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Molecule Parameter List for PKA-active | 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 |
PKA-active 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 | 2 | 0 | 0 | 0 | 0 |
Accession and Pathway Details | |
Accession Name | Accession No. | Accession Type | Pathway Link | CaMKII_noPKA_ model3 | 62 | Network | Shared_Object_CaMKII_noPKA_model3, CaMKII, CaM, PP1, PP2B, PP1_PSD | This is the model of CaMKII bistability, model 3. It exhibits bistability in CaMKII activation due to autophosphorylation at the PSD and local saturation of PP1. This version of model 3 does not include the full PKA regulatory pathway, and instead has a predefined initial amount of active PKA. |
PKA-active acting as a Molecule in CaMKII_noPKA_model3 Network
PKA-active acting as an Enzyme in CaMKII_noPKA_model3 Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | 1 | PKA-active / PKA-phosph-I1
| CaMKII_noPKA_ model3 Accession No. : 62 | Shared_Object_ CaMKII_noPKA_ model3 Pathway No. : 257 | 7.50008 | 9 | 4 | explicit E-S complex | Substrate I1
Product I1*
| | #s from Bramson et al CRC crit rev Biochem 15:2 93-124. They have a huge list of peptide substrates and I have chosen high-ish rates. These consts give too much PKA activity, so lower Vmax 1/3. Now, k1 = 3e-5, k2 = 36, k3 = 9 (still pretty fast). Also lower Km 1/3 so k1 = 1e-5 Cohen et al FEBS Lett 76:182-86 1977 say rate =30% PKA act on phosphokinase beta. | 2 | PKA-active / PKA-phosph-I1_ PSD
| CaMKII_noPKA_ model3 Accession No. : 62 | Shared_Object_ CaMKII_noPKA_ model3 Pathway No. : 257 | 7.50008 | 9 | 4 | explicit E-S complex | Substrate I1
Product I1*
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