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Molecule Parameter List for PP1-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

PP1-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
simple_AMPAR_ traff_model2	61	Network	Shared_Object_simple_AMPAR_traff_model2,  Membrane,  Internal
This is a highly simplified model of the AMPAR trafficking cycle that exhibits bistability. It is model 2 from Hayer and Bhalla, PLoS 2005. Its main purpose it to illustrate how the bistability arises.

PP1-active acting as a Molecule in  simple_AMPAR_traff_model2 Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
PP1-active	simple_AMPAR_ traff_model2 Accession No. : 61	Membrane Pathway No. : 255	0.3333	0.01	No

PP1-active acting as an Enzyme in  simple_AMPAR_traff_model2 Network

	Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
1	PP1-active / PP1	simple_AMPAR_ traff_model2 Accession No. : 61	Membrane Pathway No. : 255	0.999989	0.35	4	explicit E-S complex	Substrate MR* Product MR
	Note that Km is halved from 2 to 1, as compared to original detailed model. This is because each substrate represents two subunits of the original detailed model.
2	PP1-active / PP1[1]	simple_AMPAR_ traff_model2 Accession No. : 61	Membrane Pathway No. : 255	0.999989	0.35	4	explicit E-S complex	Substrate MR** Product MR*
	Note halving of Km from 2 to 1. See also notes for internal-PKA-act. Basically, the enzyme must act on two substrate subunits which are lumped in the current simplification of the original detailed model. We thank an anonymous reviewer for pointing this out.