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Literature summary for 1.3.3.5 extracted from

  • Durand, F.; Kjaergaard, C.H.; Suraniti, E.; Gounel, S.; Hadt, R.G.; Solomon, E.I.; Mano, N.
    Bilirubin oxidase from Bacillus pumilus: a promising enzyme for the elaboration of efficient cathodes in biofuel cells (2012), Biosens. Bioelectron., 35, 140-146.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
diagnostics the BOD activity catalyzing the oxidation of bilirubin to biliverdin can be used for the diagnosis of jaundice and hyperbilirubinemia Bacillus pumilus
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 Bacillus pumilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.022
-
bilirubin unconjugated bilirubin, pH 7.2, 37°C Bacillus pumilus
0.0351
-
bilirubin conjugated bilirubin, pH 7.2, 37°C Bacillus pumilus

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ the enzyme is a multicopper oxidase, MCO, whhich contains 4 copper ions per enzyme molecule Bacillus pumilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
x * 35000, folded enzyme, SDS-PAGE, x * 60000-65000, heat denatured, unfolded enzyme, SDS-PAGE, x * 61006, mass spectrometry Bacillus pumilus
61006
-
x * 35000, folded enzyme, SDS-PAGE, x * 60000-65000, heat denatured, unfolded enzyme, SDS-PAGE, x * 61006, mass spectrometry Bacillus pumilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 bilirubin + O2 Bacillus pumilus the enzyme from Bacillus pumilus shows higher turnover activity towards bilirubin compared to other bacterial MCOs 2 biliverdin + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Bacillus pumilus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 bilirubin + O2 the enzyme from Bacillus pumilus shows higher turnover activity towards bilirubin compared to other bacterial MCOs Bacillus pumilus 2 biliverdin + 2 H2O
-
?
2 bilirubin + O2 substrates are unconjugated bilirubin and conjugated bilirubin Bacillus pumilus 2 biliverdin + 2 H2O
-
?
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 Bacillus pumilus ?
-
?

Subunits

Subunits Comment Organism
? x * 35000, folded enzyme, SDS-PAGE, x * 60000-65000, heat denatured, unfolded enzyme, SDS-PAGE, x * 61006, mass spectrometry Bacillus pumilus

Synonyms

Synonyms Comment Organism
BOD
-
Bacillus pumilus
CotA
-
Bacillus pumilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
-
assay with substrate syringaldazine at 25°C Bacillus pumilus
37
-
assay at, with bilirubin as substrate Bacillus pumilus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
purified enzyme, pH 7.0, no activity decrease after preincubation for 300 min Bacillus pumilus
80
-
purified enzyme, pH 7.0, less than 50% loss in activity after preincubation for 90 min Bacillus pumilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
66.8
-
bilirubin conjugated bilirubin, pH 7.2, 37°C Bacillus pumilus
70
-
bilirubin unconjugated bilirubin, pH 7.2, 37°C Bacillus pumilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
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 Bacillus pumilus
7.2
-
assay at, with bilirubin as substrate, the oxidation of unconjugated bilirubin can only be measured for pH above 7.0 Bacillus pumilus

General Information

General Information Comment Organism
evolution the enzyme is a CotA multicopper oxidase, MCO Bacillus pumilus