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
-
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
- 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
Advanced search results
General Information
General Information on EC 1.3.3.5 - bilirubin oxidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
physiological function
additional information
-
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
-
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
-
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
-
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
the enzyme belongs to the family of multicopper oxidases (MCOs)
evolution
the enzyme belongs to the multicopper oxidase (MCO) family. These enzymes have four copper atoms that are classified into three types according to their spectroscopic and magnetic properties: type I (T1), type II (T2) and type III (T3) Cu. The MCO family can be separated into two types by substrate specificity. The first group catalyzes the outer sphere oxidation of small organic substrates and include the plant and fungal laccases and ascorbate oxidase, CotA, bilirubin oxidase, and phenoxazinone synthase
evolution
-
the enzyme belongs to the family of multicopper oxidases (MCOs)
-
bilirubin oxidase (BOD) is one of the multicopper oxidoreductases family with many interesting possible biotechnological applications, including biocatalytic reduction of oxygen (O2) at natural pH, biosensing, biobleaching, bioremediation, chemical synthesis, and wine stabilization
physiological function
the enzyme is a copper-containing oxidase that catalyzes oxidation of various organic compounds, including phenolic ones, by molecular oxygen, the latter is reduced to water via a fourelectron mechanism
-
dissociation of type I copper, caused by thermal inactivation, is accompanied by a conformational change and a decrease in secondary structure
additional information
-
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
additional information
-
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
additional information
-
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
additional information
-
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
additional information
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
additional information
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
additional information
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
additional information
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
additional information
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions