Literature summary for 1.10.3.2 extracted from

Wang, H.; Liu, X.; Zhao, J.; Yue, Q.; Yan, Y.; Gao, Z.; Dong, Y.; Zhang, Z.; Fan, Y.; Tian, J.; Wu, N.; Gong, Y.
Crystal structures of multicopper oxidase CueO G304K mutant structural basis of the increased laccase activity (2018), Sci. Rep., 8, 14252 .

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of G304K mutant at 1.49 A resolution. The mutant shows dramatic conformational changes in methionine-rich helix and the relative regulatory loop. In the structure of Cu-soaked enzyme, the addition of Cu ions induces further conformational changes in the regulatory loop and methionine-rich helix as a result of the new Cu-binding sites on the enzyme's surface	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
G304K	mutant shows about 2.7fold increased the laccase activity. Movements of the regulatory loop combined with the changes of the methionine-rich region may uncover the T1 Cu site allowing greater access of the substrate	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.88	-	2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)	mutant G304K, pH 5.5, 25°C	Escherichia coli
3.79	-	2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonate)	wild-type, pH 5.5, 25°C	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P36649	bifunctional copper oxidase and laccase, cf. EC 1.16.3.4	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
CueO	-	Escherichia coli
YacK	-	Escherichia coli

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Release 2023.1 (January 2023)