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Literature summary extracted from

  • Mano, N.
    Features and applications of bilirubin oxidases (2012), Appl. Microbiol. Biotechnol., 96, 301-307.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Pyricularia oryzae
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Aspergillus sojae
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Penicillium janthinellum
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Ganoderma tsunodae
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Albifimbria verrucaria
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Pleurotus ostreatus
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Bacillus subtilis
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Bacillus licheniformis
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Bacillus pumilus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.3.5 recombinant expression in Pichia pastoris Albifimbria verrucaria

General Stability

EC Number General Stability Organism
1.3.3.5 after an incubation of 8 days at physiological conditions, the enzyme loses 15% of its activity Pyricularia oryzae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.3.5 DTT
-
 Ganoderma tsunodae
1.3.3.5 EDTA
-
 Ganoderma tsunodae
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Albifimbria verrucaria
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Aspergillus sojae
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Bacillus licheniformis
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators, the enzyme from Bacillus pumilus is urate-, DTT-, and EDTA-insensitive Bacillus pumilus
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Bacillus subtilis
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Ganoderma tsunodae
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Penicillium janthinellum
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Pleurotus ostreatus
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators, the enzyme from Magnaporthe oryzae is urate-, DTT-, and EDTA-insensitive Pyricularia oryzae
1.3.3.5 Urate
-
 Ganoderma tsunodae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.3.5 0.008
-
 bilirubin unconjugated bilirubin, pH 7.0, temperature not specified in the publication Bacillus subtilis
1.3.3.5 0.015
-
 bilirubin conjugated bilirubin, pH 7.0, temperature not specified in the publication Bacillus subtilis
1.3.3.5 0.018
-
 bilirubin conjugated bilirubin, pH 3.6, temperature not specified in the publication Pyricularia oryzae
1.3.3.5 0.022
-
 bilirubin unconjugated bilirubin, pH 7.2, temperature not specified in the publication Bacillus pumilus
1.3.3.5 0.035
-
 bilirubin conjugated bilirubin, pH 4.8, temperature not specified in the publication Bacillus pumilus
1.3.3.5 0.12
-
 bilirubin conjugated bilirubin, pH 5.5, temperature not specified in the publication Albifimbria verrucaria
1.3.3.5 0.37
-
 bilirubin unconjugated bilirubin, pH 8.0, temperature not specified in the publication Albifimbria verrucaria

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.3.5 Cu2+ bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains Pyricularia oryzae
1.3.3.5 Cu2+ bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains Aspergillus sojae
1.3.3.5 Cu2+ bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains Penicillium janthinellum
1.3.3.5 Cu2+ bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains Ganoderma tsunodae
1.3.3.5 Cu2+ bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains Albifimbria verrucaria
1.3.3.5 Cu2+ bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains Pleurotus ostreatus
1.3.3.5 Cu2+ bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains Bacillus subtilis
1.3.3.5 Cu2+ bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains Bacillus licheniformis
1.3.3.5 Cu2+ bilirubin oxidase utilizes four Cu+/2+ ions to reduce O2 to water. It contains four histidine-rich copper-binding domains Bacillus pumilus
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Pyricularia oryzae
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Aspergillus sojae
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Penicillium janthinellum
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Ganoderma tsunodae
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Albifimbria verrucaria
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Pleurotus ostreatus
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Bacillus subtilis
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Bacillus licheniformis
1.3.3.5 additional information BODs display a high tolerance towards chloride anions and other chelators Bacillus pumilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.3.5 2 bilirubin + O2 Pyricularia oryzae
-
 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2 Aspergillus sojae
-
 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2 Penicillium janthinellum
-
 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2 Ganoderma tsunodae
-
 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2 Albifimbria verrucaria
-
 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2 Pleurotus ostreatus
-
 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2 Bacillus subtilis
-
 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2 Bacillus licheniformis
-
 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2 Bacillus pumilus
-
 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 additional information Pyricularia oryzae 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 ?
-
 ?
1.3.3.5 additional information Aspergillus sojae 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 ?
-
 ?
1.3.3.5 additional information Penicillium janthinellum 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 ?
-
 ?
1.3.3.5 additional information Ganoderma tsunodae 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 ?
-
 ?
1.3.3.5 additional information Albifimbria verrucaria 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 ?
-
 ?
1.3.3.5 additional information Pleurotus ostreatus 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 ?
-
 ?
1.3.3.5 additional information Bacillus subtilis 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 ?
-
 ?
1.3.3.5 additional information Bacillus licheniformis 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 ?
-
 ?
1.3.3.5 additional information Bacillus pumilus 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.5 Albifimbria verrucaria Q12737
-
-
1.3.3.5 Aspergillus sojae
-
-
-
1.3.3.5 Bacillus licheniformis Q65MU7
-
-
1.3.3.5 Bacillus pumilus A8FAG9
-
-
1.3.3.5 Bacillus subtilis P07788
-
-
1.3.3.5 Ganoderma tsunodae
-
-
-
1.3.3.5 Penicillium janthinellum
-
-
-
1.3.3.5 Pleurotus ostreatus Q9UVY4
-
-
1.3.3.5 Pyricularia oryzae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.5 2 bilirubin + O2
-
 Pyricularia oryzae 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2
-
 Aspergillus sojae 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2
-
 Penicillium janthinellum 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2
-
 Ganoderma tsunodae 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2
-
 Albifimbria verrucaria 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2
-
 Pleurotus ostreatus 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2
-
 Bacillus subtilis 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2
-
 Bacillus licheniformis 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 2 bilirubin + O2
-
 Bacillus pumilus 2 biliverdin + 2 H2O
-
 ?
1.3.3.5 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 Pyricularia oryzae ?
-
 ?
1.3.3.5 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 Aspergillus sojae ?
-
 ?
1.3.3.5 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 Penicillium janthinellum ?
-
 ?
1.3.3.5 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 Ganoderma tsunodae ?
-
 ?
1.3.3.5 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 Albifimbria verrucaria ?
-
 ?
1.3.3.5 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 Pleurotus ostreatus ?
-
 ?
1.3.3.5 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 Bacillus subtilis ?
-
 ?
1.3.3.5 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 Bacillus licheniformis ?
-
 ?
1.3.3.5 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 Bacillus pumilus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.3.5 BOD
-
 Pyricularia oryzae
1.3.3.5 BOD
-
 Aspergillus sojae
1.3.3.5 BOD
-
 Penicillium janthinellum
1.3.3.5 BOD
-
 Albifimbria verrucaria
1.3.3.5 BOD
-
 Bacillus licheniformis
1.3.3.5 BOD
-
 Bacillus pumilus
1.3.3.5 CotA
-
 Ganoderma tsunodae
1.3.3.5 CotA
-
 Pleurotus ostreatus
1.3.3.5 CotA
-
 Bacillus subtilis
1.3.3.5 CotA
-
 Bacillus licheniformis
1.3.3.5 CotA
-
 Bacillus pumilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.3.5 40
-
-
 Albifimbria verrucaria
1.3.3.5 60
-
-
 Pyricularia oryzae
1.3.3.5 80
-
-
 Ganoderma tsunodae
1.3.3.5 80
-
-
 Pleurotus ostreatus
1.3.3.5 80
-
-
 Bacillus subtilis
1.3.3.5 80
-
-
 Bacillus licheniformis
1.3.3.5 80
-
-
 Bacillus pumilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.3.3.5 37
-
 half-life over 300 min Pyricularia oryzae
1.3.3.5 37
-
 loss of 50% activity after 90 min Ganoderma tsunodae
1.3.3.5 60
-
 half-life of the wild-type enzyme is 15 min, and of the recombinant enzyme 90 min Albifimbria verrucaria
1.3.3.5 60
-
 half-life over 70 min Pyricularia oryzae
1.3.3.5 80
-
 half-life above 100 min at 80°C Ganoderma tsunodae
1.3.3.5 80
-
 half-life above 100 min at 80°C Pleurotus ostreatus
1.3.3.5 80
-
 half-life above 100 min at 80°C Bacillus subtilis
1.3.3.5 80
-
 half-life above 100 min at 80°C Bacillus licheniformis
1.3.3.5 80
-
 half-life above 100 min at 80°C Bacillus pumilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.3.5 29
-
 bilirubin conjugated bilirubin, pH 3.6, temperature not specified in the publication Pyricularia oryzae
1.3.3.5 67
-
 bilirubin conjugated bilirubin, pH 4.8, temperature not specified in the publication Bacillus pumilus
1.3.3.5 70
-
 bilirubin unconjugated bilirubin, pH 7.2, temperature not specified in the publication Bacillus pumilus
1.3.3.5 94.3
-
 bilirubin unconjugated bilirubin, pH 8.0, temperature not specified in the publication Albifimbria verrucaria
1.3.3.5 117
-
 bilirubin conjugated bilirubin, pH 5.5, temperature not specified in the publication Albifimbria verrucaria

