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Literature summary for 1.10.3.2 extracted from

  • Kataoka, K.; Hirota, S.; Maeda, Y.; Kogi, H.; Shinohara, N.; Sekimoto, M.; Sakurai, T.
    Enhancement of laccase activity through the construction and breakdown of a hydrogen bond at the type I copper center in Escherichia coli CueO and the deletion mutant Deltaalpha5-7 CueO (2011), Biochemistry, 50, 558-565 .
    View publication on PubMed
Search for more literature for 1.10.3.2

Protein Variants

Protein Variants Comment Organism
D439A positive shift in the redox potential of this copper center and enhanced oxidase activity Escherichia coli
additional information mutations at Pro444 to construct a second NH-S hydrogen bond between the backbone amide and coordinating Cys500 thiolate of the type I copper result in positive shifts in the redox potential of this copper center and enhanced oxidase activity in CueO. Pro444 mutations limit the incorporation of copper ions into the trinuclear copper center. The activities of both CueO and the region Pro357-His406 deletion mutant are also enhanced by mutations to break down the hydrogen bond between the imidazole group of His443 that is coordinated to the type I copper and the beta-carboxy group of Asp439 that is located in the outer sphere of the type I copper center. The characteristics of the Cu(II)-S(Cys) bond are only minimally perturbed by mutations involving formation or disruption of a hydrogen bond from the coordinating groups to the type I copper Escherichia coli
P444A positive shift in the redox potential of this copper center and enhanced oxidase activity Escherichia coli
P444A/D439A mutation leads to a synergetic effect of the positive shift in the redox potential of the type I copper center and the increase in enzyme activity Escherichia coli
P444G mutation results in positive shifts in the redox potential of this copper center and enhanced oxidase activity in CueO and in the region Pro357-His406 deletion mutant lacking a methionine-rich helical segment that covers the substrate-binding site Escherichia coli
P444I positive shift in the redox potential of this copper center and enhanced oxidase activity Escherichia coli
P444L positive shift in the redox potential of this copper center and enhanced oxidase activity 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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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
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 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.98
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) wild-type, pH 5.5, 25°C Escherichia coli
5.7
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) mutant P444I, pH 5.5, 25°C Escherichia coli
8.7
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) mutant P444A, pH 5.5, 25°C Escherichia coli
10
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) mutant P444L, pH 5.5, 25°C Escherichia coli
15
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) region Pro357-His406 deletion plus D439A/P444A mutant, pH 5.5, 25°C Escherichia coli
17
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) mutant D439A, pH 5.5, 25°C Escherichia coli
17
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) region Pro357-His406 deletion plus P444A mutant, pH 5.5, 25°C Escherichia coli
23
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) region Pro357-His406 deletion plus P444A mutant, pH 5.5, 25°C Escherichia coli
38
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) region Pro357-His406 deletion mutant, pH 5.5, 25°C Escherichia coli
40
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) mutant D439A/P444A, pH 5.5, 25°C Escherichia coli
50
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) region Pro357-His406 deletion plus P444G mutant, pH 5.5, 25°C Escherichia coli
147
-
 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate) region Pro357-His406 deletion plus D439A mutant, pH 5.5, 25°C Escherichia coli