ExplorEnz: EC 1.16.3.4

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1.16.3.4

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 1.10.3.2). 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

References:

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]

[EC 1.16.3.4 created 2021]