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Literature summary for 4.1.3.42 extracted from

  • Vlahos, C.J.; Dekker, E.E.
    Amino acid sequence of the pyruvate and the glyoxylate active-site lysine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase (1986), J. Biol. Chem., 261, 11049-11055.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
glyoxylate substrate inhibition. Glyoxylate competes for, and inhibits aldolase activity by reacting with, the one active-site lysine residue/subunit Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A955
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(4S)-4-hydroxy-2-oxoglutarate
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Escherichia coli pyruvate + glyoxylate
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r
additional information enzyme binds any one of its substrates 2-keto-4-hydroxyglutarate, pyruvate, or glyoxylate in a competitive manner Escherichia coli ?
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?
pyruvate + glyoxylate
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Escherichia coli (4S)-4-hydroxy-2-oxoglutarate
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r