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Literature summary extracted from

  • Flint, D.H.; Emptage, M.H.; Finnegan, M.G.; Fu, W.; Johnson, M.K.
    The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase (1993), J. Biol. Chem., 268, 14732-14742.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.9 1.5
-
 2,3-dihydroxyisovalerate pH 8.0, Tris buffer, since only one of the isomers present in the racemic substrate is active, the corrected Km would be 0.75 mM Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.9 Iron contains a [4Fe-4S]2+,+ cluster which is essential for catalysis and unstable in the presence of O2 and O2- Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.9 66000
-
 2 * 66000, SDS-PAGE Escherichia coli
4.2.1.9 125000
-
 native PAGE Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.9 Escherichia coli
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
4.2.1.9 oxidative degradation appears to lead to a complete breakdown of the Fe-S cluster, and the resulting protein cannot by reactivated with Fe2+ and thiol reducing agents Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.9 63
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.9 2,3-dihydroxy-3-methylbutanoate
-
 Escherichia coli 2-oxoisovalerate + H2O
-
 ?
4.2.1.9 2,3-dihydroxy-3-methylpentanoate
-
 Escherichia coli 3-methyl-2-oxopentanoate + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.9 dimer 2 * 66000, SDS-PAGE Escherichia coli