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Information on EC 1.3.3.5 - bilirubin oxidase
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1.3.3.5 bilirubin oxidaseSpecify your search results
Word Map
- 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
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
bilirubin oxidase, multicopper oxidase, copper oxidase, mvbod, blue cu enzyme, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bilirubin oxidase
bilirubin oxidase M-1
-
-
-
-
bilirubin:oxygen oxidoreductase
BOD
BOX
BPUM_0542
copper oxidase
CotA
MCO
multicopper oxidase
oxidase, bilirubin
-
-
-
-
bilirubin oxidase
-
-
-
-
BOD
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 bilirubin + O2 = 2 biliverdin + 2 H2O
-
-
-
-
2 bilirubin + O2 = 2 biliverdin + 2 H2O
analyis of the oxygen reduction reaction mechanism, detailed overview. Bilirubin oxidase (BOD) is the best catalyst for converting oxygen directly to water because of the very low overpotential necessary to catalyze the reaction
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
bilirubin:oxygen oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
80619-01-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4E,15Z)-cyclobilirubin IX alpha + O2
?
-
phosphate buffer, pH 3.5-7.4
-
-
?
(4Z,15E)-bilirubin IX alpha + O2
?
-
no activity above pH 4.5 in phosphate buffer
-
-
?
(4Z,15Z)-bilirubin IX alpha + O2
?
-
no activity above pH 5.5 in phosphate buffer, no acticvity in citrate-lactate buffer, pH 3.7
-
-
?
1,1'-dimethylferrocene + O2
1,1'-dimethylferricenium + H2O
-
1,1'-dimethylferrocene soluble as an inclusion complex with 2-hydroxypropyl-beta-cyclodextrin
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O
cytochrome c + O2
?
-
BOD efficiently accepts cytochrome c as an electron donor in both cases when cytochrome c is in solution or electrostatically adsorbed
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
the enzyme from Bacillus pumilus shows higher turnover activity towards bilirubin compared to other bacterial MCOs
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-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
substrates are unconjugated bilirubin and conjugated bilirubin
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
substrate conjugated bilirubin
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
Pyricularia oryzae ATCC MYA-4617
-
substrate conjugated bilirubin
-
-
?
2 bilirubin + O2
2 biliverdin + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
i.e. ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
the enzyme has a higher affinity for oxygen in the presence of the nanoparticles compared to the dissolved 2,2`-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) mediator, although with a slower turnover rate
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
Albifimbria verrucaria ATCC24571
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
BOD encapsulated in ananostructured sol-gel/carbon nanotube composite electrode effectively catalyzes the reduction of molecular oxygen into water through direct electron transfer
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O
-
-
-
?
2,2'-azino-di-[3-ethylbenzthiazoline-6-sulfonic acid] + O2
?
Pyricularia oryzae ATCC MYA-4617
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
enzyme also exhibits laccase activity
-
?
bilirubin + O2
biliverdin + H2O
-
CotA with markedly higher affinity for bilirubin than conventional bilirubin oxidase
-
-
?
bilirubin + O2
biliverdin + H2O
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-
biliverdin + colourless diazo-negative compounds, including propentdyopents
?
bilirubin + O2
biliverdin + H2O
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-
biliverdin + colourless diazo-negative compounds, including propentdyopents
?
Congo Red + O2
?
100% decoloration efficiency is reached for Congo Red at pH 4.0 in 8 h
-
-
?
Congo Red + O2
?
100% decoloration efficiency is reached for Congo Red at pH 4.0 in 8 h
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
-
23% of activity with bilirubin
-
-
?
Remazol Brilliant Blue + O2
?
80% decoloration efficiency is reached for Remazol Brilliant Blue at pH 8.2 in 24 h
-
-
?
Remazol Brilliant Blue + O2
?
80% decoloration efficiency is reached for Remazol Brilliant Blue at pH 8.2 in 24 h
-
-
?
syringaldazine + O2
oxidized syringaldazine + H2O
-
-
-
?
additional information
?
-
-
cytochrome c and bilirubin oxidase are coimmobilized in a polyelectrolyte multilayer on gold electrodes and although these two proteins are not natural reaction partners, the protein architecture facilitates an electron transfer from the electrode through multiple protein layers to molecular oxygen
-
-
?
additional information
?
