Taurine dioxygenase
| Taurine dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.11.17 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Taurine dioxygenase (EC 1.14.11.17) is an enzyme that catalyzes the chemical reaction.
It oxidises taurine using molecular oxygen, converting it to sulfite and aminoacetaldehyde.[1][2][3]
This enzyme is an alpha-ketoglutarate-dependent hydroxylase with systematic name taurine, 2-oxoglutarate:O2 oxidoreductase (sulfite-forming). Other names in common use include 2-aminoethanesulfonate dioxygenase, and alpha-ketoglutarate-dependent taurine dioxygenase. It participates in taurine and hypotaurine metabolism.[1]
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.
Mechanism
The enzyme is a non-heme iron protein with ferryl active site where Fe(IV)=O is the species that transfers its oxygen to the substrate.[4][5]
The mechanism requires 2-oxoglutaric acid to activate the iron oxygen complex, and this gives succinic acid and carbon dioxide when the second atom of the molecular oxygen is removed. Ascorbic acid is also required to increase the turnover number of the enzyme by reducing any iron converted to Fe(III) back to the required Fe(II).[6][7]
References
- ^ a b Enzyme 1.14.11.17 at KEGG Pathway Database.
- ^ Elkins JM, Ryle MJ, Clifton IJ, Dunning Hotopp JC, Lloyd JS, Burzlaff NI, et al. (April 2002). "X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates". Biochemistry. 41 (16): 5185–5192. doi:10.1021/bi016014e. PMID 11955067.
- ^ Eichhorn E, van der Ploeg JR, Kertesz MA, Leisinger T (September 1997). "Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli". The Journal of Biological Chemistry. 272 (37): 23031–23036. doi:10.1074/jbc.272.37.23031. PMID 9287300.
- ^ Ryle MJ, Koehntop KD, Liu A, Que L, Hausinger RP (April 2003). "Interconversion of two oxidized forms of taurine/α-ketoglutarate dioxygenase, a non-heme iron hydroxylase: Evidence for bicarbonate binding". Proceedings of the National Academy of Sciences of the United States of America. 100 (7): 3790–3795. doi:10.1073/pnas.0636740100. PMC 153000. PMID 12642663.
- ^ Mbenza NM, Vadakkedath PG, McGillivray DJ, Leung IK (December 2017). "NMR studies of the non-haem Fe(II) and 2-oxoglutarate-dependent oxygenases". J. Inorg. Biochem. 177: 384–394. doi:10.1016/j.jinorgbio.2017.08.032. PMID 28893416.
- ^ Hibi M, Ogawa J (May 2014). "Characteristics and biotechnology applications of aliphatic amino acid hydroxylases belonging to the Fe(II)/α-ketoglutarate-dependent dioxygenase superfamily". Applied Microbiology and Biotechnology. 98 (9): 3869–3876. doi:10.1007/s00253-014-5620-z. PMID 24682483.
- ^ Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ (2001). "Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases". Eur. J. Biochem. 268 (24): 6625–36. doi:10.1046/j.0014-2956.2001.02617.x. PMID 11737217.