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.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.3.3.5
-
RECOMMENDED NAME
GeneOntology No.
bilirubin oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 bilirubin + O2 = 2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Porphyrin and chlorophyll metabolism
-
SYSTEMATIC NAME
IUBMB Comments
bilirubin:oxygen oxidoreductase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
bilirubin oxidase
-
-
-
-
bilirubin oxidase
-
-
bilirubin oxidase M-1
-
-
-
-
bilirubin:oxygen oxidoreductase
-
-
blue Cu enzyme
-
-
BOD
A8FAG9
-
BOD
Magnaporthe oryzae ATCC MYA-4617
-
-
-
BOD
Myrothecium sp.
-
-
BOD
Myrothecium verrucaria BO3
-
-
-
BOD
Myrothecium verrucaria MT-1
Q12737
-
-
BOX
Myrothecium sp.
-
-
BOX
Myrothecium verrucaria IMER1
-
-
-
CotA
A8FAG9
-
CotA
P07788
-
CotA
Q9UVY4
-
oxidase, bilirubin
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
80619-01-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Magnaporthe oryzae ATCC MYA-4617
-
-
-
Manually annotated by BRENDA team
IFO 9950, low activity
-
-
Manually annotated by BRENDA team
IFO 9531, low activity
-
-
Manually annotated by BRENDA team
Myrothecium sp.
-
-
-
Manually annotated by BRENDA team
Myrothecium sp.
strain IMER1
-
-
Manually annotated by BRENDA team
strain IMER1
-
-
Manually annotated by BRENDA team
strain MT-1
-
-
Manually annotated by BRENDA team
Myrothecium verrucaria 3.2190
-
-
-
Manually annotated by BRENDA team
Myrothecium verrucaria BO3
strain BO3
-
-
Manually annotated by BRENDA team
Myrothecium verrucaria IMER1
-
-
-
Manually annotated by BRENDA team
Myrothecium verrucaria MT-1
-
UniProt
Manually annotated by BRENDA team
Myrothecium verrucaria MT-1
strain MT-1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
Q65MU7
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
A8FAG9
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
P07788
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
Q9UVY4
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
evolution
-
the enzyme is a CotA multicopper oxidase, MCO
additional information
-
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
Q65MU7
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
additional information
A8FAG9
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
additional information
P07788
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
Q9UVY4
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4E,15Z)-cyclobilirubin + O2
?
show the reaction diagram
-
phosphate buffer, pH 3.5-7.4
-
-
?
(4Z,15E)-cyclobilirubin + O2
?
show the reaction diagram
-
no activity above pH 4.5 in phosphate buffer
-
-
?
(4Z,15Z)-cyclobilirubin + O2
?
show the reaction diagram
-
no activity above pH 5.5 in phosphate buffer, no acticvity in citrate-lactate buffer, pH 3.7
-
-
?
1,1'-dimethylferrocene + O2
1,1'-dimethylferricinium + H2O
show the reaction diagram
-
1,1'-dimethylferrocene soluble as an inclusion complex with 2-hydroxypropyl-beta-cyclodextrin
-
?
1,3-dihydroxynaphthalene + O2
?
show the reaction diagram
-
-
-
-
?
1,5-dihydroxynaphthalene + O2
?
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
Q9UVY4
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
P07788
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
Q65MU7
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
A8FAG9
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
the enzyme from Bacillus pumilus shows higher turnover activity towards bilirubin compared to other bacterial MCOs
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
substrate conjugated bilirubin
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
substrates are unconjugated bilirubin and conjugated bilirubin
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
Magnaporthe oryzae ATCC MYA-4617
-
-, substrate conjugated bilirubin
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
Myrothecium verrucaria MT-1
Q12737
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
Myrothecium verrucaria 3.2190
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
show the reaction diagram
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
show the reaction diagram
-
i.e. ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
show the reaction diagram
Myrothecium verrucaria BO3
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
show the reaction diagram
-
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-ethylbenzthiazoline-6-sulfonate) + O2
?
show the reaction diagram
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonate) + O2
?
show the reaction diagram
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzthiazoline-6-sulfonic acid] + O2
?
show the reaction diagram
Magnaporthe oryzae, Magnaporthe oryzae ATCC MYA-4617
-
-
-
-
?
ascorbic acid + O2
?
show the reaction diagram
Myrothecium verrucaria, Myrothecium verrucaria MT-1
-
very low activity
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-, Q12737
-
-
-
r
bilirubin + O2
biliverdin + H2O
show the reaction diagram
Myrothecium sp.
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
-
-
r
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
biliverdin + colourless diazo-negative compounds, including propentdyopents
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
biliverdin + colourless diazo-negative compounds, including propentdyopents
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
no formation of H2O2
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
enzyme also exhibits laccase activity
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
CotA with markedly higher affinity for bilirubin than conventional bilirubin oxidase
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
Myrothecium verrucaria BO3
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
Myrothecium verrucaria MT-1
-
-
-
?
bilirubin ditaurine + O2
?
show the reaction diagram
-
-
-
-
?
biliverdin + O2
?
show the reaction diagram
-
-
-
-
?
biliverdin + O2
?
show the reaction diagram
-
50% of activity with bilirubin
-
-
?
catechol + O2
?
show the reaction diagram
-
67% of activity with bilirubin
-
-
?
chlorophyllin + O2
?
show the reaction diagram
-
50% of activity with bilirubin
-
-
?
cytochrome c + O2
?
show the reaction diagram
-
BOD efficiently accepts cytochrome c as an electron donor in both cases when cytochrome c is in solution or electrostatically adsorbed
-
-
?
ditaurobilirubin + O2
?
show the reaction diagram
-
-
-
-
?
ditaurobilirubin + O2
?
show the reaction diagram
-
-
-
-
?
Fe(CN)64- + O2
Fe(CN)63- + H2O
show the reaction diagram
-
-
-
-
?
ferrocene + O2
ferricinium + H2O
show the reaction diagram
-
low activity
-
?
ferrocyanide + O2
?
show the reaction diagram
-
-
-
-
?
hemin + O2
?
show the reaction diagram
-
10% of activity with bilirubin
-
-
?
hexacyanoferrate(II) + O2
hexacyanoferrate(III) + H2O
show the reaction diagram
-
-
-
-
?
hydroquinone + O2
?
show the reaction diagram
-
20% of activity with bilirubin
-
-
?
indigo carmine + O2
?
show the reaction diagram
Myrothecium sp.
