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CATH Superfamily 1.10.1280.10

Di-copper center containing domain from catechol oxidase

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Di-copper center containing domain from catechol oxidase
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 2225: Pro-phenol oxidase subunit 1

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Tyrosinase. [EC: 1.14.18.1]
(1) 2 L-dopa + O(2) = 2 dopaquinone + 2 H(2)O. (2) L-tyrosine + O(2) = dopaquinone + H(2)O.
  • Found in a broad variety of bacteria, fungi, plants, insects, crustaceans, and mammals, which is involved in the synthesis of betalains and melanin.
  • The enzyme, which is activated upon binding molecular oxygen, can catalyze both a monophenolase reaction cycle or a diphenolase reaction cycle.
  • 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.
  • The enzyme remains in an inactive deoxy state, and is restored to the active oxy state by the binding of a new oxygen molecule.
  • 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.
  • The enzyme then binds a second diphenol molecule and repeats the process, ending in a deoxy state.
  • The second reaction is identical to that catalyzed by the related enzyme catechol oxidase (EC 1.10.3.1).
  • However, the latter can not catalyze the hydroxylation or monooxygenation of monophenols.
  • Formerly EC 1.14.17.2.
 33 A0A1B2G381 A0A1B2G385 A7WPD2 A8JKF6 C6K2H4 D2KBI1 D6QZJ9 E0AEY7 E0VUB6 E0VX48
(23 more...)
Catechol oxidase. [EC: 1.10.3.1]
2 catechol + O(2) = 2 1,2-benzoquinone + 2 H(2)O.
  • A type 3 copper protein that catalyzes exclusively the oxidation of catechols (i.e., o-diphenols) to the corresponding o-quinones.
  • The enzyme also acts on a variety of substituted catechols.
  • It is different from tyrosinase, EC 1.14.18.1, which can catalyze both the monooxygenation of monophenols and the oxidation of catechols.
 3 Q49I38 Q49I39 Q7K2W6