Literature summary for 1.16.3.1 extracted from

Singh, S.K.; Roberts, S.A.; McDevitt, S.F.; Weichsel, A.; Wildner, G.F.; Grass, G.B.; Rensing, C.; Montfort, W.R.
Crystal structures of multicopper oxidase CueO bound to copper(I) and silver(I) functional role of a methionine-rich sequence (2011), J. Biol. Chem., 286, 37849-3757 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop method, crystal structure of CueO at 1.1 A with the 45-residue methionine-rich segment fully resolved, revealing an N-terminal helical segment with methionine residues juxtaposed for Cu(I) ligation and a C-terminal highly mobile segment rich in methionine and histidine residues. Structures of CueO with a C500S mutation, and CueO with six methionines changed to serine	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
C500S	mutation leads to loss of the T1 copper	Escherichia coli
M358S/M361S/M362S/M364S/M366S	mutation leads to an about 4fold reduction in kcat for Cu(I) oxidation	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
Ag+	strongly inhibits CueO oxidase activities in vitro	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.12	-	Fe(II)	pH 5.0, 23 °C, wild-type enzyme	Escherichia coli
0.135	-	Fe(II)	pH 5.0, 23 °C, mutant enzyme M358S/M361S/M362S/M364S/M366S	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu+	Cu(I) coordinates to a flexible, methionine-rich sequence	Escherichia coli
Cu2+	stimulates Fe(II) oxidase activity	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P36649	-	-
Escherichia coli K12	P36649	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4 Fe(II) + 4 H+ + O2	Cu(II) stimulated Fe(II) oxidase activity. The enzyme also oxidizes Cu+ and is required for copper homeostasis in Escherichia coli	Escherichia coli	4 Fe(III) + 2 H2O	-	?
4 Fe(II) + 4 H+ + O2	Cu(II) stimulated Fe(II) oxidase activity. The enzyme also oxidizes Cu+ and is required for copper homeostasis in Escherichia coli	Escherichia coli K12	4 Fe(III) + 2 H2O	-	?

Synonyms

Synonyms	Comment	Organism
multicopper oxidase CueO	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
23	-	assay at	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
1.7	-	Fe(II)	pH 5.0, 23 °C, mutant enzyme M358S/M361S/M362S/M364S/M366S	Escherichia coli
3.9	-	Fe(II)	pH 5.0, 23 °C, wild-type enzyme	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5	-	assay at	Escherichia coli

Expression

Organism	Comment	Expression
Escherichia coli	CueO is only expressed when copper ions are present	up

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Release 2023.1 (January 2023)