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Literature summary extracted from

  • Nishihara, H.; Dekker, E.E.
    Purification, substrate specificity and binding, beta-decarboxylase activity, and other properties of Escherichia coli 2-keto-4-hydroxyglutarate aldolase (1972), J. Biol. Chem., 247, 5079-5087.
    View publication on PubMed

General Stability

EC Number General Stability Organism
4.1.3.42 irreversibly inactivated by CN- in presence of 4-hydroxy-2-oxoglutarate Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.3.42 4-mercuribenzenesulfonic acid 1 mM, 56% inhibition Escherichia coli
4.1.3.42 CN- irreversible, in presence of 4-hydroxy-2-oxoglutarate; irreversible loss of activity in presence of glyoxylate, but not in presence of pyruvate Escherichia coli
4.1.3.42 iodoacetate 46% inhibition at 5 mM; 50 mM, almost complete inhibition Escherichia coli
4.1.3.42 additional information not inhibitory: EDTA, 1,10-phenanthroline, S-hydroxyquinoline, or alpha,alpha'-dipyridyl Escherichia coli
4.1.3.42 N-ethylmaleimide 10% inhibition at 2.5 mM Escherichia coli
4.1.3.42 NaBH4 extensive loss of activity after incubation of enzyme with NaBH4 in presence of pyruvate or glyoxylate Escherichia coli
4.1.3.42 p-Mercuriphenylsulfonate 50% inhibition at 0.5 mM 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
4.1.3.42 2.3
-
 (L)-4-hydroxy-alpha-ketoglutarate
-
 Escherichia coli
4.1.3.42 2.3
-
 (4S)-4-hydroxy-2-oxoglutarate pH 8.1, 25°C Escherichia coli
4.1.3.42 2.5
-
 (D)-4-hydroxy-alpha-ketoglutarate
-
 Escherichia coli
4.1.3.42 25
-
 (4R)-4-hydroxy-2-oxoglutarate pH 8.1, 25°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.3.42 additional information no requirement Escherichia coli
4.1.3.42 additional information divalent kations are not required. No effect on activity: Mg2+, Mn2+, Zn2+, Ca2+, Ba2+, Co2+, Cu2+, Ni2+, Fe2+, Hg2+, K+, or Fe3+ Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.3.42 62500
-
 gel filtration Escherichia coli
4.1.3.42 64000
-
 sucrose density gradient centrifugation Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.3.42 4-hydroxy-2-oxoglutarate Escherichia coli possibly involved in regulation of tricarboxylic acid cycle ?
-
 ?

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.3.42 1.53
-
 (D)-4-hydroxy-alpha-ketoglutarate Escherichia coli
4.1.3.42 7.9
-
 (L)-4-hydroxy-alpha-ketoglutarate Escherichia coli
4.1.3.42 96.7
-
 pH 8.1, 25°C Escherichia coli

Storage Stability

EC Number Storage Stability Organism
4.1.3.42 4¦C, Tris-HCl buffer, pH 7.4, 40-50% loss of activity after 1 month, more labile when frozen Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.42 (4R)-4-hydroxy-2-oxoglutarate poor substrate Escherichia coli pyruvate + glyoxylate
-
 r
4.1.3.42 (4S)-4-hydroxy-2-oxobutanoate at 8% of the rate with DL-4-hydroxy-2-oxoglutarate Escherichia coli formaldehyde
-
 r
4.1.3.42 (4S)-4-hydroxy-2-oxoglutarate
-
 Escherichia coli pyruvate + glyoxylate L-4-hydroxy-2-oxoglutarate, pyruvate and glyoxylate all bind at the same active site of the enzyme r
4.1.3.42 2-Keto-4-hydroxybutyrate
-
 Escherichia coli Pyruvate + formaldehyde
-
 ?
4.1.3.42 4-Hydroxy-2-oxoglutarate
-
 Escherichia coli Pyruvate + glyoxylate
-
 ?
4.1.3.42 4-hydroxy-2-oxoglutarate possibly involved in regulation of tricarboxylic acid cycle Escherichia coli ?
-
 ?
4.1.3.42 Glyoxylate + pyruvate higher specificity for pyruvate than for glyoxylate Escherichia coli 4-Hydroxy-2-ketoglutarate
-
 ?
4.1.3.42 additional information highly specific towards L-isomer Escherichia coli ?
-
 ?
4.1.3.42 additional information enzyme additionally shows beta-decarboxylase activity towards oxalacetate Escherichia coli ?
-
 ?
4.1.3.42 Oxaloacetate better carboxylase than aldolase Escherichia coli CO2 + pyruvate
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.3.42 37
-
 enzyme assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.3.42 additional information
-
 2.2 to 2.4 times higher activity is measured in Tris-HCl buffer than in potassium phosphate buffer at the same pH values Escherichia coli
4.1.3.42 8.6
-
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.3.42 0.5
-
 p-Mercuriphenylsulfonate
-
 Escherichia coli