In molecular biology, multicopper oxidases are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre; dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water.[1] There are three spectroscopically different copper centres found in multicopper oxidases: type 1 (or blue), type 2 (or normal) and type 3 (or coupled binuclear).[2][3] Multicopper oxidases consist of 2, 3 or 6 of these homologous domains, which also share homology with the cupredoxins azurin and plastocyanin. Structurally, these domains consist of a cupredoxin-like fold, a beta-sandwich consisting of 7 strands in 2 beta-sheets, arranged in a Greek-key beta-barrel.[4]
Multicopper oxidase (type 1) | |||||||||
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Identifiers | |||||||||
Symbol | Cu-oxidase | ||||||||
Pfam | PF00394 | ||||||||
Pfam clan | CL0026 | ||||||||
InterPro | IPR001117 | ||||||||
PROSITE | PDOC00076 | ||||||||
SCOP2 | 1aoz / SCOPe / SUPFAM | ||||||||
Membranome | 253 | ||||||||
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Multicopper oxidase (type 2) | |||||||||
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Identifiers | |||||||||
Symbol | Cu-oxidase_2 | ||||||||
Pfam | PF07731 | ||||||||
Pfam clan | CL0026 | ||||||||
InterPro | IPR011706 | ||||||||
SCOP2 | 1aoz / SCOPe / SUPFAM | ||||||||
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Multicopper oxidase (type 3) | |||||||||
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Identifiers | |||||||||
Symbol | Cu-oxidase_3 | ||||||||
Pfam | PF07732 | ||||||||
Pfam clan | CL0026 | ||||||||
InterPro | IPR011707 | ||||||||
SCOP2 | 1aoz / SCOPe / SUPFAM | ||||||||
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CMulti-copper polyphenol oxidoreductase laccase | |||||||||
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Identifiers | |||||||||
Symbol | Cu-oxidase_4 | ||||||||
Pfam | PF02578 | ||||||||
InterPro | IPR003730 | ||||||||
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The family of multicopper oxidases can be divided into three groups based on the electron-donating substrate. [5] Laccases oxidize a variety of organic substrates, metalloxidases accept metal substrates and a third group contains multicopper oxidases that are specific towards one single substrate. Multicopper oxidases include:
In addition to the above enzymes there are a number of other proteins that are similar to the multi-copper oxidases in terms of structure and sequence, some of which have lost the ability to bind copper. These include: copper resistance protein A (copA) from a plasmid in Pseudomonas syringae; domain A of (non-copper binding) blood coagulation factors V (Fa V) and VIII (Fa VIII);[8] yeast Fet3p (FET3) required for ferrous iron uptake;[9] yeast hypothetical protein YFL041w; and the fission yeast homologue SpAC1F7.08.