-
dye decolorization reaction
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
show the reaction diagram
-
23% of activity with bilirubin
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
show the reaction diagram
Myrothecium verrucaria MT-1
-
-
-
-
?
o-aminophenol + O2
?
show the reaction diagram
-
-
-
-
?
o-aminophenol + O2
?
show the reaction diagram
Myrothecium verrucaria BO3
-
-
-
-
?
octacyanotungstate(IV) + O2
octacyanotungstate(V) + H2O
show the reaction diagram
-
-
-
-
?
p-phenylenediamine + O2
?
show the reaction diagram
-
-
-
-
?
p-phenylenediamine + O2
?
show the reaction diagram
-
15% of activity with bilirubin
-
-
?
p-phenylenediamine + O2
?
show the reaction diagram
Myrothecium verrucaria BO3
-
-
-
-
?
pyrogallol + O2
?
show the reaction diagram
-
10% of activity with bilirubin
-
-
?
Remazol Brilliant Blue R + O2
?
show the reaction diagram
Myrothecium sp., Myrothecium sp. IMER1
-
decolorization reaction
-
-
?
syringaldazine + O2
?
show the reaction diagram
-
-
-
-
?
[Fe(CN)6]4- + H+ + O2
[Fe(CN)6]3- + H2O
show the reaction diagram
-
-
-
-
?
K4[Fe(CN)6] + O2
K3[Fe(CN)6] + H2O
show the reaction diagram
-
-
-
-
?
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
?
-
-
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
?
-
-
activity measurement with Fe(CN)6 4-
-
-
-
additional information
?
-
-
decolorization and biodegradation of remazol brilliant blue R, an anthraquinone dye, by bilirubin oxidase
-
-
-
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
-
-
-
additional information
?
-
-
extracellular bilirubin oxidase decolorizes indigo carmine, biosorption and biodegradation of the dye is achved with more than 98% decolorization efficiency after 7 days at 26C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30C to 50C 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
?
-
Q9UVY4
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
?
-
P07788
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
?
-
Q65MU7
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
?
-
A8FAG9
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
?
-
-
the enzyme is also active with the laccase substrate 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate)
-
-
-
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
?
-
Magnaporthe 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
?
-
Myrothecium verrucaria IMER1
-
decolorization and biodegradation of remazol brilliant blue R, an anthraquinone dye, by bilirubin oxidase
-
-
-
additional information
?
-
Myrothecium verrucaria 3.2190
-
extracellular bilirubin oxidase decolorizes indigo carmine, biosorption and biodegradation of the dye is achved with more than 98% decolorization efficiency after 7 days at 26C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30C to 50C and pH 5.5-9.5 with dye concentrations of 50-200 mg/ml, overview, the enzyme is also active with the laccase substrate 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate)
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
Q9UVY4
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
P07788
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
Q65MU7
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
A8FAG9
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
the enzyme from Bacillus pumilus shows higher turnover activity towards bilirubin compared to other bacterial MCOs
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
Magnaporthe oryzae ATCC MYA-4617
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
Myrothecium verrucaria MT-1
Q12737
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
Myrothecium verrucaria 3.2190
-
-
-
-
?
additional information
?
-
-
extracellular bilirubin oxidase decolorizes indigo carmine, biosorption and biodegradation of the dye is achved with more than 98% decolorization efficiency after 7 days at 26C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30C to 50C 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
?
-
Q9UVY4
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
?
-
P07788
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
?
-
Q65MU7
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
?
-
A8FAG9
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
?
-
Myrothecium verrucaria 3.2190
-
extracellular bilirubin oxidase decolorizes indigo carmine, biosorption and biodegradation of the dye is achved with more than 98% decolorization efficiency after 7 days at 26C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30C to 50C and pH 5.5-9.5 with dye concentrations of 50-200 mg/ml, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
ferrocyanide is an effective electron donor to type 1 Cu2+
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
copper
-
metalloenzyme, 1 atom of copper per enzyme molecule
copper
-
2 Cu2+ per protein molecule
copper
-
Cu2+ can be removed by KCN, reconstitution of the apoprotein by treating with CuSO4 for 40 h at 4C 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
-
3.7 copper atoms per enzyme molecule, recombinant enzyme
copper
-
multicopper enzyme, contains type 1,2 and 3 copper, authentic and recombinant wild-type enzyme contain 4 copper atoms/protein
copper
-
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
copper
-
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
Cu
-
contains T1 and T2/T3 redox copper centers
Cu2+
-
contains a type I copper center
Cu2+
-
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+
-
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+
-
contains copper centers
Cu2+
-
multi-copper oxidase
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+
-
dissociation of type I copper, caused by thermal inactivation, is accompanied by a conformational change and a decrease in secondary structure
Cu2+
-
multicopper oxidase, ferrocyanide is an effective electron donor to type 1 Cu2+
Cu2+
-
required, 4 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+
Q65MU7
bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
Cu2+
A8FAG9
bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
Cu2+
P07788
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+
Q9UVY4
bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
Cu2+
-
the enzyme is a multicopper oxidase, MCO, whhich contains 4 copper ions per enzyme molecule
Cu2+
-
