Found in a broad variety of bacteria, fungi, plants, insects, crustaceans, and mammals, which is involved in the synthesis of betalains and melanin.
| Predicate | Object |
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| rdf:type | |
| rdfs:comment |
During the diphenolase cycle the enzyme binds an external diphenol molecule (such as L-dopa) and oxidizes it to an O-quinone that is released along with a water molecule, leaving the enzyme in the intermediate met state.,
During the monophenolase cycle, one of the bound oxygen atoms is transferred to a monophenol (such as L-tyrosine), generating an O-diphenol intermediate, which is subsequently oxidized to an o-quinone and released, along with a water molecule.,
Found in a broad variety of bacteria, fungi, plants, insects, crustaceans, and mammals, which is involved in the synthesis of betalains and melanin.,
However, the latter can not catalyze the hydroxylation or monooxygenation of monophenols.,
The enzyme remains in an inactive deoxy state, and is restored to the active oxy state by the binding of a new oxygen molecule.,
The enzyme then binds a second diphenol molecule and repeats the process, ending in a deoxy state.,
The enzyme, which is activated upon binding molecular oxygen, can catalyze both a monophenolase reaction cycle or a diphenolase reaction cycle.,
The second reaction is identical to that catalyzed by the related enzyme catechol oxidase (EC 1.10.3.1).
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| rdfs:subClassOf | |
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| uniprot:name |
Cresolase,
Monophenol monooxygenase,
Monophenol oxidase,
N-acetyl-6-hydroxytryptophan oxidase,
Phenolase,
Tyrosinase,
Tyrosine-dopa oxidase
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| uniprot:replaces | |
| uniprot:activity |
(1) 2 L-dopa + O(2) = 2 dopaquinone + 2 H(2)O.,
(2) L-tyrosine + O(2) = dopaquinone + H(2)O.
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| uniprot:cofactor |
Copper
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