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Literature summary extracted from

  • Vlahos, C.J.; Dekker, E.E.
    Active-site residues of 2-keto-4-hydroxyglutarate aldolase from Escherichia coli (1990), J. Biol. Chem., 265, 20384-20389.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.3.42 Bromopyruvate 85% inhibition at 1 mM, pyruvate or 2-keto-4-hydroxyglutarate protect; substrate analog. Treatment results in a time- and concentration-dependent loss of enzymatic activity. The substrates pyruvate and 2-keto-4-hydroxyglutarate provide more than 90% protection against inactivation by bromopyruvate, no protective effect is seen with glycolaldehyde. 1.1 mol of bromopyruvate is incorporated per enzyme subunit by esterification of residue Glu45 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.3.42 additional information
-
 additional information
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.3.42 additional information no requirement Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.42 Escherichia coli
-
-
-
4.1.3.42 Escherichia coli P0A955
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.42
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.42 additional information active-site residues Escherichia coli ?
-
 ?
4.1.3.42 additional information residue Glu45 is essential for catalytic activity, most likely acting as the amphoteric proton donor/acceptor Escherichia coli ?
-
 ?

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.1.3.42 1.6
-
 95% loss of activity after 10 min at 4°C, reactivation within 20 min at pH 6-8 Escherichia coli