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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Inhibitors
Inhibitors on EC 1.3.3.5 - bilirubin oxidase
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bilirubin
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0.09 mM, complete inhibition of enzyme activity in 50 : 50 chloroform-n-heptane two-phase system
guanidinium hydrochloride
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reversible inactivation at 1 M, pH 7.0, kinetics, overview
NaCl
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50% inhibition at about 10 mM, inactivation at 150 mM with substrate conjugated bilirubin
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the enzyme is irreversibly and rapidly damaged by urate in the presence of O2
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measurements of reversible and irreversible inactivation processes of the redox enzyme bilirubin oxidase by electrochemical methods based on bioelectrocatalysis, overview
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additional information
BODs display a high tolerance towards chloride anions and other chelators
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additional information
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the enzyme is not affected by urea and EDTA
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additional information
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not affected by ascorbic acid, urea, D-glucose, uric acid, or triglycerides
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additional information
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BODs display a high tolerance towards chloride anions and other chelators
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additional information
BODs display a high tolerance towards chloride anions and other chelators
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additional information
BODs display a high tolerance towards chloride anions and other chelators, the enzyme from Bacillus pumilus is urate-, DTT-, and EDTA-insensitive
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additional information
BODs display a high tolerance towards chloride anions and other chelators
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additional information
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the immobilized wired bilirubin oxidase electrocatalyst is not only irreversibly deactivated by urate in the presence of O2 in a few hours, but is initially reversibly deactivated, in 1 min or less, by the urate in the presence of O2
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additional information
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BODs display a high tolerance towards chloride anions and other chelators
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additional information
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BODs display a high tolerance towards chloride anions and other chelators
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additional information
BODs display a high tolerance towards chloride anions and other chelators
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additional information
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BODs display a high tolerance towards chloride anions and other chelators, the enzyme from Magnaporthe oryzae is urate-, DTT-, and EDTA-insensitive
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