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1.3.3.5: bilirubin oxidase

This is an abbreviated version!
For detailed information about bilirubin oxidase, go to the full flat file.

Word Map on EC 1.3.3.5

Reaction

2 bilirubin +

O2
= 2 biliverdin + 2 H2O

Synonyms

bilirubin oxidase, bilirubin oxidase M-1, bilirubin:oxygen oxidoreductase, blue Cu enzyme, BOD, BODx, BOX, BPUM_0542, copper oxidase, CotA, MCO, multicopper oxidase, MvBO, MvBOD, oxidase, bilirubin

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.3 With oxygen as acceptor
                1.3.3.5 bilirubin oxidase

pH Range

pH Range on EC 1.3.3.5 - bilirubin oxidase

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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9.5
activity range, inactive above and below. In reaction with electron donor substrates, the enzyme exhibits the maximal activity at acidic pH values: pH 4.0 for 2,2'-azino-bis-[3-ethylbenzthiazoline-6-sulfonic acid] (ABTS) and pH 3.0 for potassium ferricyanide. Catalytic activity decreases on pH increase, and the enzyme becomes completely inactive at pH above 9.5. At neutral pH values, bilirubin oxidase retains about 50% maximal activity in oxidation of both substrates. In reaction with a hydrogen atom donor (catechol), the pH profile of the enzyme activity is shifted to alkaline values: enzymatic activity is not exhibited at pH below 6.0. This is probably related with the higher reactivity of the substrate as a phenolate anion
3.5 - 4.5
-
using 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate
4 - 9
4.5 - 8.2
-
under acidic condition enzyme oxidizes only conjugated bilirubin
5 - 8.5
-
activity range with substrate remazol brilliant blue R, profile overview
6.5 - 8
-
using p-phenylenediamine or o-aminophenol as a substrate
8 - 10
-
at pH 8.0 and 10.0: about 30% of maximum activity
additional information