Biology:Thymine dioxygenase
| Thymine dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.14.11.6 | ||||||||
| CAS number | 37256-67-0 | ||||||||
| 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 | ||||||||
| |||||||||
Thymine dioxygenase (EC 1.14.11.6) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The enzyme oxidises thymine to give 5-hydroxymethyluracil.[1][2]
The enzyme is an alpha-ketoglutarate-dependent hydroxylase with systematic name thymine,2-oxoglutarate:oxygen oxidoreductase (7-hydroxylating). Other names in common use include thymine 7-hydroxylase, 5-hydroxy-methyluracil dioxygenase, and 5-hydroxymethyluracil oxygenase.[3]
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]
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).[5][6][7]
- REDIRECT Template:Chemical reaction
References
- ↑ "Oxygenases involved in thymine and thymidine metabolism in Neurospora crassa". FEBS Lett. 21 (2): 135–138. 1972. doi:10.1016/0014-5793(72)80121-2. PMID 11946494. Bibcode: 1972FEBSL..21..135B.
- ↑ "Catalysis of three sequential dioxygenase reactions by thymine 7-hydroxylase". Arch. Biochem. Biophys. 159 (1): 180–7. 1973. doi:10.1016/0003-9861(73)90443-8. PMID 4274083.
- ↑ Enzyme 1.14.11.6 at KEGG Pathway Database.
- ↑ "NMR studies of the non-haem Fe(II) and 2-oxoglutarate-dependent oxygenases". J. Inorg. Biochem. 177: 384–394. December 2017. doi:10.1016/j.jinorgbio.2017.08.032. PMID 28893416.
- ↑ "Markedly different ascorbate dependencies of the sequential alpha-ketoglutarate dioxygenase reactions catalyzed by an essentially homogeneous thymine 7-hydroxylase from Rhodotorula glutinis". J. Biol. Chem. 258 (17): 10551–7. 1983. doi:10.1016/S0021-9258(17)44491-7. PMID 6684117.
- ↑ "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. May 2014. doi:10.1007/s00253-014-5620-z. PMID 24682483.
- ↑ "Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases". Eur. J. Biochem. 268 (24): 6625–36. 2001. doi:10.1046/j.0014-2956.2001.02617.x. PMID 11737217.
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