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Literature summary for 4.2.1.9 extracted from

  • Myers, J.W.
    Dihydroxy acid dehydrase: an enzyme involved in the biosynthesis of isoleucine and valine (1961), J. Biol. Chem., 236, 1414-1418.
    View publication on PubMed
Search for more literature for 4.2.1.9

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ CuSO4 Escherichia coli
EDTA
-
 Escherichia coli
NaF
-
 Escherichia coli
PCMB
-
 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ divalent metal ion required, Fe2+ is most effective Escherichia coli
Mg2+ divalent metal ion required, less effective than Fe2+ Escherichia coli
Mn2+ divalent metal ion required, less effective than Fe2+ Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2,3-dihydroxy-3-methylpentanoate Escherichia coli
-
 ?
-
 ?
2,3-dihydroxyisovalerate Escherichia coli
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 K-12
-

Purification (Commentary)

Purification (Comment) Organism
partial Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.416
-
-
 Escherichia coli

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
 2,3-dihydroxy-3-methylpentanoate Escherichia coli
7.9
-
 2,3-dihydroxyisovalerate Escherichia coli