR traffikcing bistability, and the CaMKII autophosphorylation bistability. In this model, there are three stable states: Both off, AMPAR on, or both on. The fourth possible state: CaMKII on but AMPAR off, is not truly stable, since over the course of hours the AMPAR also turns on.

AC1-CaM acting as a Molecule in  AMPAR_CaMKII_weak_coupling Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
AC1-CaM	AMPAR_CaMKII_ weak_coupling Accession No. : 65	AC Pathway No. : 289	0	0.09	No
This version of cyclase is Calmodulin activated. Gs stims it but betagamma inhibits.

AC1-CaM acting as an Enzyme in  AMPAR_CaMKII_weak_coupling Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
AC1-CaM / kenz	AMPAR_CaMKII_ weak_coupling Accession No. : 65	AC Pathway No. : 289	299.998	4.5	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate ATP Product cAMP
17 Feb 2005 Halved Vmax as the amount of enzyme has been doubled to get an integer value in the spine. 18 Feb 2005. Updated Km from BRENDA: EC No 4.6.1.1 Rat Km: 0.95 mM Turnover 12/sec. Human Km: 0.3 mM 12 umol/min/mg for mammalia, turnover is 12/sec See PMID 8663304 by Dessauer and Gilman JBC 271 1996 Unfortunately turnover range is from 34 down to 0.1 in different studies, according to BRENDA.

AC1-CaM acting as a Product in a reaction in  AMPAR_CaMKII_weak_coupling 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	AMPAR_CaMKII_ weak_coupling Accession No. : 65	AC Pathway No. : 289	49.9997 (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 kb/kf = 20 nM = 12000 #/cell so kf = kb/12000 = kb * 8.333e-5