Taurine dioxygenase

In enzymology, a taurine dioxygenase (EC 1.14.11.17) is an enzyme that catalyzes the chemical reaction

taurine + 2-oxoglutarate + O2 sulfite + aminoacetaldehyde + succinate + CO2
taurine dioxygenase
Identifiers
EC number1.14.11.17
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

The 3 substrates of this enzyme are taurine, 2-oxoglutarate, and O2, whereas its 4 products are sulfite, aminoacetaldehyde, succinate, and CO2.[1]

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 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is taurine, 2-oxoglutarate:O2 oxidoreductase (sulfite-forming). Other names in common use include 2-aminoethanesulfonate dioxygenase, and alpha-ketoglutarate-dependent taurine dioxygenase. This enzyme participates in taurine and hypotaurine metabolism. It has 3 cofactors: iron, Ascorbate, and Fe2+.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1GQW, 1GY9, 1OS7, and 1OTJ.

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References
  1. Elkins, Jonathan M.; Ryle, Matthew J.; Clifton, Ian J.; Dunning Hotopp, Julie C.; Lloyd, John S.; Burzlaff, Nicolai I.; Baldwin, Jack E.; Hausinger, Robert P.; Roach, Peter L. (2002). "X-ray Crystal Structure of Escherichia coli Taurine/α-Ketoglutarate Dioxygenase Complexed to Ferrous Iron and Substrates†,‡". Biochemistry. 41 (16): 5185–5192. doi:10.1021/bi016014e. PMID 11955067.


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