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
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Metals Ions
Metals Ions on EC 1.3.3.5 - bilirubin oxidase
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copper
Cu
Cu2+
additional information
copper
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Cu2+ can be removed by KCN, reconstitution of the apoprotein by treating with CuSO4 for 40 h at 4°C and pH 7-8, Cu2+ reconstituted enzyme regains full activity, Fe2+ reconstituts 59,1% activity, Co2+ reconstituts 31% activity and Cd2+ reconstituts 24.5% activity
copper
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multicopper enzyme, contains type 1,2 and 3 copper, authentic and recombinant wild-type enzyme contain 4 copper atoms/protein
copper
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multicopper oxidase contains 4 copper ions per protein molecule. Cu-binding sites are not affected by differences in carbohydrate content and the N-terminal extension of four amino acid residues
copper
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multicopper oxidase, the redox state of type I Cu is an equilibrium state of the oxidized and reduced forms highly depending on pH, possibly by a shift of the radical center between Cu and cys sulfur
Cu
the enzyme consists of 3 cupredoxin-like domains with 4 copper ions forming two active sites
Cu
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the enzyme contains type I copper and a trinuclear copper center comprised of a type II copper and a pair of type III coppers
Cu
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the enzyme possesses a trinuclear Cu center, which is composed of one T2Cu and a pair of T3Cu atoms, T3aCu and T3bCu
Cu2+
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multicopper oxidase containing four Cu centers, type 1 Cu, type II Cu, and a pair of type III Cu's in a protein molecule consisting of three domains with homologous structure to cupredoxin containing only type I Cu
Cu2+
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dissociation of type I copper, caused by thermal inactivation, is accompanied by a conformational change and a decrease in secondary structure
Cu2+
multicopper oxidase with copper-binding sites. The type I Cu is coordinated by four amino-acid residues His398, Cys457, His462 and Met 467, and the type II Cu is coordinated by two amino-acid residues, His94 and His401, binding structure, overview
Cu2+
multicopper oxidase, ferrocyanide is an effective electron donor to type 1 Cu2+
Cu2+
bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
Cu2+
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highly activating, the enzyme contains four copper ions per functional unit
Cu2+
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bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
Cu2+
bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
Cu2+
bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
Cu2+
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the enzyme is a multicopper oxidase, MCO, whhich contains 4 copper ions per enzyme molecule
Cu2+
bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
Cu2+
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the organic substrate binding center comprises one copper ion and is denoted T1, the O2-binding center comprises a cluster of three copper centers denoted T2 and T3
Cu2+
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bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
Cu2+
-
bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
Cu2+
bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
Cu2+
-
bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
BODs display a high tolerance towards chloride anions and other chelators
additional information
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BODs display a high tolerance towards chloride anions and other chelators
additional information
BODs display a high tolerance towards chloride anions and other chelators
additional information
BODs display a high tolerance towards chloride anions and other chelators
additional information
BODs display a high tolerance towards chloride anions and other chelators
additional information
-
BODs display a high tolerance towards chloride anions and other chelators
additional information
-
BODs display a high tolerance towards chloride anions and other chelators
additional information
BODs display a high tolerance towards chloride anions and other chelators
additional information
-
BODs display a high tolerance towards chloride anions and other chelators