The Enzyme Database

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Accepted name: cuproxidase
Reaction: 4 Cu+ + 4 H+ + O2 = 4 Cu2+ + 2 H2O
Other name(s): cueO (gene name); cuprous oxidase; Cu(I) oxidase; copper efflux oxidase
Systematic name: copper(I):oxygen oxidoreductase
Comments: 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 However, in vivo this site is occupied by a copper(I) ion and the enzyme functions as a cuprous oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Kim, C., Lorenz, W.W., Hoopes, J.T. and Dean, J.F. Oxidation of phenolate siderophores by the multicopper oxidase encoded by the Escherichia coli yacK gene. J. Bacteriol. 183 (2001) 4866–4875. [DOI] [PMID: 11466290]
2.  Grass, G. and Rensing, C. CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli. Biochem. Biophys. Res. Commun. 286 (2001) 902–908. [DOI] [PMID: 11527384]
3.  Outten, F.W., Huffman, D.L., Hale, J.A. and O'Halloran, T.V. The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J. Biol. Chem. 276 (2001) 30670–30677. [DOI] [PMID: 11399769]
4.  Roberts, S.A., Weichsel, A., Grass, G., Thakali, K., Hazzard, J.T., Tollin, G., Rensing, C. and Montfort, W.R. Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli. Proc. Natl. Acad. Sci. USA 99 (2002) 2766–2771. [DOI] [PMID: 11867755]
5.  Roberts, S.A., Wildner, G.F., Grass, G., Weichsel, A., Ambrus, A., Rensing, C. and Montfort, W.R. A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO. J. Biol. Chem. 278 (2003) 31958–31963. [DOI] [PMID: 12794077]
6.  Singh, S.K., Grass, G., Rensing, C. and Montfort, W.R. Cuprous oxidase activity of CueO from Escherichia coli. J. Bacteriol. 186 (2004) 7815–7817. [DOI] [PMID: 15516598]
7.  Galli, I., Musci, G. and Bonaccorsi di Patti, M.C. Sequential reconstitution of copper sites in the multicopper oxidase CueO. J. Biol. Inorg. Chem. 9 (2004) 90–95. [DOI] [PMID: 14648285]
8.  Djoko, K.Y., Chong, L.X., Wedd, A.G. and Xiao, Z. Reaction mechanisms of the multicopper oxidase CueO from Escherichia coli support its functional role as a cuprous oxidase. J. Am. Chem. Soc. 132 (2010) 2005–2015. [DOI] [PMID: 20088522]
9.  Singh, S.K., Roberts, S.A., McDevitt, S.F., Weichsel, A., Wildner, G.F., Grass, G.B., Rensing, C. and Montfort, W.R. Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I): functional role of a methionine-rich sequence. J. Biol. Chem. 286 (2011) 37849–37857. [DOI] [PMID: 21903583]
10.  Cortes, L., Wedd, A.G. and Xiao, Z. The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli. Metallomics 7 (2015) 776–785. [DOI] [PMID: 25679350]
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