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Literature summary extracted from

  • Matoba, Y.; Kumagai, T.; Yamamoto, A.; Yoshitsu, H.; Sugiyama, M.
    Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis (2006), J. Biol. Chem., 281, 8981-8990.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.10.3.1 SDS PPO from membrane shows no diphenolase activity unless it is activated by trypsin or sodium dodecyl sulfate Beta vulgaris
1.10.3.1 Trypsin PPO from membrane shows no diphenolase activity unless it is activated by trypsin or sodium dodecyl sulfate, kinetics of the activation process of latent PPO by trypsin Beta vulgaris

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.10.3.1 additional information
-
 additional information kinetics of the activation process of latent PPO by trypsin, Michaelis-Menten mechanism with double intermediate Beta vulgaris

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.10.3.1 membrane PPO from membrane shows no diphenolase activity unless it is activated by trypsin or sodium dodecyl sulfate Beta vulgaris 16020
-
1.10.3.1 soluble solubel PPO isozyme Beta vulgaris
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.10.3.1 Cu2+ two Cu2+ ions per catalytic center Beta vulgaris

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.10.3.1 32000
-
 x * 36000, latent, nonactivated membrane isozyme, SDS-PAGE, x * 32000, trypsin-activated membrane isozyme, SDS-PAGE Beta vulgaris
1.10.3.1 36000
-
 x * 36000, latent, nonactivated membrane isozyme, SDS-PAGE, x * 32000, trypsin-activated membrane isozyme, SDS-PAGE Beta vulgaris

Organism

EC Number Organism UniProt Comment Textmining
1.10.3.1 Beta vulgaris
-
 red beet
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.10.3.1 proteolytic modification PPO from membrane shows no diphenolase activity unless it is roteolytically activated by trypsin, kinetics of the activation process of latent PPO by trypsin at pH 7.0 and 25°C Beta vulgaris

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.10.3.1 root
-
 Beta vulgaris
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.10.3.1 dopamine + 1/2 O2
-
 Beta vulgaris dopamine quinone + H2O
-
 ?
1.10.3.1 additional information the enzyme catalyses two different reactions, each using molecular oxygen: the hydroxylation of monophenols to o-diphenols, monophenolase activity, and the oxidation of o-diphenols to o-quinones, diphenolase, overview Beta vulgaris ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.10.3.1 ? x * 36000, latent, nonactivated membrane isozyme, SDS-PAGE, x * 32000, trypsin-activated membrane isozyme, SDS-PAGE Beta vulgaris

Synonyms

EC Number Synonyms Comment Organism
1.10.3.1 diphenolase
-
 Beta vulgaris
1.10.3.1 More cf. EC 1.14.18.1 Beta vulgaris
1.10.3.1 polyphenol oxidase
-
 Beta vulgaris
1.10.3.1 PPO
-
 Beta vulgaris
1.10.3.1 tyrosinase
-
 Beta vulgaris

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.3.1 25
-
 assay at Beta vulgaris

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.3.1 4.5
-
 latent, nonactivated membrane isozyme Beta vulgaris
1.10.3.1 6.5
-
 activated membrane isozyme Beta vulgaris
1.10.3.1 6.5 7 latent, nonactivated soluble isozyme Beta vulgaris

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.10.3.1 additional information
-
 pH profile for the trypsin-activated PPO, pH is a determining factor in the expression of enzyme activity, it alters the ionization state of amino acid side chains or of the substrate, overview Beta vulgaris