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-
activity measurement with Fe(CN)6 4-
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-
?
additional information
?
-
-
decolorization and biodegradation of remazol brilliant blue R, an anthraquinone dye, by bilirubin oxidase
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-
?
additional information
?
-
direct proton uptake of Glu463 plays a key role in the proton donation to the activated oxygen species in the catalytic cycle, redox-induced protonation state changes of Glu463, electrochemistry-induced ATR-FTIR spectroscopy, overview
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-
?
additional information
?
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extracellular bilirubin oxidase decolorizes indigo carmine, biosorption and biodegradation of the dye is achved with more than 98% decolorization efficiency after 7 days at 26°C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30°C to 50°C and pH 5.5-9.5 with dye concentrations of 50-200 mg/ml, overview
-
-
?
additional information
?
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
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the enzyme is also active with the laccase substrate 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate)
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-
?
additional information
?
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oxidative polymerization of dihydroquercetin from Larix sibirica using bilirubin oxidase as a biocatalyst. DHQ oligomers (oligoDHQ) with molecular mass of 2800 and polydispersity of 8.6 are obtained by enzymatic reaction under optimal conditions. The oligomers appear to be soluble in dimethylsulfoxide, dimethylformamide, and methanol. UVvisible spectra of oligoDHQ in dimethylsulfoxide indicate the presence of highly conjugated bonds. Irregular structure of a polymer formed via the enzymatic oxidation of DHQ followed by nonselective radical polymerization. As compared with the monomer, oligoDHQ demonstrates higher thermal stability and high antioxidant activity
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-
?
additional information
?
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the enzyme needs to be fully reduced before it gets activated for catalysis
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-
?
additional information
?
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the enzyme needs to be fully reduced before it gets activated for catalysis
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-
?
additional information
?
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the oxygen reduction reaction activity of the enzyme with direct electron transfer reactions is higher than that with mediated electron transfer reactions
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-
-
additional information
?
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-
extracellular bilirubin oxidase decolorizes indigo carmine, biosorption and biodegradation of the dye is achved with more than 98% decolorization efficiency after 7 days at 26°C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30°C to 50°C and pH 5.5-9.5 with dye concentrations of 50-200 mg/ml, overview
-
-
?
additional information
?
-
-
the enzyme is also active with the laccase substrate 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate)
-
-
?
additional information
?
-
-
decolorization and biodegradation of remazol brilliant blue R, an anthraquinone dye, by bilirubin oxidase
-
-
?
additional information
?
-
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
-
the enzyme is also activity with the laccase, EC 1.10.3.2, substrates 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine and 2,6-dimethoxyphenol
-
-
?
additional information
?
-
usage of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,6-dimethoxyphenol as substrates, optimization of the assay method
-
-
?
additional information
?
-
-
usage of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,6-dimethoxyphenol as substrates, optimization of the assay method
-
-
?
additional information
?
-
usage of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,6-dimethoxyphenol as substrates, optimization of the assay method
-
-
?
additional information
?
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
-
O2 is catalytically reduced on BOD-modified spectrographic graphite electrodes, very slow direct electron transfer is observed for the enzyme absorbed on gold electrodes
-
-
?
additional information
?
-
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
-
in addition to the oxidation of bilirubin to biliverdin and of biliverdin to a purple pigment, BODs utilize also the more traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate) and syringaldazine. The enzyme is efficient in decolorizing textile dyes such as Remazol brilliant Blue R
-
-
?
additional information
?
-
Pyricularia oryzae ATCC MYA-4617
-
in addition to the oxidation of bilirubin to biliverdin and of biliverdin to a purple pigment, BODs utilize also the more traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate) and syringaldazine. The enzyme is efficient in decolorizing textile dyes such as Remazol brilliant Blue R
-
-
?
additional information
?
-
in the presence of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as the mediator, the enzyme decolorizes crystal violet, malachite green and Congo red dyes at a rate of about 36%, 63% and 71%, respectively in 2 h
-
-
-
additional information
?
-
in the presence of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as the mediator, the enzyme decolorizes crystal violet, malachite green and Congo red dyes at a rate of about 36%, 63% and 71%, respectively in 2 h
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 bilirubin + O2
2 biliverdin + H2O