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Literature summary for 1.10.3.2 extracted from

  • Trubitsina, L.I.; Tishchenko, S.V.; Gabdulkhakov, A.G.; Lisov, A.V.; Zakharova, M.V.; Leontievsky, A.A.
    Structural and functional characterization of two-domain laccase from Streptomyces viridochromogenes (2015), Biochimie, 112, 151-159 .
    View publication on PubMed

Application

Application Comment Organism
environmental protection laccase can be efficiently used to decolorize synthetic dye and help in waste water treatment. The enzyme can also be considered as a candidate for treating industrial effluent containing malachite green Streptomyces viridochromogenes

Cloned(Commentary)

Cloned (Comment) Organism
overproduced in Escherichia coli Streptomyces viridochromogenes

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion method, X-ray quality crystals are generated and the structure is solved to a resolution of 2.4 A Streptomyces viridochromogenes

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
Streptomyces viridochromogenes
additional information the enzyme is resistant to specific inhibitors of copper-containing oxidases, such as NaN3 and NaF Streptomyces viridochromogenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.3
-
guaiacol pH 8.5, temperature not specified in the publication Streptomyces viridochromogenes
0.38
-
2,6-dimethoxyphenol pH 8.5, temperature not specified in the publication Streptomyces viridochromogenes
4.5
-
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) pH 4.0, temperature not specified in the publication Streptomyces viridochromogenes
9.9
-
K4[Fe(CN)6] pH 4.0, temperature not specified in the publication Streptomyces viridochromogenes

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm the recombinant protein is found in the cytoplasmic fraction Streptomyces viridochromogenes 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ copper-containing enzyme. Contains 4 atoms per molecule of the enzyme Streptomyces viridochromogenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
88000 90000 gel filtration Streptomyces viridochromogenes

Organism

Organism UniProt Comment Textmining
Streptomyces viridochromogenes J9S5G3
-
-
Streptomyces viridochromogenes VKM Ac-629 J9S5G3
-
-

Storage Stability

Storage Stability Organism
20°C, 2 days, pH 6.0-10.0, the enzyme retains about 70% residual activity Streptomyces viridochromogenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
-
Streptomyces viridochromogenes ?
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) + O2
-
Streptomyces viridochromogenes VKM Ac-629 ?
-
?
2,6-dimethoxyphenol + O2
-
Streptomyces viridochromogenes ?
-
?
2,6-dimethoxyphenol + O2
-
Streptomyces viridochromogenes VKM Ac-629 ?
-
?
guaiacol + O2
-
Streptomyces viridochromogenes ?
-
?
guaiacol + O2
-
Streptomyces viridochromogenes VKM Ac-629 ?
-
?
K4[Fe(CN)6] + O2
-
Streptomyces viridochromogenes ?
-
?
additional information phenolic compounds are oxidized in the presence of the enzyme under alkaline but not acidic conditions. Conversely, nonphenolic compounds are oxidized at acidic but not alkaline pH. The enzyme catalyses oxidation of nonphenolic compounds more efficiently than that of phenols. The two-domain laccase displays a cytochrome c oxidase activity and exhibits no ferroxidase activity Streptomyces viridochromogenes ?
-
?
additional information phenolic compounds are oxidized in the presence of the enzyme under alkaline but not acidic conditions. Conversely, nonphenolic compounds are oxidized at acidic but not alkaline pH. The enzyme catalyses oxidation of nonphenolic compounds more efficiently than that of phenols. The two-domain laccase displays a cytochrome c oxidase activity and exhibits no ferroxidase activity Streptomyces viridochromogenes VKM Ac-629 ?
-
?

Subunits

Subunits Comment Organism
homotrimer 3 * 33900, calculated from sequence Streptomyces viridochromogenes
homotrimer 3 * 39000, SDS-PAGE after boiling Streptomyces viridochromogenes

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.2
-
K4[Fe(CN)6] pH 4.0, temperature not specified in the publication Streptomyces viridochromogenes
1.9
-
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) pH 4.0, temperature not specified in the publication Streptomyces viridochromogenes
8
-
guaiacol pH 8.5, temperature not specified in the publication Streptomyces viridochromogenes
34.4
-
2,6-dimethoxyphenol pH 8.5, temperature not specified in the publication Streptomyces viridochromogenes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
-
below, substrate: 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) Streptomyces viridochromogenes
8.5
-
substrate: 2,6-dimethoxyphenol Streptomyces viridochromogenes

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
phenolic compounds are oxidized in the presence of the enzyme under alkaline but not acidic conditions. Conversely, nonphenolic compounds are oxidized at acidic but not alkaline pH Streptomyces viridochromogenes

pH Stability

pH Stability pH Stability Maximum Comment Organism
2
-
20°C, 2 days, the enzyme retains about 30% residual activity Streptomyces viridochromogenes
3
-
20°C, 2 days, the enzyme retains about 42% residual activity Streptomyces viridochromogenes
4
-
20°C, 2 days, the enzyme retains about 65-60% residual activity Streptomyces viridochromogenes
5
-
20°C, 2 days, the enzyme retains about 65-60% residual activity Streptomyces viridochromogenes
6 10 20°C, 2 days, the enzyme retains about 70% residual activity Streptomyces viridochromogenes

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
8
-
pH 8.5, temperature not specified in the publication Streptomyces viridochromogenes EDTA
14
-
pH 4.0, temperature not specified in the publication Streptomyces viridochromogenes EDTA

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.02
-
K4[Fe(CN)6] pH 4.0, temperature not specified in the publication Streptomyces viridochromogenes
0.42
-
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid) pH 4.0, temperature not specified in the publication Streptomyces viridochromogenes
26.6
-
guaiacol pH 8.5, temperature not specified in the publication Streptomyces viridochromogenes
90.5
-
2,6-dimethoxyphenol pH 8.5, temperature not specified in the publication Streptomyces viridochromogenes