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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 2204: Polyphenol oxidase F, chloroplastic

There are 5 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
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.
 60 A0A0B2P1N0 A0A0B2P669 A0A0B2PDF7 A0A0B2PGN9 A0A0B2PHV4 A0A0B2PIC8 A0A0B2PLU0 A0A0B2RGX4 A0A0B2SNE1 A0A0B2SNW5
(50 more...)
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.
 19 A0A059UAM0 A0A110AXN9 B0LLV3 B9VNV4 C5MRF7 C5MRF8 D2CVT3 D2SMN2 F5CEP1 I7BG84
(9 more...)
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.
 12 B3WFP2 B9VU65 F8V189 F8V190 G4U402 G4U403 G4U404 U3UB68 U3UB71 U3UB75
(2 more...)
Aureusidin synthase. [EC: 1.21.3.6]
(1) 2',4,4',6'-tetrahydroxychalcone 4'-O-beta-glucoside + O(2) = aureusidin 6-O-beta-glucoside + H(2)O. (2) 2 2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-glucoside + O(2) = 2 aureusidin 6-O-beta-glucoside + 2 H(2)O. (3) 2',3,4,4',6'-pentahydroxychalcone 4'-O-beta-glucoside + O(2) = bracteatin 6-O-beta-glucoside + H(2)O.
  • Plays a key role in the yellow coloration of flowers such as Antirrhinum majus (snapdragon).
  • The enzyme is a homolog of plant polyphenol oxidase and catalyzes two separate chemical transformations, i.e. 3-hydroxylation and oxidative cyclization (2',-dehydrogenation).
  • H(2)O(2) activates reaction (1) but inhibits reaction (2).
  • Originally considered to act on the phenol but now thought to mainly act on the 4'-O-beta-glucoside in vivo.
 1 Q9FRX6
(+)-larreatricin hydroxylase. [EC: 1.14.99.47]
(+)-larreatricin + O(2) + AH(2) = (+)-3'-hydroxylarreatricin + A + H(2)O.
  • Isolated from the plant Larrea tridentata (creosote bush).
  • The enzyme has a strong preference for the 3' position of (+)- larreatricin.
 1 Q6UIL3
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