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Molecule Parameter List for ATP | 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 |
| ATP 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 | 0 | 2 | 0 | 0 | 0 |
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. |
ATP acting as a Molecule in AMPAR_CaMKII_weak_coupling Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | ATP | AMPAR_CaMKII_
weak_coupling
Accession No. : 65 | AC
Pathway No. : 289 | 2000 | 0.09 | Yes | | ATP is present in all cells between 2 and 10 mM. See Lehninger |
ATP acting as a Substrate for 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 | | 1 | 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. | | 2 | AC2* /
kenz | AMPAR_CaMKII_
weak_coupling
Accession No. : 65 | AC
Pathway No. : 289 | 300.002 | 2 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | Substrate
ATP
Product
cAMP
| | | Reduced Km to match expt data for basal activation of AC2 by PKC. Now k1 = 2.9e-6, k2 = 72, k3 = 18 18 Feb: Raised Km to 300 based on BRENDA data. Unlikely to make much difference, given the vast amount of ATP. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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