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
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1.3.3.5
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electrode
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oxidases
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biofuel
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cathode
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ceruloplasmin
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myrothecium
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anode
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laccases
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verrucaria
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biocathode
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ferroxidase
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trinuclear
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abts
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laccase-like
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dioxygen
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bioanode
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electrocatalytic
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bioelectrocatalytic
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2,6-dimethoxyphenol
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biliverdin
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cuprous
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multi-copper
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syringaldazine
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copa
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copper-binding
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four-electron
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mniii
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self-powered
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aceruloplasminemia
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hephaestin
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p-phenylenediamine
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manganeseii
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bioelectrodes
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open-circuit
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membrane-less
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cupredoxins
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analysis
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electrocatalysts
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manganese-oxidizing
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methionine-rich
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diazo
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biodevice
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energy production
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medicine
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diagnostics
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biotechnology
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synthesis
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environmental protection
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industry
- 1.3.3.5
-
electrode
- oxidases
-
biofuel
-
cathode
- ceruloplasmin
- myrothecium
-
anode
- laccases
- verrucaria
-
biocathode
- ferroxidase
-
trinuclear
- abts
-
laccase-like
- dioxygen
-
bioanode
-
electrocatalytic
-
bioelectrocatalytic
- 2,6-dimethoxyphenol
- biliverdin
-
cuprous
-
multi-copper
- syringaldazine
- copa
-
copper-binding
-
four-electron
-
mniii
-
self-powered
-
aceruloplasminemia
- hephaestin
- p-phenylenediamine
-
manganeseii
-
bioelectrodes
-
open-circuit
-
membrane-less
- cupredoxins
- analysis
-
electrocatalysts
-
manganese-oxidizing
-
methionine-rich
-
diazo
-
biodevice
- energy production
- medicine
- diagnostics
- biotechnology
- synthesis
- environmental protection
- industry
Reaction
2 bilirubin + = 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
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pH Range
pH Range on EC 1.3.3.5 - bilirubin oxidase
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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
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using 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate
4 - 9
4.5 - 8.2
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under acidic condition enzyme oxidizes only conjugated bilirubin
5 - 8.5
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activity range with substrate remazol brilliant blue R, profile overview
additional information
analysis of pH dependence of the enzyme immobilized on electrodes, detailed overview