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词条 Bilirubin oxidase
释义

  1. References

{{enzyme
| Name = bilirubin oxidase
| EC_number = 1.3.3.5
| CAS_number = 80619-01-8
| IUBMB_EC_number = 1/3/3/5
| GO_code = 0047705
| image = MvBO_2xll_thumb.png
| width = 220px
| caption = Cartoon representation of the X-ray structure of bilirubin oxidase from Myrothecium verrucaria based on PDB accession code {{PDB link|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.
}}

In enzymology, a bilirubin oxidase ({{EC number|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

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 {{PDB link|3abg}} and {{PDB link|2xll}}).[3][4]

References

1. ^{{cite journal |author1 = Murao S |author2 =Tanaka N | year = 1981 | title = A new enzyme bilirubin oxidase produced by Myrothecium verrucaria MT-1 | journal = Agric. Biol. Chem. | volume = 45 | pages = 2383–2384 | doi=10.1271/bbb1961.45.2383}}
2. ^{{cite journal |author1 = Tanaka N |author2 =Murao S | year = 1985 | title = Reaction of bilirubin oxidase produced by Myrothecium verrucaria MT-1. Agr | journal = Biol. Chem. | volume = 49 | pages = 843–844 | doi=10.1271/bbb1961.49.843}}
3. ^{{cite journal | vauthors = Mizutani K, Toyoda M, Sagara K, Takahashi N, Sato A, Kamitaka Y, Tsujimura S, Nakanishi Y, Sugiura T, Yamaguchi S, Kano K, Mikami B | title = X-ray analysis of bilirubin oxidase from Myrothecium verrucaria at 2.3 A resolution using a twinned crystal | journal = Acta Crystallographica Section F | volume = 66 | issue = Pt 7 | pages = 765–70 | date = July 2010 | pmid = 20606269 | doi = 10.1107/S1744309110018828 | pmc = 2898457 }}
4. ^{{cite journal | vauthors = Cracknell JA, McNamara TP, Lowe ED, Blanford CF | title = Bilirubin oxidase from Myrothecium verrucaria: X-ray determination of the complete crystal structure and a rational surface modification for enhanced electrocatalytic O2 reduction | journal = Dalton Transactions | volume = 40 | issue = 25 | pages = 6668–75 | date = July 2011 | pmid = 21544308 | doi = 10.1039/c0dt01403f }}
{{CH-CH oxidoreductases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{1.3-enzyme-stub}}

2 : EC 1.3.3|Copper enzymes
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