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Molecule Parameter List for MKK-P

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

*MKK-P* 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	2	2	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.

MKK-P acting as a Molecule in MAPK_osc Network

Name	Accession Name	Pathway Name	Initial Conc. (uM)	Volume (fL)	Buffered
MKK-P	MAPK_osc Accession No. : 27	MAPK Pathway No. : 139	0	0.0016667	No
This is the single phoshorylated form of MKK. from Kholodenko, 2000.

MKK-P 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
1	MKKK-P / 4	MAPK_osc Accession No. : 27	MAPK Pathway No. : 139	0.0150001	0.025	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate MKK-P Product MKK-PP
	Km is 15nM and Vmax is 0.025s-1 from Kholodenko, 2000.
2	int3 / 6	MAPK_osc Accession No. : 27	MAPK Pathway No. : 139	0.015	0.75	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate MKK-P Product MKK
	The Km is 15nM and the Vmax is 0.75nM.s-1 from Kholodenko 2000.

MKK-P 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
1	MKKK-P / 3	MAPK_osc Accession No. : 27	MAPK Pathway No. : 139	0.0150001	0.025	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate MKK Product MKK-P
	Km is 15 nM and Vmax is 0.025s-1 from Kholodenko, 2000
2	int2 / 5	MAPK_osc Accession No. : 27	MAPK Pathway No. : 139	0.015	0.75	4	Classical Michaelis-Menten V = Etot.S.Kcat/Km+S	Substrate MKK-PP Product MKK-P
	The Km is 15nM and Vmax is 0.75nM.s-1 from Kholodenko, 2000

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