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Literature summary for 1.14.18.1 extracted from

  • Olivares, C.; Solano, F.
    New insights into the active site structure and catalytic mechanism of tyrosinase and its related proteins (2009), Pigment Cell Melanoma Res., 22, 750-760.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ tyrosinases is a copper-containing enzyme belonging to the type 3 copper protein family Gallus gallus
Cu2+ tyrosinases is a copper-containing enzyme belonging to the type 3 copper protein family Mus musculus
Cu2+ tyrosinases is a copper-containing enzyme belonging to the type 3 copper protein family Homo sapiens
Cu2+ tyrosinases is a copper-containing enzyme belonging to the type 3 copper protein family Streptomyces castaneoglobisporus

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-
Homo sapiens
-
-
-
Mus musculus
-
-
-
Streptomyces castaneoglobisporus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein single chain type I membrane glycoprotein Gallus gallus
glycoprotein single chain type I membrane glycoprotein Mus musculus
glycoprotein single chain type I membrane glycoprotein Homo sapiens
glycoprotein single chain type I membrane glycoprotein Streptomyces castaneoglobisporus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tyrosine + L-dopa + O2
-
Gallus gallus L-dopa + dopaquinone + H2O
-
?
L-tyrosine + L-dopa + O2
-
Mus musculus L-dopa + dopaquinone + H2O
-
?
L-tyrosine + L-dopa + O2
-
Homo sapiens L-dopa + dopaquinone + H2O
-
?
L-tyrosine + L-dopa + O2
-
Streptomyces castaneoglobisporus L-dopa + dopaquinone + H2O
-
?

Synonyms

Synonyms Comment Organism
monophenol monooxygenase
-
Gallus gallus
monophenol monooxygenase
-
Mus musculus
monophenol monooxygenase
-
Homo sapiens
monophenol monooxygenase
-
Streptomyces castaneoglobisporus
tyr
-
Gallus gallus
tyr
-
Mus musculus
tyr
-
Homo sapiens
tyr
-
Streptomyces castaneoglobisporus
tyrosinase this enzyme is able to catalyse two different reactions: the hydroxylation of monophenols to o-diphenols (monophenolase or cresolase activity, EC 1.14.18.1), and the oxidation of o-diphenols to o-quinones (diphenolase or catechol oxidase activity, EC 1.10.3.1) Gallus gallus
tyrosinase this enzyme is able to catalyse two different reactions: the hydroxylation of monophenols to o-diphenols (monophenolase or cresolase activity, EC 1.14.18.1), and the oxidation of o-diphenols to o-quinones (diphenolase or catechol oxidase activity, EC 1.10.3.1) Mus musculus
tyrosinase this enzyme is able to catalyse two different reactions: the hydroxylation of monophenols to o-diphenols (monophenolase or cresolase activity, EC 1.14.18.1), and the oxidation of o-diphenols to o-quinones (diphenolase or catechol oxidase activity, EC 1.10.3.1) Homo sapiens
tyrosinase this enzyme is able to catalyse two different reactions: the hydroxylation of monophenols to o-diphenols (monophenolase or cresolase activity, EC 1.14.18.1), and the oxidation of o-diphenols to o-quinones (diphenolase or catechol oxidase activity, EC 1.10.3.1) Streptomyces castaneoglobisporus

General Information

General Information Comment Organism
physiological function tyrosinases are essential enzymes in melanin biosynthesis and therefore responsible for pigmentation of skin and hair Mus musculus
physiological function tyrosinases are essential enzymes in melanin biosynthesis and therefore responsible for pigmentation of skin and hair Homo sapiens