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词条 Thymine dioxygenase
释义

  1. References

{{enzyme
| Name = thymine dioxygenase
| EC_number = 1.14.11.6
| CAS_number = 37256-67-0
| IUBMB_EC_number = 1/14/11/6
| GO_code = 0050341
| image =
| width =
| caption =
}}

In enzymology, a thymine dioxygenase ({{EC number|1.14.11.6}}) is an enzyme that catalyzes the chemical reaction

thymine + 2-oxoglutarate + O2 5-hydroxymethyluracil + succinate + CO2

The 3 substrates of this enzyme are thymine, 2-oxoglutarate, and O2, whereas its 3 products are 5-hydroxymethyluracil, succinate, and CO2.

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 thymine,2-oxoglutarate:oxygen oxidoreductase (7-hydroxylating). Other names in common use include thymine 7-hydroxylase, 5-hydroxy-methyluracil dioxygenase, and 5-hydroxymethyluracil oxygenase. It has 2 cofactors: iron, and Ascorbate.

References

  • {{cite journal | vauthors = Bankel L, Holme E, Lindstedt G, Lindstedt S | date = 1972 | title = Oxygenases involved in thymine and thymidine metabolism in Neurospora crassa | journal = FEBS Lett. | volume = 21 | pages = 135–138 | pmid = 11946494 | doi = 10.1016/0014-5793(72)80121-2 | issue = 2 }}
  • {{cite journal | vauthors = Liu CK, Hsu CA, Abbott MT | date = 1973 | title = Catalysis of three sequential dioxygenase reactions by thymine 7-hydroxylase | journal = Arch. Biochem. Biophys. | volume = 159 | pages = 180–7 | pmid = 4274083 | doi = 10.1016/0003-9861(73)90443-8 | issue = 1 }}
  • {{cite journal | vauthors = Warn-Cramer BJ, Macrander LA, Abbott MT | date = 1983 | title = Markedly different ascorbate dependencies of the sequential alpha-ketoglutarate dioxygenase reactions catalyzed by an essentially homogeneous thymine 7-hydroxylase from Rhodotorula glutinis | journal = J. Biol. Chem. | volume = 258 | pages = 10551–7 | pmid = 6684117 | issue = 17 }}
{{Dioxygenases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{1.14-enzyme-stub}}

4 : EC 1.14.11|Iron enzymes|Ascorbate enzymes|Enzymes of unknown structure

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