Biphenyl 2,3-dioxygenase

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biphenyl 2,3-dioxygenase
Identifiers
EC no.1.14.12.18
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a biphenyl 2,3-dioxygenase (EC 1.14.12.18) is an enzyme that catalyzes the chemical reaction

biphenyl + NADH + H+ + O2 (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+

The 4 substrates of this enzyme are biphenyl, NADH, H+, and O2, whereas its two products are (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol and NAD+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of two atoms o oxygen into the other donor. The systematic name of this enzyme class is biphenyl,NADH:oxygen oxidoreductase (2,3-hydroxylating). This enzyme is also called biphenyl dioxygenase. This enzyme participates in biphenyl degradation.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1ULI and 1ULJ.

References

  • Haddock JD, Gibson DT (1995). "Purification and characterization of the oxygenase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400". J. Bacteriol. 177 (20): 5834–9. doi:10.1128/jb.177.20.5834-5839.1995. PMC 177406. PMID 7592331.
  • Haddock JD, Pelletier DA, Gibson DT (1997). "Purification and properties of ferredoxinBPH, a component of biphenyl 2,3-dioxygenase of Pseudomonas sp strain LB400". J. Ind. Microbiol. Biotechnol. 19 (5–6): 355–9. doi:10.1038/sj.jim.2900429. PMID 9451832. S2CID 2654044.
  • Broadus RM, Haddock JD (1998). "Purification and characterization of the NADH:ferredoxinBPH oxidoreductase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400". Arch. Microbiol. 170 (2): 106–12. doi:10.1007/s002030050621. PMID 9683647. S2CID 11693349.