Catechol oxidase (dimerizing)

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Identifiers
EC number1.10.3.1
CAS number9002-10-2
Alt. names
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway



Catechol oxidase (dimerizing) is an enzyme that belongs to the oxidoreductase family, specifically those acting on diphenols and related substances as donors with oxygen as the acceptor. This enzyme is crucial in the biochemical process of oxidation and is involved in the browning reaction in various fruits and vegetables.

Structure[edit | edit source]

Catechol oxidase is a copper-containing enzyme that typically exists as a dimer. The active site of the enzyme contains two copper ions, which are essential for its catalytic activity. The enzyme's structure allows it to bind to catechol substrates and facilitate their oxidation.

Function[edit | edit source]

The primary function of catechol oxidase is to catalyze the oxidation of catechol to o-quinone, a reaction that involves the reduction of molecular oxygen to water. This reaction is a key step in the biosynthesis of melanin and other pigments in plants and some microorganisms.

Mechanism[edit | edit source]

Catechol oxidase operates through a binuclear copper center mechanism. The enzyme binds to catechol, and the copper ions facilitate the transfer of electrons from the substrate to molecular oxygen, resulting in the formation of o-quinone and water. This process is crucial for the defense mechanism in plants, as the o-quinone products can polymerize to form protective barriers against pathogens.

Biological Role[edit | edit source]

In plants, catechol oxidase plays a significant role in wound healing and defense. When plant tissues are damaged, the enzyme is activated, leading to the production of quinones that can deter herbivores and inhibit the growth of microbial pathogens.

Applications[edit | edit source]

Catechol oxidase has applications in various fields, including food industry, biotechnology, and medicine. In the food industry, understanding the enzyme's activity is important for controlling the browning of fruits and vegetables. In biotechnology, catechol oxidase is used in biosensors for detecting phenolic compounds.

Related Enzymes[edit | edit source]

Catechol oxidase is related to other polyphenol oxidases, such as tyrosinase and laccase, which also catalyze the oxidation of phenolic compounds. These enzymes share similar structural features and catalytic mechanisms.

See Also[edit | edit source]

External Links[edit | edit source]

  • [Enzyme Database]
  • [Protein Data Bank]


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Contributors: Prab R. Tumpati, MD