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Literature summary for 1.10.3.1 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
Search for more literature for 1.10.3.1

Activating Compound

Activating Compound Comment Organism Structure
SDS PPO from membrane shows no diphenolase activity unless it is activated by trypsin or sodium dodecyl sulfate Beta vulgaris
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]

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

Localization

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Beta vulgaris
-
 red beet
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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

Source Tissue Comment Organism Textmining
root
-
 Beta vulgaris
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dopamine + 1/2 O2
-
 Beta vulgaris dopamine quinone + H2O
-
 ?
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

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
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