4-hydroxy-2-oxoglutarate aldolase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: 4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate. [EC:4.1.3.16]

4-Hydroxy-2-oxoglutarate aldolase activity refers to the enzymatic catalysis of the reversible cleavage of 4-hydroxy-2-oxoglutarate into pyruvate and glyoxylate. This reaction is crucial for the metabolism of L-hydroxyproline, a non-proteinogenic amino acid, and plays a significant role in various biological processes. The enzyme responsible for this activity, 4-hydroxy-2-oxoglutarate aldolase, utilizes a Schiff base mechanism involving a lysine residue in its active site. The reaction proceeds in two steps: 1) condensation of 4-hydroxy-2-oxoglutarate with the lysine residue to form a Schiff base intermediate. 2) cleavage of the Schiff base intermediate into pyruvate and a glyoxylate-lysine adduct. The glyoxylate is then released from the enzyme, regenerating the active site lysine residue. This enzymatic activity is essential for the degradation of hydroxyproline and the synthesis of various metabolites, including glyoxylate and pyruvate, which are further utilized in metabolic pathways like the tricarboxylic acid cycle and gluconeogenesis.'
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Proteins (2)

Compounds (3)