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Literature summary for 3.7.1.6 extracted from

  • Pokorny, D.; Brecker, L.; Pogorevc, M.; Steiner, W.; Griengl, H.; Kappe, T.; Ribbons, D.W.
    Proton-nuclear magnetic resonance analyses of the substrates specificity of a beta-ketolase from Pseudomonas putida, acetopyruvate hydrolase (1999), J. Bacteriol., 181, 5051-5059.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.7.1.6

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ 0.1 mM Pseudomonas putida

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
 SDS-PAGE Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetylpyruvate + H2O Pseudomonas putida plays a role in the orcinol catabolism acetate + pyruvate
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas putida

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.8
-
-
 Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetylpyruvate + H2O plays a role in the orcinol catabolism Pseudomonas putida acetate + pyruvate
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 38000, SDS-PAGE Pseudomonas putida