highly activating, the enzyme contains four copper ions per functional unit
additional information
-
BODs display a high tolerance towards chloride anions and other chelators
additional information
Q65MU7
BODs display a high tolerance towards chloride anions and other chelators
additional information
A8FAG9
BODs display a high tolerance towards chloride anions and other chelators
additional information
P07788
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
Q9UVY4
BODs display a high tolerance towards chloride anions and other chelators
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Albumin
-
-
-
Albumin
-
0.008 mM, 50% inhibition
-
Bilirubin
-
0.09 mM, complete inhibition of enzyme activity in 50 : 50 chloroform-n-heptane two-phase system
bromosulphothalein
-
1 mM, 60% inhibition
cysteine
-
1 mM, 40% inhibition
Digitonin
-
0.1%, 50% inhibition
dithiothreitol
-
1 mM, 60% inhibition
DTT
-
62.3% inhibition at 1 mM
Fe2+
-
1 mM, complete inhibition
-
guanidinium hydrochloride
-
reversible inactivation at 1 M, pH 7.0, kinetics, overview
KCl
-
50 mM, 40% inhibition
KCN
-
0.1 mM, complete inhibition
KCN
-
30 mM, 78% inhibition
KCN
-
0.03 mM, 70% inhibition
L-cysteine
-
87% inhibition at 1 mM, no significant effect at 0.1 mM
mercaptoethanol
-
1 mM, 50% inhibition
NaCl
-
crude enzyme
NaCl
-
50 mM, 17% inhibition
NaCl
-
50% inhibition at about 10 mM, inactivation at 150 mM with substrate conjugated bilirubin
NAD+
-
1 mM, 66% inhibition
NADH
-
1 mM, 72% inhibition
NADH
-
0.2 mM, 50% inhibition
NaN3
-
76% inhibition at 10 mM
Remazol Brilliant Blue R
-
substrate inhibition above 100 mg/l
Sodium azide
-
0.1 mM, 42% inhibition
sodium taurocholate
-
0.5%, 50% inhibition
Thiourea
-
0.1 mM, 15% inhibition
Urate
-
the enzyme is irreversibly and rapidly damaged by urate in the presence of O2
MgCl2
-
50 mM, 52% inhibition
additional information
-
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
-
additional information
-
measurements of reversible and irreversible inactivation processes of the redox enzyme bilirubin oxidase by electrochemical methods based on bioelectrocatalysis, overview
-
additional information
-
BODs display a high tolerance towards chloride anions and other chelators
-
additional information
Q65MU7
BODs display a high tolerance towards chloride anions and other chelators
-
additional information
A8FAG9
BODs display a high tolerance towards chloride anions and other chelators, the enzyme from Bacillus pumilus is urate-, DTT-, and EDTA-insensitive
-
additional information
P07788
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, the enzyme from Magnaporthe oryzae is urate-, DTT-, and EDTA-insensitive
-
additional information
-
BODs display a high tolerance towards chloride anions and other chelators
-
additional information
Q9UVY4
BODs display a high tolerance towards chloride anions and other chelators
-
additional information
-
the enzyme is not affected by urea and EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
i.e. ABTS, can serve as an electron mediator to facilitate the oxidation of remazol brilliant blue R
Salt
-
maximum activity at a ionic strength of 60 mM, independent of salt type
Triton X-100
-
0.01%, 25% increase in activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.076
-
2,2'-azino-bis(3-ethylbenzthioline-6-sulfonic acid)
-
at pH 2.7, Km increases with pH
-
0.25
-
2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 6.5, authentic bilirubin oxidase
0.34
-
2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 6.5, recombinant enzyme from Pichia pastoris
0.008
-
Bilirubin
-
-
0.008
-
Bilirubin
P07788
unconjugated bilirubin, pH 7.0, temperature not specified in the publication
0.015
-
Bilirubin
P07788
conjugated bilirubin, pH 7.0, temperature not specified in the publication
0.018
-
Bilirubin
-
conjugated bilirubin, pH 3.6, temperature not specified in the publication
0.021
-
Bilirubin
-
pH 7.5, 25C
0.022
-
Bilirubin
A8FAG9
unconjugated bilirubin, pH 7.2, temperature not specified in the publication
0.022
-
Bilirubin
-
unconjugated bilirubin, pH 7.2, 37C
0.035
-
Bilirubin
A8FAG9
conjugated bilirubin, pH 4.8, temperature not specified in the publication
0.0351
-
Bilirubin
-
conjugated bilirubin, pH 7.2, 37C
0.04
-
Bilirubin
-
-
0.0602
-
Bilirubin
-
preparations of enzyme lyophilized from N-(2-hydroxyethyl)-piperazine-N'-(3-propane-sulfonic acid) buffer suspended in 50 : 50 v/v chloroform-n-heptane mixture
0.077
-
Bilirubin
-
-
0.1
-
Bilirubin
-
pH 8.0, recombinant enzyme from Pichia pastoris
0.109
-
Bilirubin
-
enzyme immobilized on alginate-silicate beads
0.12
-
Bilirubin
-
pH 8.0, authentic bilirubin oxidase
0.12
-
Bilirubin
-
conjugated bilirubin, pH 5.5, temperature not specified in the publication
0.136
-
Bilirubin
-
-
0.19
-
Bilirubin
-
-
0.19
-
Bilirubin
-
assay in purely aqueous system
0.222
-
Bilirubin
-
-
0.37
-
Bilirubin
-
unconjugated bilirubin, pH 8.0, temperature not specified in the publication
14.41
-
Bilirubin
-
mutant I402G
24.22
-
Bilirubin
-
recombinant enzyme
0.18
-
Biliverdin
-
-
0.015
-
ditaurobilirubin
-
-
0.14
-
ditaurobilirubin
-
pH 5.5, recombinant enzyme from Pichia pastoris
0.37
-
ditaurobilirubin
-
pH 5.5, authentic bilirubin oxidase
0.0192
-
K4[Fe(CN)6]
-
wild type recombinant enzyme, at pH 7.0 and 25C
9.6
-
p-phenylenediamine
-
pH 6.5, recombinant enzyme from Pichia pastoris
9.8
-
p-phenylenediamine
-
pH 6.5, authentic bilirubin oxidase
0.047
-
syringaldazine
-
at pH 8.2, lower Km at pH 7.0 and pH 9.0
5.966
-
K4[Fe(CN)6]
-
mutant enzyme M467Q, at pH 7.0 and 25C
additional information
-
additional information
-
first-order kinetics, voltammogram for the bioelectrolytic reaction, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.17
-
2,2'-azino-bis(3-ethylbenzthioline-6-sulfonic acid)
-
at pH 5.3, about 3fold higher value at pH 2.5
-
115
-
2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 6.5, authentic bilirubin oxidase
164
-
2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 6.5, recombinant enzyme from Pichia pastoris
0.00133
-
Bilirubin
-
preparations of enzyme lyophilized from N-(2-hydroxyethyl)-piperazine-N'-(3-propane-sulfonic acid) buffer suspended in 50 : 50 v/v chloroform-n-heptane mixture
0.115
-
Bilirubin
-
mutant I402G
2.19
-
Bilirubin
-
pH 7.5, 25C
3.93
-
Bilirubin
-
recombinant enzyme
29
-
Bilirubin
-
