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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_traff_ model0 | 59 | Network | Shared_Object_AMPAR_traff_model0, CaMKII, CaM, PP1, PP2B, PP1_PSD, PKA, AC, AMPAR, AMPAR_memb | This is model 0 from Hayer and Bhalla, PLoS Comput Biol 2005. It has a bistable model of AMPAR traffick, plus a
non-bistable model of CaMKII. This differs from the reference model (model 1) in that model0 lacks degradation and turno
ver reactions for AMPAR. |
ATP acting as a Molecule in AMPAR_traff_model0 Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | ATP | AMPAR_traff_ model0 Accession No. : 59 | AC Pathway No. : 241 | 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_traff_model0 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | 1 | AC1-CaM / kenz | AMPAR_traff_ model0 Accession No. : 59 | AC Pathway No. : 241 | 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_traff_ model0 Accession No. : 59 | AC Pathway No. : 241 | 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 This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
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