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Molecule Parameter List for PPhosphatase2A | 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 |
PPhosphatase2A 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
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PPhosphatase2A acting as a Molecule in MAPK-bistability-fig1c Network
Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | PPhosphatase2A | MAPK-bistability -fig1c Accession No. : 35 | Shared_Object_ MAPK-bistability -fig1c Pathway No. : 179 | 0.224 | 1000 | No | Refs: Pato et al Biochem J 293:35-41(93); CoInit values span a range depending on source. Pato et al 1993 Biochem J 293:35-41 and Cohen et al 1988 Meth Enz 159:390-408 estimate 80 nM from muscle Zolneierowicz et al 1994 Biochem 33:11858-11867 report levels of 0.4 uM again from muscle, but expression is also strong in brain. Our estimate of 0.224 is between these two. There are many substrates for PP2A in this model, so I put the enzyme rate calculations here: Takai&Mieskes Biochem J 275:233-239 have mol wt 36 KDa. They report Vmax of 119 umol/min/mg i.e. 125/sec for k3 for pNPP substrate, Km of 16 mM. This is obviously unreasonable for protein substrates. For chicken gizzard myosin light chan, we have Vmax = 13 umol/min/mg or about k3 = 14/sec. Pato et al 1993 Biochem J 293:35-41 report caldesmon: Km = 2.2 uM, Vmax = 0.24 umol/min/mg. They do not think caldesmon is a good substrate. Calponin: Km = 14.3, Vmax = 5. Our values approximate these. |
PPhosphatase2A acting as an Enzyme in MAPK-bistability-fig1c Network
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