1.16.3.4: cuproxidase
This is an abbreviated version!
For detailed information about cuproxidase, go to the full flat file.
Word Map on EC 1.16.3.4
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1.16.3.4
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multicopper
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laccase
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oxidases
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methionine-rich
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trinuclear
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2,6-dimethoxyphenol
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dioxygen
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bioelectrocatalysis
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ferroxidase
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cathodic
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ceruloplasmin
- 1.16.3.4
-
multicopper
- laccase
-
oxidases
-
methionine-rich
-
trinuclear
- 2,6-dimethoxyphenol
- dioxygen
-
bioelectrocatalysis
- ferroxidase
-
cathodic
- ceruloplasmin
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
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General Information on EC 1.16.3.4 - cuproxidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
metabolism
the three copper sites play related but distinct roles in CueO oxidase activities. The internal Cu5 site is part of the essential electron transfer pathway connecting surface-exposed sites Cu6 and Cu7 to site T1. Both Cu6 and Cu7 are dominant substrate-docking-oxidation sites on the protein surface. The two surface-exposed sites Cu6 and Cu7 are the direct substrate-docking-oxidation sites for both oxidase functions and buried site Cu5 channels electrons from the oxidations to the Type 1 site of the multicopper oxidase machinery
physiological function
physiological function
presence of CueO in the periplasm protects alkaline phosphatase from copper-induced damage
physiological function
Salmonella typhimurium CueO mutant is more sensitive to copper ions than wild-type. In a murine model of infection, the CueO mutant is significantly attenuated, although there is no significant difference in recovery from Peyer's patches and mesenteric lymph nodes. The intracellular survival of the CueO mutant in unprimed or gamma-interferon-primed murine macrophages is not statistically different from that of wild-type Salmonella typhimurium. The CueO mutant does not show greater sensitivity to hydrogen peroxide and its sensitivity to copper ions is not affected by siderophores
physiological function
the cue pathway, which includes a copper exporter, CopA, and a periplasmic oxidase, CueO, is the primary aerobic system for copper tolerance. During anaerobic growth, however, copper toxicity increases, and the independent cus copper exporter is also necessary for full copper tolerance. Oxidase activity is abolished in the strain lacking CueO regardless of the presence of added copper, deletion of CueO does not affect copper sensitivity relative to that of wild-type strains
physiological function
the enzyme is required for copper homeostasis in Escherichia coli
physiological function
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
physiological function
the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
physiological function
when expressed in an Escherichia coli CueO knock-out strain, enzyme exhibits phenol oxidase activity in vivo and enhances the copper tolerance of the strain
physiological function
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Salmonella typhimurium CueO mutant is more sensitive to copper ions than wild-type. In a murine model of infection, the CueO mutant is significantly attenuated, although there is no significant difference in recovery from Peyer's patches and mesenteric lymph nodes. The intracellular survival of the CueO mutant in unprimed or gamma-interferon-primed murine macrophages is not statistically different from that of wild-type Salmonella typhimurium. The CueO mutant does not show greater sensitivity to hydrogen peroxide and its sensitivity to copper ions is not affected by siderophores
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physiological function
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the enzyme is required for iron homeostasis. It also plays a major role in maintaining the cuprous/cupric redox balance
-
physiological function
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the enzyme is required for copper homeostasis in Escherichia coli
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