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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_
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. |
ATP acting as a Molecule in AMPAR_CaMKII_strong_coupling Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | ATP | AMPAR_CaMKII_
strong_coupling
Accession No. : 64 | AC
Pathway No. : 278 | 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_strong_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_
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. | | 2 | AC2* /
kenz | AMPAR_CaMKII_
strong_coupling
Accession No. : 64 | AC
Pathway No. : 278 | 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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