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Literature summary for 4.1.3.42 extracted from

  • Winter, H.C.; Lewinski, N.D.; Wang, J.K.; Dekker, E.E.
    Dimerization occurs during the reversible acid inactivation of 2-oxo-4-hydroxyglutarate aldolase from Escherichia coli (1983), Biochim. Biophys. Acta, 749, 52-61.
    View publication on PubMed

General Stability

General Stability Organism
exposure to phosphoric acid at pH 1.6 for 10 min at 4°C causes 95% or greater inactivation. Chloride ion at 50-100 mM or 10 mM 2-oxo-4-hydroxyglutarate markedly decreases both the rate and extent of inactivation; good protection is also afforded by 10 mM pyruvate, glyoxylate, glyoxal, 2-oxoglutarate or 2-oxobutyrate. The inactivation process is characterized by an alteration of secondary and tertiary structure as well as an aggregation to a dimer of the native molecule. Reactivation of enzyme activity to 60-80% of the original level is seen within 20 min at pH 6 to 8 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.45
-
(4S)-4-hydroxy-2-oxoglutarate pH 8.4, temperature not specified in the publication Escherichia coli
3.5
-
(4S)-4-hydroxy-2-oxoglutarate enzyme reactivated after acidic denaturation, pH 8.4, temperature not specified in the publication Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
exposure to phosphoric acid at pH 1.6 for 10 min at 4°C causes 95% or greater inactivation. The inactivation process is characterized by an alteration of secondary and tertiary structure as well as an aggregation to a dimer of the native molecule. Reactivation of enzyme activity to 60-80% of the original level is seen within 20 min at pH 6 to 8 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(4S)-4-hydroxy-2-oxoglutarate
-
Escherichia coli pyruvate + glyoxylate
-
r