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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 asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1002200

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
MAPK_osc27Pathway
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
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
MKK-PMAPK_osc
Accession No. : 27
MAPK
Pathway No. : 139
00.0016667No
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 NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
1MKKK-P  /
4
MAPK_osc
Accession No. : 27
MAPK
Pathway No. : 139
0.01500010.0254Classical 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.
2int3  /
6
MAPK_osc
Accession No. : 27
MAPK
Pathway No. : 139
0.0150.754Classical 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 NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
1MKKK-P  /
3
MAPK_osc
Accession No. : 27
MAPK
Pathway No. : 139
0.01500010.0254Classical 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
2int2  /
5
MAPK_osc
Accession No. : 27
MAPK
Pathway No. : 139
0.0150.754Classical 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



Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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