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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Crystallization
Crystallization on EC 1.3.3.5 - bilirubin oxidase
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hanging drop vapour diffusion method, 0.003 ml of 9.2 mg/ml protein in 10 mM Tris-HCl, pH 8.0, are mixed with 0.003 ml of recipitant solution containing 10% 2-methyl-2,4-pentanediol, 1.44 M ammonium sulfate, 10% glycerol and 0.5 M KCl, equilibration against 0.2-1.0 ml precipitant solution at 20°C, X-ray diffraction structure determination and analysis at 2.3-2.5 A resolution, modelling
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
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wild type and mutant enzymes W396A and W396F bound to ferricyanide, hanging drop vapor diffusion method, using 0.1 M succinic acid, 14% (w/v) polyethylene glycol 3350