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CATH Superfamily 2.60.40.420

Cupredoxins - blue copper proteins

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:

"
Cupredoxins - blue copper proteins
".

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 23926: Multicopper oxidase, laccase

There are 3 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
Laccase. [EC: 1.10.3.2]
4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O.
  • A group of multi-copper proteins of low specificity.
  • Acts on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine.
  • The semiquinone may react further either enzymically or non- enzymically.
 570 A0A067NGQ1 A0A067NGQ1 A0A067NRU7 A0A067NRU7 A0A0A0Q492 A0A0A0Q492 A0A0A0Q5C2 A0A0A0Q5C2 A0A0A0Q5C7 A0A0A0Q5C7
(560 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.
 8 Q9HDS7 Q9HDS7 Q9HDS8 Q9HDS8 Q9HDS9 Q9HDS9 Q9UVU8 Q9UVU8
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.
 2 B5B8U2 B5B8U2
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