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Literature summary for 4.1.2.14 extracted from

  • Taha, T.S.; Deits, T.L.
    Purification and characterization of 2-keto-3-deoxy-6-phosphogluconate aldolase from Azotobacter vinelandii: evidence that the enzyme is bifunctional towards 2-keto-4-hydroxyglutarate cleavage (1994), Biochem. Biophys. Res. Commun., 200, 459-466.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
KCl 100 mM, 67% inhibition Azotobacter vinelandii
KI 100 mM, 93% inhibition Azotobacter vinelandii
NaBr 100 mM, 88% inhibition Azotobacter vinelandii
NaCl 100 mM, 76% inhibition Azotobacter vinelandii
NaF 100 mM, 45% inhibition Azotobacter vinelandii
NaI 100 mM, 93% inhibition Azotobacter vinelandii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.038
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
Azotobacter vinelandii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
3 * 24000, SDS-PAGE Azotobacter vinelandii
70000
-
-
Azotobacter vinelandii

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
bifunctional enzyme Ec4.1.2.14/Ec4.1.3.16
-

Purification (Commentary)

Purification (Comment) Organism
-
Azotobacter vinelandii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
625
-
-
Azotobacter vinelandii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
Azotobacter vinelandii pyruvate + D-glyceraldehyde 3-phosphate
-
?

Subunits

Subunits Comment Organism
trimer 3 * 24000, SDS-PAGE Azotobacter vinelandii