View source for Biphenyl-2,3-diol 1,2-dioxygenase

{{infobox enzyme
| Name       = biphenyl-2,3-diol 1,2-dioxygenase
| EC_number  = 1.13.11.39
| CAS_number = 103679-58-9
| GO_code    = 0018583
| image      = 2ZI8.png
| width      =
| caption    = [[X-ray crystallography#Biological macromolecular crystallography|Crystallographic structure]] of the  HsaC extradiol dioxygenase from ''[[Mycobacterium tuberculosis|M. tuberculosis]]''  (rainbow colored, [[N-terminus]] = blue, [[C-terminus]] = red) complexed with 3,4-[[DHSA]] ([[space-filling model]] (carbon = white, oxygen = red).<ref name="pmid19300498">{{PDB|2ZI8}}; {{cite journal | vauthors = Yam KC, D'Angelo I, Kalscheuer R, Zhu H, Wang JX, Snieckus V, Ly LH, Converse PJ, Jacobs WR, Strynadka N, Eltis LD | title = Studies of a Ring-Cleaving Dioxygenase Illuminate the Role of Cholesterol Metabolism in the Pathogenesis of Mycobacterium tuberculosis | journal = PLOS Pathog. | volume = 5 | issue = 3 | pages = e1000344 |date=March 2009 | pmid = 19300498 | pmc = 2652662 | doi = 10.1371/journal.ppat.1000344 | editor1-last = Ramakrishnan | editor1-first = Lalita | doi-access = free }}</ref>
}}
'''Biphenyl-2,3-diol 1,2-dioxygenase''' ({{EC number|1.13.11.39}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
:biphenyl-2,3-diol + O<sub>2</sub> <math>\rightleftharpoons</math> 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H<sub>2</sub>O
Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[biphenyl-2,3-diol]] and [[oxygen]], whereas its two [[product (chemistry)|products]] are [[2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate]] and [[water]].
This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on single donors with O<sub>2</sub> as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O<sub>2</sub>.  The [[List of enzymes|systematic name]] of this enzyme class is '''biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (decyclizing)'''. Other names in common use include '''2,3-dihydroxybiphenyl dioxygenase''', and '''biphenyl-2,3-diol dioxygenase'''.  This enzyme participates in [[gamma-hexachlorocyclohexane degradation]] and [[biphenyl degradation]].
==Structural studies==
As of late 2007, 16 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1DHY}}, {{PDB link|1EIL}}, {{PDB link|1EIQ}}, {{PDB link|1EIR}}, {{PDB link|1HAN}}, {{PDB link|1KMY}}, {{PDB link|1KND}}, {{PDB link|1KNF}}, {{PDB link|1KW3}}, {{PDB link|1KW6}}, {{PDB link|1KW8}}, {{PDB link|1KW9}}, {{PDB link|1KWB}}, {{PDB link|1KWC}}, {{PDB link|1LGT}}, and {{PDB link|1LKD}}.
==References==
{{reflist|1}}
* {{cite journal |author1 = Utsumi T |author2 =Funatsu G | date = 1986 | title = Induction of superoxide production in polymorphonuclear leukocytes by ricinus lectins and its dependency on lectin valency | journal = Agric. Biol. Chem.  | volume = 50 | pages = 1047&ndash;1049 | doi = 10.1271/bbb1961.50.1047 | issue = 4 | doi-access = free }}
{{Monooxygenases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}
[[Category:EC 1.13.11]]
[[Category:Enzymes of known structure]]