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Literature summary for 1.1.3.10 extracted from

  • Li, M.; Deng, H.; Ma, R.; Luo, H.; Yao, B.; Su, X.
    Biochemical and mutational analyses of a Trametes pyranose oxidase and comparison of its mutants in breadmaking (2018), AMB Express, 8, 38 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.3.10

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Trametes sp.

Protein Variants

Protein Variants Comment Organism
E539K increase in catalytic activity, shift in optimum temperature by 10 degrees Trametes sp.
K312E increase in catalytic activity Trametes sp.
K312E/E539K increase in catalytic activity, shift in optimum temperature by 10 degrees Trametes sp.
T166A/E539K increase in catalytic activity Trametes sp.

Inhibitors

Inhibitors Comment Organism Structure
Ag+ 5 mM, 95% of initial activity Trametes sp.
EDTA 5 mM, 85% of initial activity Trametes sp.
Fe2+ 5 mM, 11% of initial activity Trametes sp.
SDS 5 mM, complete loss of activity Trametes sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.5
-
 D-glucose mutant T166A/E539K, pH 6.5, 30°C Trametes sp.
0.6
-
 D-glucose mutant K312E/E539K, pH 6.5, 30°C Trametes sp.
0.7
-
 D-glucose mutant E359K, pH 6.5, 30°C Trametes sp.
0.8
-
 D-glucose mutant K312E, pH 6.5, 30°C Trametes sp.
1.2
-
 D-glucose wild-type, pH 6.5, 30°C Trametes sp.

Metals/Ions

Metals/Ions Comment Organism Structure
K+ 5 mM, 110% of initial activity Trametes sp.
Mg2+ 5 mM, 113% of initial activity Trametes sp.
Mn2+ 5 mM, 113% of initial activity Trametes sp.
Na+ 5 mM, 109% of initial activity Trametes sp.
Ni2+ 5 mM, 119% of initial activity Trametes sp.

Organism

Organism UniProt Comment Textmining
Trametes sp. A0A2P1MAF4
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4
-
 mutant T166A/E539K, pH 6.5, 30°C Trametes sp.
5.3
-
 mutant E359K, pH 6.5, 30°C Trametes sp.
6.2
-
 mutant K312E/E539K, pH 6.5, 30°C Trametes sp.
6.4
-
 wild-type, pH 6.5, 30°C Trametes sp.
10.2
-
 mutant K312E, pH 6.5, 30°C Trametes sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + O2
-
 Trametes sp. 2-dehydro-D-glucose + H2O2
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 wild-type and mutants K312E, T166A/E539K Trametes sp.
60
-
 mutant E359K, K312E/E539K Trametes sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.9
-
 D-glucose mutant T166A/E539K, pH 6.5, 30°C Trametes sp.
6.1
-
 D-glucose wild-type, pH 6.5, 30°C Trametes sp.
7.6
-
 D-glucose mutant E359K, pH 6.5, 30°C Trametes sp.
7.6
-
 D-glucose mutant K312E/E539K, pH 6.5, 30°C Trametes sp.
8.5
-
 D-glucose mutant K312E, pH 6.5, 30°C Trametes sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 mutant K312E Trametes sp.
6
-
 mutants E359K, K312E/E539K, T166A/E539K Trametes sp.
6.5
-
 wiild-type Trametes sp.

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.08
-
 D-glucose wild-type, pH 6.5, 30°C Trametes sp.
5.8
-
 D-glucose mutant T166A/E539K, pH 6.5, 30°C Trametes sp.
10.62
-
 D-glucose mutant K312E, pH 6.5, 30°C Trametes sp.
10.86
-
 D-glucose mutant E359K, pH 6.5, 30°C Trametes sp.
12.67
-
 D-glucose mutant K312E/E539K, pH 6.5, 30°C Trametes sp.