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Literature summary for 3.1.1.24 extracted from

  • Ornston, L.N.
    The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida (1966), J. Biol. Chem., 241, 3787-3794.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012
-
2-(5-oxo-4,5-dihydrofuran-2-yl)acetic acid
-
Pseudomonas putida

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33000
-
-
Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
A.312
-
Pseudomonas putida A.312
-
A.312
-

Purification (Commentary)

Purification (Comment) Organism
422fold Pseudomonas putida

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
717
-
-
Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O 3-oxoadipate enol-lactone Pseudomonas putida 3-oxoadipate
-
?
(5-oxo-4,5-dihydrofuran-2-yl)acetic acid + H2O 3-oxoadipate enol-lactone Pseudomonas putida A.312 3-oxoadipate
-
?

Synonyms

Synonyms Comment Organism
beta-ketoadipate enol-lactone hydrolase
-
Pseudomonas putida

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
half-life, 3 min in 0.02 M sodium potassium phosphate buffer, pH 6.8, 0.005 mM Mg-EDTA Pseudomonas putida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 10 decrease of the activity is dependent on the buffer, the enzyme is less active in Tris-HCl than in potassium phosphate buffer at pH 7.5 Pseudomonas putida