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Literature summary for 4.1.3.42 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
Search for more literature for 4.1.3.42

Inhibitors

Inhibitors Comment Organism Structure
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]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli P0A955
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

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

pH Stability

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