Bilirubin oxidase
| bilirubin oxidase | |||||||||
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Cartoon representation of the X-ray structure of bilirubin oxidase from Myrothecium verrucaria based on PDB accession code 2xll. The protein ribbon is rainbow colored with the N-terminus in blue and the C-terminus in red. The four copper atoms are shown as spheres and the glycans shown as sticks. | |||||||||
| Identifiers | |||||||||
| EC number | 1.3.3.5 | ||||||||
| CAS number | 80619-01-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a bilirubin oxidase (EC 1.3.3.5) is an enzyme that catalyzes the chemical reaction
- 2 bilirubin + O2 2 biliverdin + 2 H2O
Thus, the two substrates of this enzyme are bilirubin and O2, whereas its two products are biliverdin and H2O.
This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. The systematic name of this enzyme class is bilirubin:oxygen oxidoreductase. This enzyme is also called bilirubin oxidase M-1. This enzyme participates in porphyrin and chlorophyll metabolism.[1][2]
Two structures of bilirubin oxidase from the ascomycete Myrothecium verrucaria have been deposited in the Protein Data Bank (accession codes 3abg and 2xll).[3][4]
References
- ↑ Murao S; Tanaka N (1981). "A new enzyme bilirubin oxidase produced by Myrothecium verrucaria MT-1". Agric. Biol. Chem. 45: 2383–2384. doi:10.1271/bbb1961.45.2383.
- ↑ Tanaka N; Murao S (1985). "Reaction of bilirubin oxidase produced by Myrothecium verrucaria MT-1. Agr". Biol. Chem. 49: 843–844. doi:10.1271/bbb1961.49.843.
- ↑ Mizutani, Kimihiko; Toyoda, Mayuko; Sagara, Kenta; Takahashi, Nobuyuki; Sato, Atsuko; Kamitaka, Yuji; Tsujimura, Seiya; Nakanishi, Yuji; Sugiura, Toshiyuki; Yamaguchi, Shotaro; Kanob, Kenji; Mikamia, Bunzo (2010), "X-ray analysis of bilirubin oxidase from Myrothecium verrucaria at 2.3 Å resolution using a twinned crystal", Acta Crystallogr. F, 66 (7): 765–770, doi:10.1107/S1744309110018828
- ↑ Cracknell, James A.; McNamara, Thomas P.; Lowe, Edward D.; Blanford, Christopher F. (2011), "Bilirubin oxidase from Myrothecium verrucaria: X-ray determination of the complete crystal structure and a rational surface modification for enhanced electrocatalytic O2 reduction", Dalton Trans., 40 (25): 765–770, doi:10.1039/c0dt01403f
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