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Literature summary for 1.14.18.1 extracted from

  • Gandia-Herrero, F.; Nez-Atieanzar, M.J.; Cabanes, J.; Garcia-Carmona, F.; Escribano, J.
    Differential activation of a latent polyphenol oxidase mediated by sodium dodecyl sulfate (2005), J. Agric. Food Chem., 53, 6825-6830.
    View publication on PubMed
Search for more literature for 1.14.18.1

Activating Compound

Activating Compound Comment Organism Structure
Sodium dodecyl sulfate differential activation of the latent enzyme, 4fold for L-tyrosine and tyramine, 2fold for L-DOPA and dopamine Beta vulgaris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic mechanism, general kinetic model Beta vulgaris

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane bound Beta vulgaris 16020
-
soluble
-
 Beta vulgaris
-
-

Organism

Organism UniProt Comment Textmining
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 + O2
-
 Beta vulgaris ?
-
 ?
L-DOPA + O2
-
 Beta vulgaris ?
-
 ?
L-tyrosine + L-dopa + O2
-
 Beta vulgaris L-dopa + dopaquinone + H2O
-
 ?
tyramine + O2
-
 Beta vulgaris ?
-
 ?

Synonyms

Synonyms Comment Organism
monophenolase
-
 Beta vulgaris
More cf. EC 1.10.3.1 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
6 6.5 dependent on the substrate Beta vulgaris

pH Range

pH Minimum pH Maximum Comment Organism
3.5 7.5
-
 Beta vulgaris