Parent Class:

EC-Numbers → 1 -- Oxidoreductases → 1.16 -- Oxidizing metal ions → 1.16.3 -- With oxygen as acceptor

Synonyms: cuprous oxidase, Cu(I) oxidase, copper efflux oxidase, cueO (gene name)

Systematic Name: copper(I):oxygen oxidoreductase

Unification Links: BRENDA:1.16.3.4, ENZYME:1.16.3.4, IUBMB-ExplorEnz:1.16.3.4

Reaction:
4 Cu⁺_[periplasm] + 4 H⁺_[periplasm] + dioxygen_[periplasm] → 4 Cu²⁺_[periplasm] + 2 H₂O_[periplasm]

Enzymes and Genes:
multicopper oxidase CueO: cueO ( Escherichia coli K-12 substr. MG1655 )

Summary:
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. However, in vivo this site is occupied by a copper(I) ion and the enzyme functions as a cuprous oxidase.

Citations: [Kim01, Grass01, Outten01, Roberts02, Roberts03, Singh04, Galli04, Djoko10, Singh11, Cortes15]

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References

Cortes15: Cortes L, Wedd AG, Xiao Z (2015). "The functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli." Metallomics 7(5);776-85. PMID: 25679350

Djoko10: Djoko KY, Chong LX, Wedd AG, Xiao Z (2010). "Reaction mechanisms of the multicopper oxidase CueO from Escherichia coli support its functional role as a cuprous oxidase." J Am Chem Soc 132(6);2005-15. PMID: 20088522

Galli04: Galli I, Musci G, Bonaccorsi di Patti MC (2004). "Sequential reconstitution of copper sites in the multicopper oxidase CueO." J Biol Inorg Chem 9(1);90-5. PMID: 14648285

Grass01: Grass G, Rensing C (2001). "CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli." Biochem Biophys Res Commun 286(5);902-8. PMID: 11527384

Kim01: Kim C, Lorenz WW, Hoopes JT, Dean JF (2001). "Oxidation of phenolate siderophores by the multicopper oxidase encoded by the Escherichia coli yacK gene." J Bacteriol 183(16);4866-75. PMID: 11466290

Outten01: Outten FW, Huffman DL, Hale JA, O'Halloran TV (2001). "The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli." J Biol Chem 276(33);30670-7. PMID: 11399769

Roberts02: Roberts SA, Weichsel A, Grass G, Thakali K, Hazzard JT, Tollin G, Rensing C, Montfort WR (2002). "Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli." Proc Natl Acad Sci U S A 99(5);2766-71. PMID: 11867755

Roberts03: Roberts SA, Wildner GF, Grass G, Weichsel A, Ambrus A, Rensing C, Montfort WR (2003). "A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO." J Biol Chem 278(34):31958-63. PMID: 12794077

Singh04: Singh SK, Grass G, Rensing C, Montfort WR (2004). "Cuprous Oxidase Activity of CueO from Escherichia coli." J Bacteriol 186(22);7815-7. PMID: 15516598

Singh11: Singh SK, Roberts SA, McDevitt SF, Weichsel A, Wildner GF, Grass GB, Rensing C, Montfort WR (2011). "Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I): functional role of a methionine-rich sequence." J Biol Chem 286(43);37849-57. PMID: 21903583

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 46(D1):D633-D639 2018
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