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Literature summary for 1.3.3.5 extracted from

  • Kataoka, K.; Ito, T.; Okuda, Y.; Sakai, Y.; Yamashita, S.; Sakurai, T.
    Roles of the indole ring of Trp396 covalently bound with the imidazole ring of His398 coordinated to type I copper in bilirubin oxidase (2020), Biochem. Biophys. Res. Commun., 521, 620-624 .
    View publication on PubMed
Search for more literature for 1.3.3.5

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Pichia pastoris Albifimbria verrucaria

Protein Variants

Protein Variants Comment Organism
N394A/W396T the enzymatic activity of the mutant is prominently decreased compared to the wild type enzyme. The enzyme shows shifts in the redox potential of type I copper towards negative direction by more than 100 mV and decreases in cathodic current in electrochemistry, whereas optical and magnetic properties of type I copper are not affected or sparingly affected Albifimbria verrucaria
W396A the enzymatic activity of the mutant is prominently decreased compared to the wild type enzyme. The enzyme shows shifts in the redox potential of type I copper towards negative direction by more than 100 mV and decreases in cathodic current in electrochemistry, whereas optical and magnetic properties of type I copper are not affected or sparingly affected Albifimbria verrucaria
W396F the enzymatic activity of the mutant is prominently decreased compared to the wild type enzyme. The enzyme shows shifts in the redox potential of type I copper towards negative direction by more than 100 mV and decreases in cathodic current in electrochemistry, whereas optical and magnetic properties of type I copper are not affected or sparingly affected Albifimbria verrucaria
W396T the enzymatic activity of the mutant is prominently decreased compared to the wild type enzyme. The enzyme shows shifts in the redox potential of type I copper towards negative direction by more than 100 mV and decreases in cathodic current in electrochemistry, whereas optical and magnetic properties of type I copper are not affected or sparingly affected Albifimbria verrucaria
W396Y the enzymatic activity of the mutant is prominently decreased compared to the wild type enzyme. The enzyme shows shifts in the redox potential of type I copper towards negative direction by more than 100 mV and decreases in cathodic current in electrochemistry, whereas optical and magnetic properties of type I copper are not affected or sparingly affected Albifimbria verrucaria

Metals/Ions

Metals/Ions Comment Organism Structure
Cu the enzyme contains type I copper and a trinuclear copper center comprised of a type II copper and a pair of type III coppers 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
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Albifimbria verrucaria

Substrates and Products (Substrate)

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