# Thymine dioxygenase

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thymine dioxygenase
Identifiers
EC number 1.14.11.6
CAS number 37256-67-0
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MetaCyc metabolic pathway
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Gene Ontology

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

The Enzyme Commission number is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. As a system of enzyme nomenclature, every EC number is associated with a recommended name for the respective enzyme.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which is not consumed in the catalyzed reaction and can continue to act repeatedly. Because of this, only very small amounts of catalyst are required to alter the reaction rate in principle.

A chemical reaction is a process that leads to the chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the positions of electrons in the forming and breaking of chemical bonds between atoms, with no change to the nuclei, and can often be described by a chemical equation. Nuclear chemistry is a sub-discipline of chemistry that involves the chemical reactions of unstable and radioactive elements where both electronic and nuclear changes can occur.

thymine + 2-oxoglutarate + O2${\displaystyle \rightleftharpoons }$ 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.

Thymine is one of the four nucleobases in the nucleic acid of DNA that are represented by the letters G–C–A–T. The others are adenine, guanine, and cytosine. Thymine is also known as 5-methyluracil, a pyrimidine nucleobase. In RNA, thymine is replaced by the nucleobase uracil. Thymine was first isolated in 1893 by Albrecht Kossel and Albert Neumann from calves' thymus glands, hence its name.

Oxygen is the chemical element with the symbol O and atomic number 8, meaning its nucleus has 8 protons. The number of neutrons varies according to the isotope: the stable isotopes have 8, 9, or 10 neutrons. Oxygen is a member of the chalcogen group on the periodic table, a highly reactive nonmetal, and an oxidizing agent that readily forms oxides with most elements as well as with other compounds. By mass, oxygen is the third-most abundant element in the universe, after hydrogen and helium. At standard temperature and pressure, two atoms of the element bind to form dioxygen, a colorless and odorless diatomic gas with the formula O
2
. Diatomic oxygen gas constitutes 20.8% of the Earth's atmosphere. As compounds including oxides, the element makes up almost half of the Earth's crust.

Products are the species formed from chemical reactions. During a chemical reaction reactants are transformed into products after passing through a high energy transition state. This process results in the consumption of the reactants. It can be a spontaneous reaction or mediated by catalysts which lower the energy of the transition state, and by solvents which provide the chemical environment necessary for the reaction to take place. When represented in chemical equations products are by convention drawn on the right-hand side, even in the case of reversible reactions. The properties of products such as their energies help determine several characteristics of a chemical reaction such as whether the reaction is exergonic or endergonic. Additionally the properties of a product can make it easier to extract and purify following a chemical reaction, especially if the product has a different state of matter than the reactants. Reactants are molecular materials used to create chemical reactions. The atoms aren't created or destroyed. The materials are reactive and reactants are rearranging during a chemical reaction. Here is an example of reactants: CH4 + O2. A non-example is CO2 + H2O or "energy".

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 biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP or NAD+ as cofactors. Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix.

A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's activity as a catalyst, a substance that increases the rate of a chemical reaction. Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized by in an area of study called enzyme kinetics.

Iron is a chemical element with symbol Fe and atomic number 26. It is a metal, that belongs to the first transition series and group 8 of the periodic table. It is by mass the most common element on Earth, forming much of Earth's outer and inner core. It is the fourth most common element in the Earth's crust.

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## References

• Bankel L, Holme E, Lindstedt G, Lindstedt S (1972). "Oxygenases involved in thymine and thymidine metabolism in Neurospora crassa". FEBS Lett. 21 (2): 135–138. doi:10.1016/0014-5793(72)80121-2. PMID   11946494.
• Liu CK, Hsu CA, Abbott MT (1973). "Catalysis of three sequential dioxygenase reactions by thymine 7-hydroxylase". Arch. Biochem. Biophys. 159 (1): 180–7. doi:10.1016/0003-9861(73)90443-8. PMID   4274083.
• Warn-Cramer BJ, Macrander LA, Abbott MT (1983). "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. PMID   6684117.

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