conjugated bilirubin, pH 3.6, temperature not specified in the publication
66.8
-
Bilirubin
-
conjugated bilirubin, pH 7.2, 37C
67
-
Bilirubin
A8FAG9
conjugated bilirubin, pH 4.8, temperature not specified in the publication
70
-
Bilirubin
A8FAG9
unconjugated bilirubin, pH 7.2, temperature not specified in the publication
70
-
Bilirubin
-
unconjugated bilirubin, pH 7.2, 37C
94.3
-
Bilirubin
-
unconjugated bilirubin, pH 8.0, temperature not specified in the publication
115
-
Bilirubin
-
-
117
-
Bilirubin
-
pH 8.0, authentic bilirubin oxidase
117
-
Bilirubin
-
conjugated bilirubin, pH 5.5, temperature not specified in the publication
200
-
Bilirubin
-
pH 8.0, recombinant enzyme from Pichia pastoris
530
-
Bilirubin
-
-
583
-
Bilirubin
-
enzyme immobilized on alginate-silicate beads
20
-
Biliverdin
-
-
94.3
-
ditaurobilirubin
-
pH 5.5, authentic bilirubin oxidase
233
-
ditaurobilirubin
-
pH 5.5, recombinant enzyme from Pichia pastoris
374
-
K4[Fe(CN)6]
-
wild type recombinant enzyme, at pH 7.0 and 25C
1259
-
K4[Fe(CN)6]
-
mutant enzyme M467Q, at pH 7.0 and 25C
60
-
p-phenylenediamine
-
pH 6.5, authentic bilirubin oxidase
90
-
p-phenylenediamine
-
pH 6.5, recombinant enzyme from Pichia pastoris
0.0133
-
syringaldazine
-
at pH 5.3
2.08
-
syringaldazine
-
at about pH 8.0
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
104.3
-
Bilirubin
-
pH 7.5, 25C
8016
1000
-
Bilirubin
A8FAG9
conjugated bilirubin, pH 4.8, temperature not specified in the publication
8016
1513
-
Bilirubin
-
conjugated bilirubin, pH 7.0, 37C
8016
1610
-
Bilirubin
-
conjugated bilirubin, pH 3.6, temperature not specified in the publication
8016
2500
-
Bilirubin
-
unconjugated bilirubin, pH 8.0, temperature not specified in the publication
8016
3000
-
Bilirubin
A8FAG9
unconjugated bilirubin, pH 7.2, temperature not specified in the publication
8016
9800
-
Bilirubin
-
conjugated bilirubin, pH 5.5, temperature not specified in the publication
8016
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00041
-
-
mutant enzyme M467L, using bilirubin as a substrate
0.00047
-
-
mutant enzyme N459A/M467F, using bilirubin as a substrate
0.00051
-
-
enzyme activity in small intestine
0.00064
-
-
mutant enzyme M467F, using bilirubin as a substrate
0.00157
-
-
enzyme activity in liver mitochondria
0.074
-
-
M467G mutant enzyme
0.3
-
-
ferrocyanide oxidase activity of mutant M467G
1.19
-
-
mutant enzyme M467Q, using bilirubin as a substrate
1.2
-
-
bilirubin oxidase activity of mutant D105A
1.67
-
-
mutant I402G
2.83
-
-
commercial preparation, pH not specified in the publication, temperature not specified in the publication
5.5
-
-
mutant 1Ru-C457S
6.42
-
-
mutant 2Ru-C457S
8.03
-
-
enzyme immobilized on alginate-silicate beads
11
-
-
bilirubin oxidase activity of mutant D105E
24
-
-
recombinant wild-type enzyme expressed in Aspergillus oryzae
24
-
-
bilirubin oxidase activity of authentic enzyme; bilirubin oxidase activity of recombinant enzyme
25.4
-
-
purified enzyme with substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), pH 6.0, 24C
30
-
-
authentic enzyme
46.1
-
-
recombinant wild type enzyme, using bilirubin as a substrate
214.3
-
-
purified enzyme after anion exchange chromatography step, pH 7.5, 25C
additional information
-
-
0.02 units/ml, 1 unit is defined as the equivalent amount of enzyme that reduces DELTA A at 440 nm by 1.05/min, enzyme activity in crude extracts
additional information
-
-
0.67 units/ml, 1 unit is defined as the equivalent amount of enzyme that reduces DELTA A at 440 nm by 1.05/min, enzyme activity in crude extracts
additional information
-
-
3.3 units/ml, 1 unit is defined as the equivalent amount of enzyme that reduces DELTA A at 440 nm by 1.05/min, enzyme activity in crude extracts
additional information
-
-
206 units/A280, 1 unit is defined as the equivalent amount of enzyme that reduces DELTA A at 440 nm by 1.05/min, enzyme activity in crude extracts
additional information
-
-
0.0013 mmol O2/min/0.08 mg protein
additional information
-
-
no bilirubin oxidase activity of mutant C457S and mutant D105N
additional information
-
-
mutant C457S shows no activity
additional information
-
-
relative activity 0.09, 0.2 g/l BOD stored in 0.5 g/l poly[ethyleneimine], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.09, 0.2 g/l BOD stored in 2 g/l poly[ethyleneimine], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.17, 0.2 g/l BOD stored in 0.1 M H2PO4--HPO42- buffer system, pH 7.0, 30C, 2 days; relative activity 0.22, 0.2 g/l BOD stored in 0.5 g/l poly[(dimethylimino)-1,6-hexanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.22, 0.2 g/l BOD stored in 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,6-hexanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,6-hexanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.22, 0.2 g/l BOD stored in 2 g/l poly[(dimethylimino)-1,6-hexanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.22, 0.2 g/l BOD stored in 2 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,6-hexanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,6-hexanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.23, 0.2 g/l BOD stored in 0.5 g/l poly(diallydimethylammonium), 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.23, 0.2 g/l BOD stored in 2 g/l poly(diallydimethylammonium), 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.26, 0.2 g/l BOD stored in 0.5 g/l poly[metacrylpropyltrimethylammonium], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.26, 0.2 g/l BOD stored in 2 g/l poly[metacrylpropyltrimethylammonium], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.27, 0.2 g/l BOD stored in 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea], 0.1 M H2PO4--HPO42- buffer system, pH 7.0, 30C, 2 days; relative activity 0.27, 0.2 g/l BOD stored in 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,3-propanediyl], 0.1 M H2PO4--HPO42- buffer system, pH 7.0, 30C, 2 days; relative activity 0.28, 0.2 g/l BOD stored in 0.5 g/l poly[allyamine], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.28, 0.2 g/l BOD stored in 0.5 g/l poly(dimethylamine-co-epichrohydrin), 0.1 M H2PO4--HPO42- buffer system, pH 7.0, 30C, 2 days; relative activity 0.28, 0.2 g/l BOD stored in 2 g/l poly[allyamine], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.30, 0.2 g/l BOD stored in 