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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 | AMPAR_CaMKII_
strong_coupling | 64 | Network |
Shared_Object_AMPAR_CaMKII_strong_coupling, CaMKII, CaM,
PP1, AMPAR_memb, PP2B,
PKA, AC, PP1_PSD,
AMPAR | | This is a model of tight coupling between the AMPAR trafficking bistability, and the CaMKII autophosphorylation bistability. In this model, the CaMKII activity is self sustaining only when AMPAR is turned on. Further, CaMKII turns on when AMPAR is turned on. |
AC1-CaM acting as a Molecule in AMPAR_CaMKII_strong_coupling Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | AC1-CaM | AMPAR_CaMKII_
strong_coupling
Accession No. : 64 | AC
Pathway No. : 278 | 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_strong_coupling Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | AC1-CaM /
kenz
| AMPAR_CaMKII_
strong_coupling
Accession No. : 64 | AC
Pathway No. : 278 | 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_strong_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_
strong_coupling
Accession No. : 64 | AC
Pathway No. : 278 | 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 |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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