Biphenyl 2,3-dioxygenase

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
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PMCarticles
PubMedarticles
NCBIproteins

Biphenyl 2,3-dioxygenase (EC 1.14.12.18) is an enzyme that catalyzes the chemical reaction

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

The four substrates of this enzyme are biphenyl, reduced nicotinamide adenine dinucleotide (NADH), oxygen, and a proton. Its products are (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol and oxidised NAD+.[1][2][3][4]

This enzyme is an oxidoreductase that uses molecular oxygen as oxidant and incorporates both its atoms into the starting material. The systematic name of this enzyme class is biphenyl,NADH:oxygen oxidoreductase (2,3-hydroxylating). It is also called biphenyl dioxygenase. It is a Rieske protein containing an iron–sulfur cluster and participates in biphenyl degradation.[1]

Structural studies

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

References

  1. ^ a b Enzyme 1.14.12.18 at KEGG Pathway Database.
  2. ^ 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.
  3. ^ 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.
  4. ^ 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. Bibcode:1998ArMic.170..106B. doi:10.1007/s002030050621. PMID 9683647. S2CID 11693349.