Toluene dioxygenase

toluene dioxygenase
Identifiers
EC no.1.14.12.11
CAS no.120038-36-0
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, toluene dioxygenase (EC 1.14.12.11) is an enzyme that catalyzes the chemical reaction

 
 
O2 + H+
 
Reversible left-right reaction arrow with minor forward substrate(s) from top left and minor reverse product(s) to bottom left
O2 + H+
 
 
2D representation of the chemical structure of Q27098106.
(1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol
+ NAD+
 

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

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 toluene,NADH:oxygen oxidoreductase (1,2-hydroxylating). This enzyme is also called toluene 2,3-dioxygenase. It participates in toluene and xylene degradation.[1]

References

  1. ^ a b Enzyme 1.14.12.11 at KEGG Pathway Database.
  2. ^ Renganathan V (1989). "Possible involvement of toluene-2,3-dioxygenase in defluorination of 3-fluoro-substituted benzenes by toluene-degrading Pseudomonas sp strain T-12". Applied and Environmental Microbiology. 55 (2): 330–334. Bibcode:1989ApEnM..55..330R. doi:10.1128/aem.55.2.330-334.1989. PMC 184110. PMID 16347845.
  3. ^ Subramanian V, Liu TN, Yeh WK, Gibson DT (1979). "Toluene dioxygenase: purification of an iron-sulfur protein by affinity chromatography". Biochemical and Biophysical Research Communications. 91 (3): 1131–9. Bibcode:1979BBRC...91.1131S. doi:10.1016/0006-291X(79)91998-3. PMID 526270.