1.16.3.4: cuproxidase

This is an abbreviated version!
For detailed information about cuproxidase, go to the full flat file.

Reaction

4 Cu+ + 4 H+ +

Synonyms

ceruloplasmin, copper efflux oxidase, Cu(I) oxidase, CueO, CuiD, cuprous oxidase, DA2_0547, fet3p, More, multicopper oxidase, multicopper oxidase CueO, YacK

ECTree

     1 Oxidoreductases

         1.16 Oxidizing metal ions

             1.16.3 With oxygen as acceptor

                1.16.3.4 cuproxidase

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1	Activating Compound
6	AA Sequence
9	Cloned(Commentary)
7	Crystallization (Commentary)
3	Expression
11	General Information
3	Inhibitors
6	kcat/KM [mM/s]
2	Ki Value [mM]
23	KM Value [mM]
5	Localization
10	Metals/Ions
2	Molecular Weight [Da]
6	Natural Substrates/ Products (Substrates)
28	Organism
5	pH Optimum
1	pH Range
41	Protein Variants
2	Purification (Commentary)
1	Reaction
28	Reference
2	Renatured (Commentary)
8	Specific Activity [micromol/min/mg]
34	Substrates and Products (Substrate)
1	Subunits
36	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
3	Temperature Stability [°C]
17	Turnover Number [1/s]

Systematic Name

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Systematic Name on EC 1.16.3.4 - cuproxidase

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SYSTEMATIC NAME

IUBMB Comments

copper(I):oxygen oxidoreductase

The enzyme, characterized from the bacterium Escherichia coli, is involved in copper tolerance under aerobic conditions. The enzyme contains a substrate binding (type 1) copper site and a trinuclear copper center (consisting of type 2 and type 3 copper sites) in which oxygen binding and reduction takes place. It also contains a methionine rich region that can bind additional copper ions. In vitro, if the substrate binding site is occupied by copper(II), the enzyme can function as a laccase-type quinol oxidase (EC 1.10.3.2). However, in vivo this site is occupied by a copper(I) ion and the enzyme functions as a cuprous oxidase.