A group of multi-copper proteins of low specificity acting on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. The semiquinone may react further either enzymically or non-enzymically.
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SYSTEMATIC NAME
IUBMB Comments
benzenediol:oxygen oxidoreductase
A group of multi-copper proteins of low specificity acting on both o- and p-quinols, and often acting also on aminophenols and phenylenediamine. The semiquinone may react further either enzymically or non-enzymically.
the purified enzyme is able to decolourize Green Dye, Orange Dye and Acid Red Dye. The enzyme is unable to decolourize NBB, RBB, or Congo Red. However, with 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate) (5 mM) acting as redox mediator, the enzyme decolourizes NBB, RBB, or Congo Red
the purified enzyme is able to decolourize Green Dye, Orange Dye and Acid Red Dye. The enzyme is unable to decolourize NBB, RBB, or Congo Red. However, with 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonate) (5 mM) acting as redox mediator, the enzyme decolourizes NBB, RBB, or Congo Red
the enzyme oxidizes a range of phenolic and nonphenolic compounds using molecular oxygen as an electron acceptor to produce water with a broad substrate specificity
the enzyme oxidizes a range of phenolic and nonphenolic compounds using molecular oxygen as an electron acceptor to produce water with a broad substrate specificity
the enzyme requires copper ions for activity. The dependence of the activity on Cu2+ concentration is sigmoidal with the midpoint at 0.00304 mM. Other metal ions (Mg2+, Mn2+, Ca2+, Ni2+, or Zn2+ each at 1 mM) fail to support the activity. The methionine-rich region from Met271 to Met283 may be involved in copper binding
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
two-domain-type by sitting-drop vapour-diffusion method, mixing of 0.001 ml of a protein solution, containing 8.5 mg/ml protein, with 0.001 ml of reservoir solution, containing 0.2 M potassium chloride, 0.05 M HEPES, pH 7.5, and 35% v/v pentaerythritol propoxylate, at 20°C, X-ray diffraction structure determination and analysis at 1.7 A resolution, single-wavelength anomalous diffraction technique using Cu atoms
mutation in T1 Cu site, incorporation of 3-4 copper atoms, similar to wild-type. Mutation results in an increase of 100 mV in the O2 reduction potential, while the enzymatic activity for ABTS oxidation is decreased
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 50%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 50%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0
mutant with the lower laccase activity displays a decreased decolorization efficiency as compared to the wild-type enzyme. Expressed in a lower level, about 16%, of the wild type enzyme. Optimum pH shifts towards the acidic value (0.5-1 units) relative to the wild type enzyme which has an optimal pH 6.0
1.6fold decrease in kcat/Km for the substrate guaiacol. 70% decrease in activity of mutant enzyme after 4 h at 80°C. 30% decrease in activity of wild-type enzyme after 4 h at 80°C
0-4 h, residual enzymatic activity decreases with the increase of the incubation time. The wild-type, K428M, K428E and K428R enzymes remain 70% of corresponding initial activity after incubated for 4 h. The K428L mutant is most affected, only 30% of the initial activity is retained after 4 h
4 h, wild-type enzymed retains 80% of its activity. The thermal stability of D394R mutant decreases significantly, with the residual activity of 15% after 4 h
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
by signal peptide prediction, the enzyme is assumed to be a secretory protein starting from Gln23. The DNA encoding the mature protein is then cloned and expressed in Escherichia coli BL21 (DE3). The recombinant enzyme, expressed as an apoprotein, is dialyzed against copper-containing buffer to yield a holoprotein
the enzyme may be used in a variety of biotechnological applications, including textile dye bleaching, pulp bleaching, bioremediation, polymer synthesis and biosensors