Biphenyl-2,3-diol 1,2-dioxygenase

Biphenyl-2,3-diol 1,2-dioxygenase (EC 1.13.11.39) is an enzyme that catalyzes the chemical reaction

biphenyl-2,3-diol + O2 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
biphenyl-2,3-diol 1,2-dioxygenase
Crystallographic structure of the HsaC extradiol dioxygenase from M. tuberculosis (rainbow colored, N-terminus = blue, C-terminus = red) complexed with 3,4-DHSA (space-filling model (carbon = white, oxygen = red).[1]
Identifiers
EC number1.13.11.39
CAS number103679-58-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are biphenyl-2,3-diol and oxygen, whereas its two products are 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate and water.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The 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 structures have been solved for this class of enzymes, with PDB accession codes 1DHY, 1EIL, 1EIQ, 1EIR, 1HAN, 1KMY, 1KND, 1KNF, 1KW3, 1KW6, 1KW8, 1KW9, 1KWB, 1KWC, 1LGT, and 1LKD.

gollark: ... okay, yes.
gollark: Or have much/any data read out of them.
gollark: I was looking into doing something vaguely like this in userspace for broadly insane reasons, but coroutines can't be serialized apparently.
gollark: Oh neat, OCish persistence eventually™?
gollark: ↓ quite bland

References
  1. PDB: 2ZI8​; Yam KC, D'Angelo I, Kalscheuer R, Zhu H, Wang JX, Snieckus V, Ly LH, Converse PJ, Jacobs WR, Strynadka N, Eltis LD (March 2009). Ramakrishnan L (ed.). "Studies of a Ring-Cleaving Dioxygenase Illuminate the Role of Cholesterol Metabolism in the Pathogenesis of Mycobacterium tuberculosis". PLoS Pathog. 5 (3): e1000344. doi:10.1371/journal.ppat.1000344. PMC 2652662. PMID 19300498.
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