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Molecule Parameter List for MAPK

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

MAPK 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	0	1	1	0	0

Accession and Pathway Details

Accession Name	Accession No.	Accession Type	Pathway Link
MAPK_osc	27	Pathway	MAPK
This MAPK model is based on Boris N. Kholodenko Eur J Biochem. (2000) 267(6):1583-8 for data from Xenopus oocytes extracts.

MAPK acting as a Molecule in  MAPK_osc Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MAPK	MAPK_osc Accession No. : 27	MAPK Pathway No. : 139	0.3	0.0016667	No
The total concn. of MAPK is 300nM from Kholodenko, 2000.

MAPK acting as a Substrate for an Enzyme in  MAPK_osc Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
MKK-PP  / 7	MAPK_osc Accession No. : 27	MAPK Pathway No. : 139	0.0150001	0.025	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate MAPK Product MAPK-P
The Km is 15nM which is 0.015uM Vmax is 0.025s-1 from Kholodenko, 2000.

MAPK acting as a Product of an Enzyme in  MAPK_osc Network

Enzyme Molecule / Enzyme Activity	Accession Name	Pathway Name	Km (uM)	kcat (s^-1)	Ratio	Enzyme Type	Reagents
int5  / 10	MAPK_osc Accession No. : 27	MAPK Pathway No. : 139	0.0149997	0.5	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate MAPK-P Product MAPK
The Km is 15nM and Vmax is 0.5nM.s-1 from Kholodenko, 2000