|
Enter a Search String | | Special character and space not allowed in the query term.
Search string should be at least 2 characters long. |
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_
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 |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
|
