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Literature summary extracted from

  • Orenes-Pinero, E.; Garcia-Carmona, F.; Sanchez-Ferrer, A.
    A kinetic study of p-cresol oxidation by quince fruit polyphenol oxidase (2005), J. Agric. Food Chem., 53, 1196-1200.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.10.3.1 additional information
-
 additional information general kinetic mechanism, the diphenolase activity is characterized by a lag period, whose duration depends on the substrate concentration, the pH, and the presence of catalytic amounts of o-diphenol, overview Cydonia oblonga
1.10.3.1 1.2
-
 4-methylcatechol pH 7.0, 25°C Cydonia oblonga
1.14.18.1 additional information
-
 additional information steady-state rate in monophenolase activity Cydonia oblonga
1.14.18.1 2.2
-
 p-Cresol pH 7.0, 25°C Cydonia oblonga

Organism

EC Number Organism UniProt Comment Textmining
1.10.3.1 Cydonia oblonga
-
 var. Gigante de Vranja, quince
-
1.14.18.1 Cydonia oblonga
-
 var. Gigante de Vranja, quince
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.10.3.1 partially purified in a sequential two-phase system based on Triton X-114 and PEG-8000/phosphate, followed by ammonium sulfate fractionation Cydonia oblonga
1.14.18.1 partially purified in a sequential two-phase system based on Triton X-114 and PEG-8000/phosphate, followed by ammonium sulfate fractionation Cydonia oblonga

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.10.3.1 fruit
-
 Cydonia oblonga
-
1.14.18.1 fruit
-
 Cydonia oblonga
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.10.3.1 additional information
-
 assay optimization Cydonia oblonga
1.14.18.1 additional information
-
 assay optimization Cydonia oblonga

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.1 4-methylcatechol + O2
-
 Cydonia oblonga 4-methyl-1,2-benzoquinone + H2O
-
 ?
1.10.3.1 catechol + 1/2 O2
-
 Cydonia oblonga 1,2-benzoquinone + H2O
-
 ?
1.10.3.1 additional information the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview Cydonia oblonga ?
-
 ?
1.14.18.1 additional information the enzyme catalyzes the hydroxylation of monophenols to o-diphenols, monophenolase activity EC 1.14.18.1, and the oxidation of the o-diphenols to o-quinones, diphenolase activity EC 1.10.3.1, cross-reaction analysis, overview Cydonia oblonga ?
-
 ?
1.14.18.1 p-cresol + O2
-
 Cydonia oblonga 4-methyl-o-quinone + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.10.3.1 catecholase
-
 Cydonia oblonga
1.10.3.1 dihydroxy-L-phenylalanine:oxygen oxidoreductase
-
 Cydonia oblonga
1.10.3.1 diphenolase
-
 Cydonia oblonga
1.10.3.1 More cf. 1.14.18.1 Cydonia oblonga
1.10.3.1 polyphenol oxidase
-
 Cydonia oblonga
1.10.3.1 PPO
-
 Cydonia oblonga
1.14.18.1 cresolase
-
 Cydonia oblonga
1.14.18.1 dihydroxy-L-phenylalanine:oxygen oxidoreductase
-
 Cydonia oblonga
1.14.18.1 monophenolase
-
 Cydonia oblonga
1.14.18.1 More cf. 1.10.3.1 Cydonia oblonga
1.14.18.1 polyphenol oxidase
-
 Cydonia oblonga
1.14.18.1 PPO
-
 Cydonia oblonga

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.3.1 25
-
 assay at Cydonia oblonga
1.14.18.1 25
-
 assay at Cydonia oblonga

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.3.1 7
-
 assay at Cydonia oblonga
1.14.18.1 7
-
 assay at Cydonia oblonga

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.10.3.1 additional information
-
 catecholase activity pH profile Cydonia oblonga
1.14.18.1 additional information
-
 monophenolase activity pH profile Cydonia oblonga