Literature summary for 1.3.3.5 extracted from

Akter, M.; Tokiwa, T.; Shoji, M.; Nishikawa, K.; Shigeta, Y.; Sakurai, T.; Higuchi, Y.; Kataoka, K.; Shibata, N.
Redox potential-dependent formation of an unusual His-Trp bond in bilirubin oxidase (2018), Chemistry, 24, 18052-18058 .

Search for more literature for 1.3.3.5

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Pichia pastoris	Albifimbria verrucaria

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting drop vapor diffusion method, wild type enzyme is crystallized with 0.1 M sodium citrate pH 5.0 and 20% (w/v) PEG 8000. Mutant enzyme M47Q is crystallized with 0.1 M MES pH 5.5,12% (w/v) PEG 8000, and 0.1 M calcium acetate	Albifimbria verrucaria

Protein Variants

Protein Variants	Comment	Organism
M467Q	the mutant is inactive against bilirubin. A post-translational crosslink between Trp396 and His398, formed in the vicinity of the T1Cu site in wild type enzyme, is absent in the mutant	Albifimbria verrucaria

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu	the active sites of the enzyme comprise four copper atoms	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 + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Albifimbria verrucaria	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
Toyopearl Butyl-650M column chromatography and Superdex 200 gel filtration	Albifimbria verrucaria

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
BOD	-	Albifimbria verrucaria

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Release 2023.1 (January 2023)