| 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 no. | 1.3.3.5 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
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In enzymology, a bilirubin oxidase, BOD or BOx, (EC 1.3.3.5) is an enzyme encoded by a gene in various organisms that catalyzes the chemical reaction
- 2 bilirubin + O2 2 biliverdin + 2 H2O
2 biliverdin + 2 H2OThis 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. It is widely studied as a catalyst for oxygen reduction.
Two structures of bilirubin oxidase from the ascomycete Myrothecium verrucaria have been deposited in the Protein Data Bank (accession codes 3abg and 2xll).
The active site consists of four copper centers, reminiscent of laccase. These centers are classified as type I (cys, met, his, his), type II (3his), and two type III (2his). The latter two centers are arranged in a trinuclear copper cluster forming the active site for oxygen reduction. The type I copper center is the primary electron acceptor and the site for the reduction of bilirubin.
References
- Mano N, Edembe L (December 2013). "Bilirubin oxidases in bioelectrochemistry: features and recent findings". Biosensors & Bioelectronics. 50: 478–485. doi:10.1016/j.bios.2013.07.014. PMID 23911663.
- Mizutani K, Toyoda M, Sagara K, Takahashi N, Sato A, Kamitaka Y, et al. (July 2010). "X-ray analysis of bilirubin oxidase from Myrothecium verrucaria at 2.3 A resolution using a twinned crystal". Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 66 (Pt 7): 765–770. doi:10.1107/S1744309110018828. PMC 2898457. PMID 20606269.
- Cracknell JA, McNamara TP, Lowe ED, Blanford CF (July 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 Transactions. 40 (25): 6668–6675. doi:10.1039/c0dt01403f. PMID 21544308.
- Jones SM, Solomon EI (March 2015). "Electron transfer and reaction mechanism of laccases". Cellular and Molecular Life Sciences. 72 (5): 869–883. doi:10.1007/s00018-014-1826-6. PMC 4323859. PMID 25572295.
- Mano N, de Poulpiquet A (March 2018). "O2 Reduction in Enzymatic Biofuel Cells" (PDF). Chemical Reviews. 118 (5): 2392–2468. doi:10.1021/acs.chemrev.7b00220. PMID 28930449.
Further reading
- Murao S, Tanaka N (1981). "A new enzyme bilirubin oxidase produced by Myrothecium verrucaria MT-1". Agricultural and Biological Chemistry. 45 (10): 2383–2384. doi:10.1271/bbb1961.45.2383.
- Tanaka N, Murao S (1985). "Reaction of bilirubin oxidase produced by Myrothecium verrucaria MT-1". Agricultural and Biological Chemistry. 49 (3): 843–844. doi:10.1271/bbb1961.49.843.
| Oxidoreductases: CH–CH oxidoreductases (EC 1.3) | |
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| 1.3.1: NAD/NADP acceptor | |
| 1.3.3: Oxygen acceptor | |
| 1.3.5: Quinone | |
| 1.3.99: Other acceptors | |
| Enzymes | |
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| Activity | |
| Regulation | |
| Classification | |
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