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.30, 0.2 g/l BOD stored in 2 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.31, 0.2 g/l BOD stored in 0.5 g/l poly[lysine], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.31, 0.2 g/l BOD stored in 2 g/l poly[lysine], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.38, 0.2 g/l BOD stored in 0.5 g/l poly(dimethylamine-co-epichrohydrin), 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.38, 0.2 g/l BOD stored in 2 g/l poly(dimethylamine-co-epichrohydrin), 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.43, 0.2 g/l BOD stored in 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,3-propanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.43, 0.2 g/l BOD stored in 2 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,3-propanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30C, 2 days; relative activity 0.51, 0.2 g/l BOD stored in 0.1 M BisTrisH+-BisTris0 buffer system, pH 7.0, 30C, 2 days; relative activity 0.58, 0.2 g/l BOD stored in 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,3-propanediyl], 0.1 M BisTrisH+-BisTris0 buffer system, pH 7.0, 30C, 2 days; relative activity 0.64, 0.2 g/l BOD stored in 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea], 0.1 M BisTrisH+-BisTris0 buffer system, pH 7.0, 30C, 2 days; relative activity 0.89, 0.2 g/l BOD stored in 0.5 g/l poly(dimethylamine-co-epichrohydrin), 0.1 M BisTrisH+-BisTris0 buffer system, pH 7.0, 30C, 2 days
additional information
-
-
relative activity 0.17, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M H2PO4--HPO42- buffer system, no additive; relative activity 0.19, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M MOPS0-MOPS- buffer system, no additive; relative activity 0.25, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M H2PO4--HPO42- buffer system, 0.5 g/l poly[oxyethylene(dimethylimino)propyl(dimethylimino)ethylene]; relative activity 0.27, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M H2PO4--HPO42- buffer system, 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea]; relative activity 0.27, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M H2PO4--HPO42- buffer system, 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-ethanediyl)-(dimethylimino)-1,3-propanediyl]; relative activity 0.28, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M H2PO4--HPO42- buffer system, 0.5 g/l poly(dimethylamine-co-epichrohydrin); relative activity 0.30, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M MOPS0-MOPS- buffer system, 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea]; relative activity 0.38, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M MOPS0-MOPS- buffer system, 0.5 g/l poly(dimethylamine-co-epichrohydrin); relative activity 0.40, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M MOPS0-MOPS- buffer system, 0.5 g/l poly[oxyethylene(dimethylimino)propyl(dimethylimino)ethylene]; relative activity 0.43, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M MOPS0-MOPS- buffer system, 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-etanediyl)-(dimethylimino)-1,3-propanediyl]; relative activity 0.51, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M BisTrisH+-BisTris0 buffer system, no additive; relative activity 0.58, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M BisTrisH+-BisTris0 buffer system, 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-etanediyl)-(dimethylimino)-1,3-propanediyl]; relative activity 0.64, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M BisTrisH+-BisTris0 buffer system, 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea]; relative activity 0.64, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M BisTrisH+-BisTris0 buffer system, 0.5 g/l poly[oxyethylene(dimethylimino)propyl(dimethylimino)ethylene]; relative activity 0.89, 0.2 g/l BOD stored at 30C for 2 days in 0.1 M BisTrisH+-BisTris0 buffer system, 0.5 g/l poly(dimethylamine-co-epichrohydrin)
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.7
-
-
oxidation of 2,2'-azino-bis(3-ethylbenzthioline-6-sulfonic acid)
4
-
-
optimal for ditaurobilirubin oxidation
4
-
-
using 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate
4.5
-
Myrothecium sp.
-
for the indigo carmine dye decolorization reaction
5
7
-
oxidation of 1,1'-dimethylferrocene, activity decreases above pH 7.5
5
-
-
with substrate remazol brilliant blue R, in absence of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
6
-
-
assay at, substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
6.5
7.5
-
using p-phenylenediamine as a substrate
7
-
-
optimal for bilirubin oxidation
7
-
Myrothecium sp.
-
using Remazol Brilliant Blue R as subsrate
7
-
-
activity assay
7
-
Q9UVY4
BODs display a high activity and stability at neutral pH
7.2
-
-
assay at with bilirubin
7.2
-
-
assay at, with bilirubin as substrate, the oxidation of unconjugated bilirubin can only be measured for pH above 7.0
7.5
-
-
substrate bilirubin
8
8.5
-
using o-aminophenol as a substrate
8
-
-
with substrate remazol brilliant blue R and activating 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
8.2
-
-
oxidation of syringaldazine
8.2
-
-
oxidation of conjugated and unconjugated bilirubin
8.6
-
-
Tris-HCl buffer
8.9
9.2
-
diethylethanolamine buffer
additional information
-
-
the actvity with laccase substrates 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate) and syringaldazine is assayed at pH 3.6 and pH 6.2, respectively
additional information
-
-
BODs display a high activity and stability at neutral pH
additional information
-
Q65MU7
BODs display a high activity and stability at neutral pH
additional information
-
A8FAG9
BODs display a high activity and stability at neutral pH
additional information
-
P07788
BODs display a high activity and stability at neutral pH
additional information
-
-
BODs display a high activity and stability at neutral pH
additional information
-
-
assay with substrates 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine and 2,6-dimethoxyphenol at pH 3.2, pH 6.2, and pH 6.8, respectively
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
4.5
-
using 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate
4
9
Myrothecium sp.
-
for the indigo carmine dye decolorization reaction
4
9
Myrothecium sp.
