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Molecule Parameter List for PP2A | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| PP2A 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 | 4 | 0 | 0 | 0 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
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. | |||
PP2A acting as a Molecule in AMPAR_CaMKII_strong_coupling Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| PP2A | strong_coupling Accession No. : 64 | AMPAR_CaMKII_ strong_coupling Pathway No. : 271 | 0.1111 | 0.09 | No | |
PP2A acting as 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 | PP2A / | strong_coupling Accession No. : 64 | AMPAR_CaMKII_ strong_coupling Pathway No. : 271 | 15.9999 | 2 | 4.1667 | explicit E-S complex | Substrate I1* Product I1 |
| PP2A does most of the dephosph of I1 at basal Ca levels. See the review by Cohen in Ann Rev Biochem 1989. For now, lets halve Km. k1 was 3.3e-6, now 6.6e-6 | ||||||||
| 2 | PP2A / 1-I* | strong_coupling Accession No. : 64 | AMPAR_CaMKII_ strong_coupling Pathway No. : 271 | 15.9999 | 2 | 4.1667 | explicit E-S complex | Substrate PP1-I1* Product PP1-I1 |
| k1 changed from 3.3e-6 to 6.6e-6 | ||||||||
| 3 | PP2A / PP2A-dephosph-I1 _ PSD | strong_coupling Accession No. : 64 | AMPAR_CaMKII_ strong_coupling Pathway No. : 271 | 15.9999 | 2 | 4.1667 | explicit E-S complex | Substrate I1* Product I1 |
| PP2A does most of the dephosph of I1 at basal Ca levels. See the review by Cohen in Ann Rev Biochem 1989. For now, lets halve Km. k1 was 3.3e-6, now 6.6e-6 | ||||||||
| 4 | PP2A / PP2A-dephosph-PP 1-I*_ PSD | strong_coupling Accession No. : 64 | AMPAR_CaMKII_ strong_coupling Pathway No. : 271 | 15.9999 | 2 | 4.1667 | explicit E-S complex | Substrate PP1-I1* Product PP1-I1 |
| k1 changed from 3.3e-6 to 6.6e-6 | ||||||||
color.