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Literature summary for 1.10.3.2 extracted from

  • Zhang, Y.; Dai, Z.; Zhang, S.; Yang, X.
    The catalytic properties of Thermus thermophilus SG0.5JP17-16 laccase were regulated by the conformational dynamics of pocket loop 6 (2021), Biochim. Biophys. Acta Gen. Subj., 1865, 129872 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Thermus thermophilus

Protein Variants

Protein Variants Comment Organism
D394E 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 Thermus thermophilus
D394M 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 Thermus thermophilus
D394R 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 Thermus thermophilus
D396A mutant enzyme with higher catalytic efficiency decolorizes the synthetic dye more efficiently than the wild-type enzyme Thermus thermophilus
D396E mutant enzyme with higher catalytic efficiency decolorizes the synthetic dye more efficiently than the wild-type enzyme Thermus thermophilus
D396M mutant enzyme with higher catalytic efficiency decolorizes the synthetic dye more efficiently than the wild-type enzyme Thermus thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.215
-
guaiacol pH 6.0, 90°C, mutant enzyme D394M Thermus thermophilus
0.243
-
guaiacol pH 6.0, 90°C, mutant enzyme D394R Thermus thermophilus
0.266
-
guaiacol pH 6.0, 90°C, mutant enzyme D394E Thermus thermophilus
0.325
-
guaiacol pH 6.0, 90°C, mutant enzyme D396A Thermus thermophilus
0.356
-
guaiacol pH 6.0, 90°C, mutant enzyme D396M Thermus thermophilus
0.382
-
guaiacol pH 6.0, 90°C, mutant enzyme D396E Thermus thermophilus
0.392
-
guaiacol pH 6.0, 90°C, mutant enzyme D396N Thermus thermophilus
0.407
-
guaiacol pH 6.0, 90°C, wild-type enzyme Thermus thermophilus
0.439
-
guaiacol pH 6.0, 90°C, mutant enzyme D394N Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
copper multicopper oxidase Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus F6DF14
-
-
Thermus thermophilus SG0.5JP17-16 F6DF14
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Congo Red + O2 the enzyme decolorizes the azo dye Thermus thermophilus ?
-
?
Congo Red + O2 the enzyme decolorizes the azo dye Thermus thermophilus SG0.5JP17-16 ?
-
?
guaiacol + O2
-
Thermus thermophilus 6-methoxycyclohexa-2,4-dienone + H2O
-
?
guaiacol + O2
-
Thermus thermophilus SG0.5JP17-16 6-methoxycyclohexa-2,4-dienone + H2O
-
?
Reactive Black B + O2 the enzyme decolorizes the azo dye Thermus thermophilus ?
-
?
Reactive Black B + O2 the enzyme decolorizes the azo dye Thermus thermophilus SG0.5JP17-16 ?
-
?
Reactive Black WNN + O2 the enzyme decolorizes the azo dye Thermus thermophilus ?
-
?
Reactive Black WNN + O2 the enzyme decolorizes the azo dye Thermus thermophilus SG0.5JP17-16 ?
-
?
Remazol Brilliant Blue R + O2 the enzyme decolorizes the anthraquinone dye Thermus thermophilus ?
-
?
Remazol Brilliant Blue R + O2 the enzyme decolorizes the anthraquinone dye Thermus thermophilus SG0.5JP17-16 ?
-
?

Synonyms

Synonyms Comment Organism
lacTT
-
Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
-
wild-type enzyme and mutant enzymes D394E, D394M and D394R Thermus thermophilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
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 Thermus thermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.8
-
guaiacol pH 6.0, 90°C, mutant enzyme D394R Thermus thermophilus
1.7
-
guaiacol pH 6.0, 90°C, mutant enzyme D394M Thermus thermophilus
3.3
-
guaiacol pH 6.0, 90°C, mutant enzyme D394E Thermus thermophilus
6.7
-
guaiacol pH 6.0, 90°C, mutant enzyme D396N Thermus thermophilus
6.9
-
guaiacol pH 6.0, 90°C, wild-type enzyme Thermus thermophilus
7.1
-
guaiacol pH 6.0, 90°C, mutant enzyme D396A Thermus thermophilus
7.3
-
guaiacol pH 6.0, 90°C, mutant enzyme D396M Thermus thermophilus
7.4
-
guaiacol pH 6.0, 90°C, mutant enzyme D394N Thermus thermophilus
7.4
-
guaiacol pH 6.0, 90°C, mutant enzyme D396E Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
wild-type enzyme Thermus thermophilus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.3
-
guaiacol pH 6.0, 90°C, mutant enzyme D394R Thermus thermophilus
7.9
-
guaiacol pH 6.0, 90°C, mutant enzyme D394M Thermus thermophilus
12.4
-
guaiacol pH 6.0, 90°C, mutant enzyme D394E Thermus thermophilus
16.8
-
guaiacol pH 6.0, 90°C, mutant enzyme D394N Thermus thermophilus
16.9
-
guaiacol pH 6.0, 90°C, wild-type enzyme Thermus thermophilus
17.1
-
guaiacol pH 6.0, 90°C, mutant enzyme D396N Thermus thermophilus
19.4
-
guaiacol pH 6.0, 90°C, mutant enzyme D396E Thermus thermophilus
20.5
-
guaiacol pH 6.0, 90°C, mutant enzyme D396M Thermus thermophilus
21.8
-
guaiacol pH 6.0, 90°C, mutant enzyme D396A Thermus thermophilus