-
using Remazol Brilliant Blue R as subsrate
4.5
8.2
-
under acidic condition enzyme oxidizes only conjugated bilirubin
5
8.5
-
activity range with substrate remazol brilliant blue R, profile overview
6.5
8
-
using p-phenylenediamine or o-aminophenol as a substrate
8
10
-
at pH 8.0 and 10.0: about 30% of maximum activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24
-
-
assay at, substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
28
-
Myrothecium sp.
-
using Remazol Brilliant Blue R as subsrate
37
-
-
assay at
37
-
-
assay at, with bilirubin as substrate
40
-
Myrothecium sp.
-
for the indigo carmine dye decolorization reaction
40
-
-
with substrate remazol brilliant blue R
40
-
-
substrate bilirubin
55
-
-
enzyme immobilized on alginate-silicate beads
80
-
A8FAG9
-
80
-
P07788
-
80
-
Q9UVY4
-
additional information
-
-
assay with substrate syringaldazine at 25C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
70
-
10C: about 36% of maximum, 70C: about 10% of maximum
20
60
-
20C: about 60% of maximum, 60C: about 40% of maximum
20
60
-
activity range, profile overview
21
37
-
at 24C approximately 50% of the CotA protein is detected in the soluble fraction
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Myrothecium verrucaria 3.2190
-
-
-
Manually annotated by BRENDA team
-
maximum activity in jejunum
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Myrothecium verrucaria 3.2190
-
-
-
-
Manually annotated by BRENDA team
-
inner and outer membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
52000
-
-
gel filtration
59950
-
-
deduced from amino acid sequence
62000
-
Myrothecium sp.
-
SDS-PAGE
66000
-
-
all mutants expressed in Pichia pastoris, SDS-PAGE
68000
-
-
about, native PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 66000, SDS-PAGE
?
-
x * 49000, recombinant glycoslated enzyme, SDS-PAGE, x * 63975, mature protein, after N-terminal cleavage, sequence determination
?
-
x * 35000, folded enzyme, SDS-PAGE, x * 60000-65000, heat denatured, unfolded enzyme, SDS-PAGE, x * 61006, mass spectrometry
?
Magnaporthe oryzae ATCC MYA-4617
-
x * 49000, recombinant glycoslated enzyme, SDS-PAGE, x * 63975, mature protein, after N-terminal cleavage, sequence determination
-
?
Myrothecium verrucaria IMER1
-
x * 63000
-
monomer
-
1 * 64000, difference to deduced MW may be due to glycosylation, SDS-PAGE
monomer
-
1 * 45000-50000, smear, SDS-PAGE
monomer
-
1 * 63000, recombinant wild-type enzyme, SDS-PAGE; 1 * 66000, authentic enzyme, SDS-PAGE
monomer
-
1 * 68100, SDS-PAGE
monomer
Myrothecium verrucaria 3.2190
-
1 * 68100, SDS-PAGE
-
additional information
-
molecular-dynamics simulation of a BOD-mediator complex, mediator is 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), i.e. ABTS, overview
additional information
Myrothecium verrucaria MT-1
-
molecular-dynamics simulation of a BOD-mediator complex, mediator is 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), i.e. ABTS, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
-
two putative N-glycosylation sites at positions 472 and 482
glycoprotein
-
the recombinant enzyme expressed in Pichia pastoris contains non-native type N-linked sugar chains
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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 20C, X-ray diffraction structure determination and analysis at 2.3-2.5 A resolution, modelling
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9.7
-
37C, 60 min
7
-
Q9UVY4
BODs display a high activity and stability at neutral pH
8
-
-
stability drops when 100 mM cetyltrimethyl ammonium bromide are added to the aqueous solution, half-life of inactivation: 1500 min
9.2
9.7
-
5C, 5 days, unstable below pH 9.0
11
-
-
enzyme is completey inactivated above pH 11.0 due to unfolding
additional information
-
-
the reaction of BOD at gold electrodes is shown to be efficient only at low pH
additional information
-
-
BODs display a high activity and stability at neutral pH
additional information
-
Q65MU7
BODs display a high activity and stability at neutral pH
additional information
-
A8FAG9
BODs display a high activity and stability at neutral pH
additional information
-
P07788
BODs display a high activity and stability at neutral pH
additional information
-
-
BODs display a high activity and stability at neutral pH
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
pH 7.4, half-life: 300 h
20
30
-
at pH 2.7
20
60
-
at pH 6.1
20
60
-
1 h incubation at 60C, free enzyme retains 26% of its original activity, immobilized enzyme 73%
20
70
-
at pH 9.0
22
-
-
pH 7.4, half-life: 25 h
37
-
-
15 min, stable up to 37C
37
-
-
soluble enzyme, half-life: 12 h immobilized enzyme, half-life: 63 h
37
-
-
purified recombinant enzyme, half-life for deactivation is more than 300 min
37
-
-
loss of 50% activity after 90 min
37
-
-
half-life over 300 min
37
-
-
purified enzyme, pH 7.0, no activity decrease after preincubation for 300 min
40
50
-
the enzyme activity is stable after incubation for 1 h at a temperature up to 40C, thermal stability is decreased beyond 50?C
40
61
-
sol-gel encapsulated BOD shows no decrease in relative activity until over 50C while free enzyme loses some 40% activity at 40C
50
70
-
the half life of BOD at 50C is 114 min, residual activity after 30 min at 50C is 83.3% of the original activity, at 70C BOD activity disappears within several min
60
-
-
half-life of the recombinant enzyme expressed in Escherichia coli is 90 min, half-life of authentic enzyme is 15 min
60
-
-
irreversible thermal inactivation, dynamics and kinetics, overview
60
-
-
purified recombinant enzyme, half-life for deactivation is about 70 min
60
-
-
half-life over 70 min
60
-
-
half-life of the wild-type enzyme is 15 min, and of the recombinant enzyme 90 min
65
-
-
stable for 60 min
70
-
-
lyophilized enzyme stored at 70C in the presence of polyvinylalcohol for 5 h, 40% of acitivity are lost after rehydration
70
-
-
lyophilized enzyme stored at 70C in the presence of alpha,beta-poly(N-hydroxyethyl)-L-aspartamide for 5 h, about 10% of acitivity are lost after rehydration
80
-
Q65MU7
half-life above 100 min at 80C
80
-
A8FAG9
half-life above 100 min at 80C
80
-
P07788
half-life above 100 min at 80C
80
-
-
half-life above 100 min at 80C
80
-
Q9UVY4
half-life above 100 min at 80C
80
-
-
purified enzyme, pH 7.0, less than 50% loss in activity after preincubation for 90 min
84
-
-
stable for 30 min
100
-
-
5 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
after an incubation of 8 days at physiological conditions, the enzyme loses 15% of its activity
-
the recombinant enzyme shows high tolerance towards urea
-
bilirubin oxidase-coated carbon cathode operates for more than 1 week at 37C in a glucose-containing physiological buffer solution. The cathode is short-lived in serum, losing its electrocatalytic activity in a few hours, caused by a product of the reaction of urate and dissolved oxygen. Exclusion of urate, by application of Nafion(TM) film in the cathode, improves the stability in serum
Myrothecium sp.
