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Literature summary for 1.10.3.2 extracted from

  • Kajikawa, T.; Kataoka, K.; Sakurai, T.
    Modifications on the hydrogen bond network by mutations of Escherichia coli copper efflux oxidase affect the process of proton transfer to dioxygen leading to alterations of enzymatic activities (2012), Biochem. Biophys. Res. Commun., 422, 152-156 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D507A about 10% increase in specific activity activity Escherichia coli
D507N about 80% increase in specific activity activity Escherichia coli
E506A mutation results in the formation of a compensatory hydrogen bond network with one or two extra water molecules Escherichia coli
E506D about 20% decrease in specific activity activity Escherichia coli
E506I mutation results in the complete shutdown of the hydrogen bond network leading to loss of enzymatic activities Escherichia coli
E506Q mutation results in the hydrogen bond network without the proton transport function Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P36649 bifunctional copper oxidase and laccase, cf. EC 1.16.3.4
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.052
-
wild-type, phosphate buffer, pH 6, 25°C Escherichia coli
0.14
-
wild-type, citrate buffer, pH 5.5, 25°C Escherichia coli
0.42
-
wild-type, acetate buffer, pH 5.5, 25°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) + O2
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Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
CueO
-
Escherichia coli
YacK
-
Escherichia coli