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Literature summary for 4.1.3.42 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

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

Inhibitors

Inhibitors Comment Organism Structure
4-mercuribenzenesulfonic acid 1 mM, 56% inhibition Escherichia coli
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
iodoacetate 46% inhibition at 5 mM; 50 mM, almost complete inhibition Escherichia coli
additional information not inhibitory: EDTA, 1,10-phenanthroline, S-hydroxyquinoline, or alpha,alpha'-dipyridyl Escherichia coli
N-ethylmaleimide 10% inhibition at 2.5 mM Escherichia coli
NaBH4 extensive loss of activity after incubation of enzyme with NaBH4 in presence of pyruvate or glyoxylate Escherichia coli
p-Mercuriphenylsulfonate 50% inhibition at 0.5 mM Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Escherichia coli
2.3
-
(L)-4-hydroxy-alpha-ketoglutarate
-
Escherichia coli
2.3
-
(4S)-4-hydroxy-2-oxoglutarate pH 8.1, 25°C Escherichia coli
2.5
-
(D)-4-hydroxy-alpha-ketoglutarate
-
Escherichia coli
25
-
(4R)-4-hydroxy-2-oxoglutarate pH 8.1, 25°C Escherichia coli

Metals/Ions

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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

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

Storage Stability

Storage Stability Organism
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)

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

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
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
8.6
-
-
Escherichia coli

Ki Value [mM]

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