-
BOD can undergo non-catalytic direct electron transfer between enzyme and carbon electrode and retains its catalytic activity, 1%-2% of the immobilized BOD (as a first monolayer on the electrode surface) participates in direct electrical communication with a carbon electrode
-
immobilized enzyme, increased heat stability
-
multi-walled carbon nanotube modification of glassy carbon electrodes strongly enhances the oxygen reduction of bilirubin oxidase compared to unmodified electrodes, the quasi-reversible redox reaction might be attributed to the trinuclear T2/T3 cluster of BOD, a BOD-multi-walled carbon nanotube-modified electrode retains 70% of the initial activity for oxygen reduction after 4 days
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
chloroform
-
chloroform-n-heptane mixture, preparations of enzyme lyophilized from N-(2-hydroxyethyl)-piperazine-N'-(3-propane-sulfonic acid) buffer suspended in 50:50 v/v chloroform-n-heptane mixture are activ if more than 0.081% v/v water are present in the two-phase system
chloroform
-
water-in-oil cetyltrimethyl ammonium bromide microemulsions of the enzyme, 60% of activity decay with a rate constant of 0.0183/min, 40% are lost at a rate constant of 0.000278/min
n-heptane
-
chloroform-n-heptane mixture, preparations of enzyme lyophilized from N-(2-hydroxyethyl)-piperazine-N'-(3-propane-sulfonic acid) buffer suspended in 50:50 v/v chloroform-n-heptane mixture are active if more than 0.081% v/v water are present in the two-phase system
n-heptane
-
water-in-oil cetyltrimethyl ammonium bromide microemulsions of the enzyme, 60% of activity decay with a rate constant of 0.0183/min, 40% are lost at a rate constant of 0.000278/min
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 50 mM phosphate buffer, pH 7.4, less than 10% activity are lost after 2 days
-
5C, pH 9.2-9.7, 5 d
-
freeze-dried, rehydrated at 15C in the presence of trehalose, 20% loss of activity
-
immobilized enzyme, 4C or 25, stable for at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by gel filtration
-
by gel filtration
-
to homogeneity
-
recombinant holo-enzyme from Pichia pastoris strain GS115 to homogeneity by hydrophobic interaction chromatography
-
DEAE-Sepharose Fast Flow column chromatography and Sephadex G-100 gel filtration
Myrothecium sp.
-
ammonium sulfate, charcoal, Sephadex a-50, Sephadex G-100
-
by gel filtration
-
extracellular enzyme 3.92fold by ammonium sulfate fractionation and anion exchange chromatography, an additional step of gel filtration lowers the enzyme purity and amount
-
native enzyme by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
native enzyme by anion exchange chromatography and hydrophobic interaction chromatography
-
recombinant enzyme
-
recombinant wild-type enzyme and mutants
-
to homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Escherichia coli JM109 transformed with pUC119 carrying the CotA gene, produces large amounts of the soluble protein under low-temperature conditions
-
overexpression of holo-enzyme in Pichia pastoris strain GS115, subcloning in Escherichia coli strain DH5alpha
-
expressed in Pichia pastoris
-
expressed in Pichia pastoris and Aspergillus oryzae
-
expression in Aspergillus oryzae
-
expression in Aspergillus oryzae, enzyme is in a resting form different from that of authentic bilirubin oxidase, but reaches the resting form of the authentic enzyme after one cycle of reduction and reoxidation with dioxygen
-
expression in Aspergillus oryzae; expression of H94V, H134/136V, C457V, C457A and H456/458V mutants in Aspergillus oryzae
-
expression in Pichia pastoris. The cDNA encoding bilirubin oxidase is cloned into the Pichia pastoris expression vector pPIC9K under the control of the alcohol oxidase 1 promoter and its protein product is secreted using the Saccharomyces alpha-mating factor signal sequence
-
expression in Saccharomyces cerevisiae
-
Pichia pastoris GS115 transformed using the pPICBO derivative linearized with Bpu1102I
-
recombinant expression in Pichia pastoris
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C457S
-
virtually no enzyme activity, Ru-incorporation conferrs higher enzyme activity
I402G
-
low enzyme activity
biotechnology
-
bilirubin oxidase has been found to be the best enzyme for converting O2 to H2O as a cathodic enzyme in biofuel cells
C457A
-
no oxidase activity
C457S
-
can react with dioxygen, affords reaction intermediate I with absorption maxima at 340, 470, and 675 nm
C457V
-
no oxidase activity
D105A
-
exhibits 7.5% bilirubin oxidase activity compared to the wild-type enzyme, indicating that Asp105 conserved in all multi-copper oxidases donates a proton to reaction intermediates I and II
D105E
-
exhibits 46% bilirubin oxidase activity compared to the wild-type enzyme, indicating that Asp105 conserved in all multi-copper oxidases donates a proton to reaction intermediates I and II
D105N
-
does not react with dioxygen
E463Q
-
site-directed mutagenesis
H134/136V
-
no oxidase activity
H456/458V
-
no oxidase activity
H456D/H458D
-
mutant with weak bilirubin oxidase and ferroxidase activity
H456K/H458K
-
mutant with weak bilirubin oxidase and ferroxidase activity
H456V/H458V
-
inactive mutant
H94V
-
no oxidase activity
M467F
-
the mutated type I Cu center shows characteristics of phytocyanins
M467G
-
weak oxidase activity
M467G
-
with modified spectroscopic properties and redox potential, affords reaction intermediate II with absorption maxima at 355 and 450 nm
M467L
-
the mutated type I Cu center shows characteristics of phytocyanins
M467Q
-
the enzymatic activity of the mutant is very low toward bilirubin but it works as a good catalyst in direct electron transfer-type bioelectrocatalytic reduction of dioxygen into water, the kcat value is 3fold increased
N459A/M467F
-
activity is decreased to 1% of the recombinant wild type enzyme, the mutated type I Cu center shows characteristics of phytocyanins, blue copper proteins with an axial coordination of Gln, due to compensatory binding of the distal Asn459
Met467Q
-
reduced activity
additional information
-
attachment of the purified enzyme to a PGE surface, from pyrolytic graphite plates, modified with 6-amino-2-naphthoic acid, modifiers tested in increasing activity are 4-aminothiophenol, 4-aminobenzonitrile, 2-aminoacridine, 2-aminoanthracene, 1-aminoanthracene, 2-aminochrysene, 4-benzyloxyaniline, 4-aminobenzoic acid, 4-aminophenylacetic acid, 6-amino-2-naphthoic acid, the latter giving best results. Method optimization, cyclic voltammetry measuring the electrocatalytic reduction of dioxygen by platinum electrodeposited on PGE, detailed overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
diagnostics
-
the BOD activity catalyzing the oxidation of bilirubin to biliverdin can be used for the diagnosis of jaundice and hyperbilirubinemia
environmental protection
Magnaporthe oryzae ATCC MYA-4617
-
the BOD from Magnaporthe oryzae is efficient in decolorizing textile dyes such as Remazol brilliant Blue R, making it useful for environmentally friendly industrial applications
-
biotechnology
Myrothecium sp.
