thymine dioxygenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.11.6 | ||||||||
CAS no. | 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 | ||||||||
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In enzymology, a thymine dioxygenase (EC 1.14.11.6) is an enzyme that catalyzes the chemical reaction
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.
In enzymology, a 2'-deoxymugineic-acid 2'-dioxygenase (EC 1.14.11.24) is an enzyme that catalyzes the chemical reaction
In enzymology, a 6β-hydroxyhyoscyamine epoxidase (EC 1.14.11.14) is an enzyme that catalyzes the chemical reaction
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In enzymology, a gibberellin 2beta-dioxygenase (EC 1.14.11.13) is an enzyme that catalyzes the chemical reaction
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In enzymology, a gibberellin-44 dioxygenase (EC 1.14.11.12) is an enzyme that catalyzes the chemical reaction
In enzymology, a hyoscyamine (6S)-dioxygenase (EC 1.14.11.11) is an enzyme that catalyzes the chemical reaction
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Alpha-ketoglutarate-dependent hydroxylases are a major class of non-heme iron proteins that catalyse a wide range of reactions. These reactions include hydroxylation reactions, demethylations, ring expansions, ring closures, and desaturations. Functionally, the αKG-dependent hydroxylases are comparable to cytochrome P450 enzymes. Both use O2 and reducing equivalents as cosubstrates and both generate water.