Tyrosinase: Difference between revisions
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== Tyrosinase == | == Tyrosinase == | ||
'''Tyrosinase''' is | [[File:PDB_1js8_EBI.jpg|Crystal structure of tyrosinase|thumb|right]] | ||
'''Tyrosinase''' is a copper-containing enzyme that is widely distributed in plants, animals, and fungi. It is a key enzyme in the biosynthesis of [[melanin]] and other [[polyphenolic compounds]]. Tyrosinase catalyzes the oxidation of [[phenols]] such as [[tyrosine]] and is responsible for the browning of fruits and vegetables, as well as the pigmentation of skin, hair, and eyes in animals. | |||
== Structure == | == Structure == | ||
Tyrosinase is a type 3 copper protein, meaning it contains two copper ions | |||
Tyrosinase is a type 3 copper protein, meaning it contains two copper ions in its active site. These copper ions are crucial for the enzyme's catalytic activity. The enzyme is typically a monomer or a dimer, depending on the organism. The crystal structure of tyrosinase reveals a complex arrangement of alpha helices and beta sheets that form a stable scaffold for the active site. | |||
[[File:Protein_nucleotides.png|Representation of protein and nucleotide interaction|thumb|left]] | |||
== Function == | == Function == | ||
The primary function of tyrosinase is to catalyze the oxidation of phenolic compounds. It converts [[tyrosine]] to [[dopaquinone]], which is a precursor to melanin. This reaction involves the hydroxylation of monophenols and the oxidation of o-diphenols to o-quinones. These quinones then polymerize to form melanin. | |||
== Biological Role == | == Biological Role == | ||
In animals, tyrosinase is crucial for the production of melanin, which provides pigmentation and protection against UV radiation. In plants, it is involved in the defense mechanism against pathogens and in the browning process of damaged tissues. | |||
== | [[File:Mason_raper_pathway.png|Mason-Raper pathway of melanin synthesis|thumb|right]] | ||
== Pathways == | |||
The [[Mason-Raper pathway]] is a well-known pathway involving tyrosinase in the synthesis of melanin. This pathway starts with the conversion of tyrosine to dopaquinone, followed by several non-enzymatic reactions leading to the formation of melanin. | |||
== Genetic Aspects == | |||
Mutations in the tyrosinase gene can lead to various pigmentation disorders. For example, certain mutations can cause [[albinism]], a condition characterized by the absence of melanin. The open reading frame of the tyrosinase gene can be affected by mutations that alter its function. | |||
[[File:Drawing_of_ORF_with_mutations_updated.png|Open reading frame with mutations|thumb|left]] | |||
== Phylogeny == | |||
Tyrosinase is evolutionarily conserved across different species, indicating its fundamental biological importance. The phylogenetic tree of tyrosinase shows its distribution and evolutionary relationships among various organisms. | |||
[[File:Tyrosinase_phylogeny.png|Phylogenetic tree of tyrosinase|thumb|right]] | |||
== Applications == | |||
Tyrosinase has applications in various industries, including cosmetics, food, and pharmaceuticals. It is used in skin-lightening products and as a biosensor for phenolic compounds. | |||
== Related Pages == | == Related Pages == | ||
* [[Melanin]] | * [[Melanin]] | ||
* [[Albinism]] | * [[Albinism]] | ||
* [[ | * [[Enzyme]] | ||
* [[Copper protein]] | |||
* | |||
[[Category:Enzymes]] | [[Category:Enzymes]] | ||
[[Category:Oxidoreductases]] | [[Category:Oxidoreductases]] | ||
[[Category:Melanin biosynthesis]] | |||
Latest revision as of 10:58, 23 March 2025
Tyrosinase[edit]
Tyrosinase is a copper-containing enzyme that is widely distributed in plants, animals, and fungi. It is a key enzyme in the biosynthesis of melanin and other polyphenolic compounds. Tyrosinase catalyzes the oxidation of phenols such as tyrosine and is responsible for the browning of fruits and vegetables, as well as the pigmentation of skin, hair, and eyes in animals.
Structure[edit]
Tyrosinase is a type 3 copper protein, meaning it contains two copper ions in its active site. These copper ions are crucial for the enzyme's catalytic activity. The enzyme is typically a monomer or a dimer, depending on the organism. The crystal structure of tyrosinase reveals a complex arrangement of alpha helices and beta sheets that form a stable scaffold for the active site.
Function[edit]
The primary function of tyrosinase is to catalyze the oxidation of phenolic compounds. It converts tyrosine to dopaquinone, which is a precursor to melanin. This reaction involves the hydroxylation of monophenols and the oxidation of o-diphenols to o-quinones. These quinones then polymerize to form melanin.
Biological Role[edit]
In animals, tyrosinase is crucial for the production of melanin, which provides pigmentation and protection against UV radiation. In plants, it is involved in the defense mechanism against pathogens and in the browning process of damaged tissues.
Pathways[edit]
The Mason-Raper pathway is a well-known pathway involving tyrosinase in the synthesis of melanin. This pathway starts with the conversion of tyrosine to dopaquinone, followed by several non-enzymatic reactions leading to the formation of melanin.
Genetic Aspects[edit]
Mutations in the tyrosinase gene can lead to various pigmentation disorders. For example, certain mutations can cause albinism, a condition characterized by the absence of melanin. The open reading frame of the tyrosinase gene can be affected by mutations that alter its function.
Phylogeny[edit]
Tyrosinase is evolutionarily conserved across different species, indicating its fundamental biological importance. The phylogenetic tree of tyrosinase shows its distribution and evolutionary relationships among various organisms.
Applications[edit]
Tyrosinase has applications in various industries, including cosmetics, food, and pharmaceuticals. It is used in skin-lightening products and as a biosensor for phenolic compounds.
