Catechol oxidase

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Catechol oxidase
EC number
CAS number 9002-10-2
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Catechol oxidase is an enzyme that catalyses the oxidation of phenols such as catechol. Catechol oxidase is a copper-containing enzyme whose activity is similar to that of tyrosinase, a related class of copper oxidases. They are ubiquitous plant enzymes that catalyze oxidation of a range of ortho-diphenols into their corresponding o-quinones coupled with the reduction of oxygen to water. It is different from tyrosinase, Ec, which can catalyze both the monooxygenation of monophenols and the oxidation of catechols.[1]

Catechol oxidase carries out the oxidation of phenols such as catechol, using dioxygen (O2). In the presence of catechol, benzoquinone is formed (see reaction below). Hydrogens removed from catechol combine with oxygen to form water. This reaction, producing the yellow compound benzoquinone, is a form of enzymatic browning exhibited in many foods upon exposure to oxygen (e.g., in bananas). The benzoquinone is then oxidised by the air to form dark-brown melanin.

Catechol is present in small quantities in the vacuoles of cells of many plant tissues. Catechol oxidase is present in the cell cytoplasm. If the plant tissues are damaged, the catechol is released and the enzyme converts the catechol to ortho-quinone, which is a natural antiseptic. Catechol oxidase, therefore, has a role in plant defence mechanisms, helping to protect damaged plants against both bacterial and fungal disease.

It has been suggested that the quantity of catechol oxidase produced by a plant may be related to its susceptibility to fungal infection. Benzoquinone inhibits the growth of microorganisms and prevents damaged fruit from rotting.[2]

Catechol oxidase activity is also of economic importance. It has been estimated that half the world’s fruit and vegetable crop is lost due to post-harvest browning reactions due to the enzyme.


Catechol oxidase has been studied from sweet potatoes and assigned into a biological assembly. The catalytic copper center is accommodated in a central four-helix-bundle located in a hydrophobic pocket close to the surface. Both metal binding sites are composed of three histidine ligands. His 109, ligated to the CuA site, is covalently linked to Cys 92 by an unusual thioether bond.[3] An additional ligand component is Cu2O and contains a Cu-O-Cu linkage.[4]

New approaches on artificial enzymes design based on amino acids or peptides as characteristic molecular moieties have led to a significant expansion of the field of artificial enzymes or enzyme mimics. Recent results by the group of Rob Liskamp have shown that scaffolded histidine residues can be used as mimics of certain metalloproteins and -enzymes. Especially the structural mimicry of certain copper proteins (e.g. hemocyanin, tyrosinase and catechol oxidase), containing so-called type-3 copper binding sites, has been shown. This is a significant improvement since the use of scaffolded histidine residues is one step closer to the mimicry of enzymes by biological relevant species such as amino acids and peptides.[5]


  1. ^ "EC Catechol oxidase.". The European Bioinformatics Institute. 
  2. ^ Wahlert, John. H. "Enzymes - Proteins That Act as Catalysts". Baruch College. 
  3. ^ Kiabunde, T; Eicken, C.; Sacchettini, J.C.; Krebs, B. (1998). "CATECHOL OXIDASE FROM IPOMOEA BATATAS (SWEET POTATOES) IN THE NATIVE CU(II)-CU(II) STATE". Nature Structural & Molecular Biology 5. doi:10.1038/4193. 
  4. ^ Virador, V.M.; Reyes Grajeda, J.P.; Blanco-Labra, A.; Mendiola-Olaya, E.; Smith, G.M.; Moreno, A.; Whitaker, J.R. (2010). "Cloning, sequencing, purification, and crystal structure of Grenache (Vitis vinifera) polyphenol oxidase.". Journal of Agricultural and Food Chemistry 58: 1189–1201. doi:10.1021/jf902939q. 
  5. ^ Scaffolded amino acids as a close structural mimic of type-3 copper binding sites. H. Bauke Albada, Fouad Soulimani, Bert M. Weckhuysen and Rob M. J. Liskamp, Chem. Commun., 2007, pages 4895-4897, doi:10.1039/B709400K

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