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Literature summary extracted from

  • Ertan, H.; Siddiqui, K.S.; Muenchhoff, J.; Charlton, T.; Cavicchioli, R.
    Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidase using isothermal titration calorimetry: Insight into manganese peroxidase activation and lignin peroxidase inhibition (2012), Biochimie, 94, 1221-1231.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.14 0.013
-
 methylene blue lignine peroxidas activity, pH 3.5, 25°C Bjerkandera adusta
1.11.1.16 0.007
-
 methylene blue manganese peroxidase activity, pH 4.5, 25°C Bjerkandera adusta
1.11.1.16 0.013
-
 methylene blue lignine peroxidas activity, pH 3.5, 25°C Bjerkandera adusta

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.14 Mn2+ activity of manganese peroxidase progressively increases with concentration of Mn2+ to a maximum at about 1.8 mM, with a corresponding decrease in lignin peroxidase activity to less than 10% Bjerkandera adusta
1.11.1.16 Mn2+ activity of manganese peroxidase progressively increases with concentration of Mn2+ to a maximum at about 1.8 mM, with a corresponding decrease in lignin peroxidase activity to less than 10% Bjerkandera adusta

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.14 Bjerkandera adusta
-
-
-
1.11.1.16 Bjerkandera adusta
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.14 3-methyl-2-benzothiazolinone hydrazone + H2O2 enzyme has several substrate binding sites for 3-methyl-2-benzothiazolinone hydrazone, in addition to low and high affinity binding sites for Mn2+ Bjerkandera adusta ? + H2O
-
 ?
1.11.1.14 methylene blue + H2O2
-
 Bjerkandera adusta ? + H2O
-
 ?
1.11.1.14 additional information manganese peroxidase activity is more efficient than lignin peroxidase activity, with activity increasing with increasing concentrations of Mn2+ due to a second metal binding site involved in homotropic substrate Mn2+ activation. The activation of maganese peroxidase is also accompanied by a decrease in both activation energy and substrate Mn2+ affinity Bjerkandera adusta ?
-
 ?
1.11.1.16 3-methyl-2-benzothiazolinone hydrazone + H2O2 enzyme has several substrate binding sites for 3-methyl-2-benzothiazolinone hydrazone, in addition to low and high affinity binding sites for Mn2+ Bjerkandera adusta ? + H2O
-
 ?
1.11.1.16 methylene blue + H2O2
-
 Bjerkandera adusta ? + H2O
-
 ?
1.11.1.16 additional information manganese peroxidase activity is more efficient than lignin peroxidase activity, with activity increasing with increasing concentrations of Mn2+ due to a second metal binding site involved in homotropic substrate Mn2+ activation. The activation of maganese peroxidase is also accompanied by a decrease in both activation energy and substrate Mn2+ affinity Bjerkandera adusta ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.11.1.14 40
-
 lignin peroxidase activity in absence of Mn2+ Bjerkandera adusta
1.11.1.16 40
-
 lignin peroxidase activity in absence of Mn2+ Bjerkandera adusta
1.11.1.16 60
-
 manganese peroxidase activity Bjerkandera adusta

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.11.1.14 0.18
-
 methylene blue lignin peroxidase activity, pH 3.5, 25°C Bjerkandera adusta
1.11.1.16 0.18
-
 methylene blue lignin peroxidase activity, pH 3.5, 25°C Bjerkandera adusta
1.11.1.16 2.92
-
 methylene blue manganese peroxidase activity, pH 4.5, 25°C Bjerkandera adusta

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.14 3 3.5 lignin peroxidase activity in absence of Mn2+ Bjerkandera adusta
1.11.1.16 3 3.5 lignin peroxidase activity in absence of Mn2+ Bjerkandera adusta
1.11.1.16 4.5
-
 manganese peroxidase activity Bjerkandera adusta