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