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Molecule Parameter List for MKK

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 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1001100

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 acting as a Molecule in  
MAPK_osc Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
MKKMAPK_osc
Accession No. : 27
MAPK
Pathway No. : 139
0.30.0016667No
The total concn. of MKK is 300nM from Kholodenko,2000

MKK acting as a Substrate for an Enzyme in  
MAPK_osc Network
Enzyme Molecule /
Enzyme Activity
Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
MKKK-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

MKK acting as a Product of an Enzyme in  
MAPK_osc Network
Enzyme Molecule /
Enzyme Activity
Accession NamePathway NameKm (uM)kcat (s^-1)RatioEnzyme TypeReagents
int3  /
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.



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