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Literature summary for 4.1.3.16 extracted from

  • Kobes, R.D.; Dekker, E.E.
    Variant properties of bovine liver 2-keto-4-hydroxyglutarate aldolase: its beta-decarboxylase activity, lack of substrate stereospecificity, and structural requirements for binding substrate analogs (1971), Biochim. Biophys. Acta, 251, 238-250.
    View publication on PubMed
Search for more literature for 4.1.3.16

Inhibitors

Inhibitors Comment Organism Structure
NaBH4 azomethine formation with substrates and substrate analogues Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no requirement Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
 bovine
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-Hydroxy-2-oxoglutarate both stereoisomers Bos taurus Pyruvate + glyoxylate
-
 ?
Glyoxylate + pyruvate higher specificity for pyruvate than for glyoxylate Bos taurus 4-Hydroxy-2-ketoglutarate
-
 ?
additional information mechanism Bos taurus ?
-
 ?
additional information 2-keto-4-hydroxy-4-methylglutarate, 2-keto-3-deoxy-6-phosphoclucanate cleaved at slow rate Bos taurus ?
-
 ?
additional information acts on both stereoisomers Bos taurus ?
-
 ?
additional information 2-keto-3-deoxyglucarate and 2-keto-4,5-dihydroxyvalerate cleaved at slow rate Bos taurus ?
-
 ?
Oxaloacetate beta-decarboxylation, about 50% as effective as aldolase Bos taurus CO2 + pyruvate
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
13.5
-
 DL-2-keto-4-hydroxyglutarate
-
 Bos taurus