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Pyricularia oryzae
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Aspergillus sojae
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Penicillium janthinellum
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Ganoderma tsunodae
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Albifimbria verrucaria
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Bacillus subtilis
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Bacillus licheniformis
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Bacillus pumilus
1.3.3.5 7
-
 BODs display a high activity and stability at neutral pH Pleurotus ostreatus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Pyricularia oryzae
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Aspergillus sojae
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Penicillium janthinellum
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Ganoderma tsunodae
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Albifimbria verrucaria
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Bacillus subtilis
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Bacillus licheniformis
1.3.3.5 additional information
-
 BODs display a high activity and stability at neutral pH Bacillus pumilus
1.3.3.5 7
-
 BODs display a high activity and stability at neutral pH Pleurotus ostreatus

General Information

EC Number General Information Comment Organism
1.3.3.5 evolution bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions Pyricularia oryzae
1.3.3.5 evolution bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions Aspergillus sojae
1.3.3.5 evolution bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions Penicillium janthinellum
1.3.3.5 evolution bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions Ganoderma tsunodae
1.3.3.5 evolution bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions Albifimbria verrucaria
1.3.3.5 evolution bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions Pleurotus ostreatus
1.3.3.5 evolution bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions Bacillus subtilis
1.3.3.5 evolution bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions Bacillus licheniformis
1.3.3.5 evolution bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu+/2+ ions Bacillus pumilus
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Pyricularia oryzae
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Aspergillus sojae
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Penicillium janthinellum
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Ganoderma tsunodae
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Albifimbria verrucaria
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Pleurotus ostreatus
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Bacillus subtilis
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Bacillus licheniformis
1.3.3.5 additional information BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions Bacillus pumilus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.3.3.5 1000
-
 bilirubin conjugated bilirubin, pH 4.8, temperature not specified in the publication Bacillus pumilus
1.3.3.5 1610
-
 bilirubin conjugated bilirubin, pH 3.6, temperature not specified in the publication Pyricularia oryzae
1.3.3.5 2500
-
 bilirubin unconjugated bilirubin, pH 8.0, temperature not specified in the publication Albifimbria verrucaria
1.3.3.5 3000
-
 bilirubin unconjugated bilirubin, pH 7.2, temperature not specified in the publication Bacillus pumilus
1.3.3.5 9800
-
 bilirubin conjugated bilirubin, pH 5.5, temperature not specified in the publication Albifimbria verrucaria