-
the wired' enzyme is superior to pure platinum as a electrocatalyst of the four-electron electroreduction of O2 to water. The 'wired' bilirubin oxidase-coated carbon cathode operates for more than 1 week at 37C in a glucose-containing physiological buffer solution. Key application would be in a glucose-O2 biofuel cell. The cathode is short-lived in serum, losing its electrocatalytic activity in a few hours. The damaging serum component is a product of the reaction of urate and dissolved oxygen. Exclusion of urate, by application of Nafion(TM) film in the cathode, improves the stability in serum
biotechnology
Myrothecium sp.
-
the enzyme functions effectively as the biocathode of a H2/O2 biofuel cell. It is immmobilized as a multiple layer in a cationic polymer (poly-L-lysine) matrix on an electrode surface. The BOD-modified electrode catalyzes four-electron reduction of O2 to water without any mediator, to produce a diffusion-controlled voltammogram for the O2 reduction in a quiescent solution. Construction of such a multiple enzyme layer is useful for increasing the current density even in direct electron transfer-type bioelectrocatalysis
analysis
-
immobilized onto aminopropyl and arylamine glass beads to form an enzyme bioreactor
analysis
-
enzyme activity in serum bilirubin assays can be monitored by capillary electrophoresis
analysis
-
sandwich-type enzyme-amplified amperometric detection of DNA with ambient O2 as the substrate at neutral pH in the presence of chloride
analysis
-
application of polyammonium cations to enzyme-immobilized electrode: application as enzyme stabilizer for bilirubin oxidase
analysis
-
application of poly[oxyethylene(dimethylimino)propyl-(dimethylimino)ethylene] as enzyme stabilizer for bilirubin oxidase immobilized electrode
analysis
-
BOD has attracted considerable attention as an enzymatic catalyst for the cathode of biofuel cells that work under neutral conditions
diagnostics
-
BOD is used for diagnostic analysis of bilirubin in serum
environmental protection
-
BOX can be used to decolorize synthetic dyes from effluents, especially for anthraquinonic dyes
industry
-
BOX can be used to decolorize synthetic dyes from effluents, especially for anthraquinonic dyes
medicine
-
immobilized bilirubin oxidase reactor could be used for the degradation of bilirubin in neonatal jaundice
environmental protection
Myrothecium verrucaria IMER1
-
BOX can be used to decolorize synthetic dyes from effluents, especially for anthraquinonic dyes
-
industry
Myrothecium verrucaria IMER1
-
BOX can be used to decolorize synthetic dyes from effluents, especially for anthraquinonic dyes
-
analysis
Myrothecium verrucaria MT-1
-
BOD has attracted considerable attention as an enzymatic catalyst for the cathode of biofuel cells that work under neutral conditions
-
medicine
-
mutants I402G and C457S are not appropriate for diagnostic purpose due to their much lower enzyme activities compared to the recombinant enzyme
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
Q65MU7
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
energy production
-
the BOD from Bacillus pumilus is an attractive candidate for application in biofuel cells and biosensors showing high activity at neutral pH and high tolerance towards NaCl
additional information
A8FAG9
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
medicine
-
great potential for use as a diagnostic reagent, can be used for accurate determination of serum bilirubin levels in patients with hepatobiliary disease
additional information
P07788
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
additional information
-
redox potential of the T1 site of BOD is > 650 mV vs. NHE, redox potential of the T2 site is near 390 mV vs. NHE
additional information
-
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
environmental protection
-
the BOD from Magnaporthe oryzae is efficient in decolorizing textile dyes such as Remazol brilliant Blue R, making it useful for environmentally friendly industrial applications
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
-
redox potential of the T1 site of BOD is close to 670 mV vs. NHE, redox potential of the T2 site is near 390 mV vs. NHE
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
-
the purified bilirubin oxidase in Myrothecium verrucaria strain has potential application in dye effluent decolorization. Extracellular bilirubin oxidase decolorizes indigo carmine, biosorption and biodegradation of the dye is achieved with more than 98% decolorization efficiency after 7 days at 26C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30C to 50C and pH 5.5-9.5 with dye concentrations of 50-200 mg/ml
additional information
Myrothecium verrucaria 3.2190
-
the purified bilirubin oxidase in Myrothecium verrucaria strain has potential application in dye effluent decolorization. Extracellular bilirubin oxidase decolorizes indigo carmine, biosorption and biodegradation of the dye is achieved with more than 98% decolorization efficiency after 7 days at 26C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30C to 50C and pH 5.5-9.5 with dye concentrations of 50-200 mg/ml
-
diagnostics
Myrothecium verrucaria MT-1
-
BOD is used for diagnostic analysis of bilirubin in serum
-
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
Q9UVY4
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions