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Information on EC 1.3.3.5 - bilirubin oxidase and Organism(s) Bacillus subtilis and UniProt Accession P07788

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EC Tree
     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.3 With oxygen as acceptor
                1.3.3.5 bilirubin oxidase
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Select one or more organisms in this record: ?
This record set is specific for:
Bacillus subtilis
UNIPROT: P07788 not found.
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
bilirubin oxidase, multicopper oxidase, copper oxidase, mvbod, blue cu enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bilirubin oxidase
-
-
-
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bilirubin oxidase M-1
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-
-
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oxidase, bilirubin
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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-
-
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SYSTEMATIC NAME
IUBMB Comments
bilirubin:oxygen oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
80619-01-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
?
bilirubin + O2
biliverdin + H2O
show the reaction diagram
-
CotA with markedly higher affinity for bilirubin than conventional bilirubin oxidase
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-
?
ditaurobilirubin + O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
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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
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
-
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains
additional information
BODs display a high tolerance towards chloride anions and other chelators
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
BODs display a high tolerance towards chloride anions and other chelators
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008 - 0.015
bilirubin
0.008
bilirubin
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-
0.015
ditaurobilirubin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
optimal for ditaurobilirubin oxidation
7
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optimal for bilirubin oxidation
additional information
BODs display a high activity and stability at neutral pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21 - 37
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at 24°C approximately 50% of the CotA protein is detected in the soluble fraction
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions
additional information
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
BODs display a high activity and stability at neutral pH
724076
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
half-life above 100 min at 80°C
65
-
stable for 60 min
84
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stable for 30 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli JM109 transformed with pUC119 carrying the CotA gene, produces large amounts of the soluble protein under low-temperature conditions
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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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
BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sakasegawa, S.; Ishikawa, H.; Imamura, S.; Sakuraba, H.; Goda, S.; Ohshima, T.
Bilirubin oxidase activity of Bacillus subtilis CotA
Appl. Environ. Microbiol.
72
972-975
2006
Bacillus subtilis
Manually annotated by BRENDA team
Mano, N.
Features and applications of bilirubin oxidases
Appl. Microbiol. Biotechnol.
96
301-307
2012
Aspergillus sojae, Penicillium janthinellum, Pyricularia oryzae, Ganoderma tsunodae, Bacillus pumilus (A8FAG9), Bacillus subtilis (P07788), Albifimbria verrucaria (Q12737), Bacillus licheniformis (Q65MU7), Pleurotus ostreatus (Q9UVY4)
Manually annotated by BRENDA team