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Literature summary for 1.3.3.5 extracted from

  • Tasca, F.; Farias, D.; Castro, C.; Acuna-Rougier, C.; Antiochia, R.
    Bilirubin oxidase from Myrothecium verrucaria physically absorbed on graphite electrodes. Insights into the alternative resting form and the sources of activity loss (2015), PLoS ONE, 10, e0132181 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.3.5

Activating Compound

Activating Compound Comment Organism Structure
additional information the enzyme needs to be fully reduced before it gets activated for catalysis Albifimbria verrucaria

Application

Application Comment Organism
synthesis mediator-less, direct electro-catalytic reduction of oxygen to water is achieved on spectrographite electrodes modified by physical adsorption of bilirubin oxidases from Myrothecium verrucaria. Bilirubin oxidase (BOD) is the best catalyst for converting oxygen directly to water because of the very low overpotential necessary to catalyze the reaction Albifimbria verrucaria

Protein Variants

Protein Variants Comment Organism
additional information mediator-less, direct electro-catalytic reduction of oxygen to water is achieved on spectrographite electrodes modified by physical adsorption of bilirubin oxidases from Myrothecium verrucaria. The existence of an alternative resting form of the enzyme is validated. Effects on the catalytic cycle by temperature, pH and the presence of halogens in the buffer, overview Albifimbria verrucaria

Inhibitors

Inhibitors Comment Organism Structure
chloride might inhibit the enzyme Albifimbria verrucaria
hydrogen peroxide
-
 Albifimbria verrucaria

Metals/Ions

Metals/Ions Comment Organism Structure
copper four copper atoms per enzyme molecule Albifimbria verrucaria

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 bilirubin + O2 Albifimbria verrucaria
-
 2 biliverdin + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Albifimbria verrucaria Q12737
-
-

Reaction

Reaction Comment Organism Reaction ID
2 bilirubin + O2 = 2 biliverdin + 2 H2O analyis of the oxygen reduction reaction mechanism, detailed overview. Bilirubin oxidase (BOD) is the best catalyst for converting oxygen directly to water because of the very low overpotential necessary to catalyze the reaction Albifimbria verrucaria
a

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Albifimbria verrucaria
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 bilirubin + O2
-
 Albifimbria verrucaria 2 biliverdin + 2 H2O
-
 ?
additional information the enzyme needs to be fully reduced before it gets activated for catalysis Albifimbria verrucaria ?
-
 ?

Synonyms

Synonyms Comment Organism
BOD
-
 Albifimbria verrucaria
MvBOD
-
 Albifimbria verrucaria

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30 60
-
 Albifimbria verrucaria

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
 the activity appears to remain constant up to 60°C Albifimbria verrucaria

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8.5
-
 Albifimbria verrucaria

pH Stability

pH Stability pH Stability Maximum Comment Organism
9
-
 loss of 50% of its activity at pH 9.0 Albifimbria verrucaria

General Information

General Information Comment Organism
evolution the enzyme belongs to the multicopper oxidase (MCO) family. These enzymes have four copper atoms that are classified into three types according to their spectroscopic and magnetic properties: type I (T1), type II (T2) and type III (T3) Cu. The MCO family can be separated into two types by substrate specificity. The first group catalyzes the outer sphere oxidation of small organic substrates and include the plant and fungal laccases and ascorbate oxidase, CotA, bilirubin oxidase, and phenoxazinone synthase Albifimbria verrucaria