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Molecule List for pathway PP1 (Pathway Number 82) in Accession Synaptic_Network (Accession Number 16) | Default ordering is done according to Pathway Number. Table headers can be used for changing the default ordering.
  arrow indicates that ordering is done according to ascending or descending order.
The entries are grouped according to Pathway Number and are alternately color coded using  and  color. |
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Name | Accession
Type | Initial
Conc.
(uM) | Volume
(fL) | Buffered | Sum Total Of | | 1 | PP1-I1* | Network | 0 | 0 | No | - | | | This form has the inibitory fragment phosphorylated. The binding of PP1 is tight when the inhibitory fragment is phosphorylated Cohen 1989 Ann Rev Biochem 58:453-508 | | 2 | PP1-I1 | Network | 0 | 0 | No | - | | | This form is bound to the non-phosphorylated inibitory subunit and is prone to dissociate. Cohen 1989 Ann Rev biochem 58:453-508 | | 3 | I1* | Network | 0.001 | 0 | No | - | | | Phosphorylated form of the inhibitor. This has a high affinity for the PP1 catalytic subunit. Upon binding the PP1 is inactivated. Cohen 1989 Ann Rev Biochem 58:453-508 | | 4 | I1 | Network | 1.8 | 0 | No | - | | | I1 is a 'mixed' inhibitor, but at high enz concs it looks like a non-compet inhibitor (Foulkes et al Eur J Biochem 132 309-313 9183). We treat it as non-competitive, so it just turns the enzyme off without interacting with the binding site. Cohen et al 1989 Ann rev Biochem 58:453-508 refer to results where concentration of the inhibitor is 1.5 to 1.8 uM. In order to get complete inhib of PP1, which is at 1.8 uM, we need >= 1.8 uM. |
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