Uracil/thymine dehydrogenase

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Uracil/thymine dehydrogenase
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EC no. 1.17.99.4
CAS no. 9029-00-9
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Uracil/thymine dehydrogenase (EC 1.17.99.4, uracil oxidase, uracil-thymine oxidase, uracil dehydrogenase ) is an enzyme with systematic name uracil:acceptor oxidoreductase. [1] [2] [3] [4] [5] This enzyme catalyses the following chemical reaction

(1) uracil + H2O + acceptor barbiturate + reduced acceptor
(2) thymine + H2O + acceptor 5-methylbarbiturate + reduced acceptor

Uracil/thymine dehydrogenase forms part of the oxidative pyrimidine-degrading pathway in some microorganisms.

Related Research Articles

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<span class="mw-page-title-main">Nucleotide</span> Biological molecules that form the building blocks of nucleic acids

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<span class="mw-page-title-main">Uracil</span> Chemical compound of RNA

Uracil is one of the four nucleobases in the nucleic acid RNA. The others are adenine (A), cytosine (C), and guanine (G). In RNA, uracil binds to adenine via two hydrogen bonds. In DNA, the uracil nucleobase is replaced by thymine (T). Uracil is a demethylated form of thymine.

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Nucleic acid metabolism is a collective term that refers to the variety of chemical reactions by which nucleic acids are either synthesized or degraded. Nucleic acids are polymers made up of a variety of monomers called nucleotides. Nucleotide synthesis is an anabolic mechanism generally involving the chemical reaction of phosphate, pentose sugar, and a nitrogenous base. Degradation of nucleic acids is a catabolic reaction and the resulting parts of the nucleotides or nucleobases can be salvaged to recreate new nucleotides. Both synthesis and degradation reactions require multiple enzymes to facilitate the event. Defects or deficiencies in these enzymes can lead to a variety of diseases.

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<span class="mw-page-title-main">Caffeine dehydrogenase</span> Enzyme

Caffeine dehydrogenase, commonly referred to in scientific literature as caffeine oxidase, is an enzyme with the systematic name caffeine:ubiquinone oxidoreductase. The enzyme is most well known for its ability to directly oxidize caffeine, a type of methylxanthine, to trimethyluric acid. Caffeine dehydrogenase can be found in bacterium Pseudomonas sp. CBB1 and in several species within the genera Alcaligenes, Rhodococcus, and Klebsiella.

References

  1. Hayaishi O, Kornberg A (May 1952). "Metabolism of cytosine, thymine, uracil, and barbituric acid by bacterial enzymes". The Journal of Biological Chemistry. 197 (2): 717–32. PMID   12981104.
  2. Wang TP, Lampen JO (February 1952). "Metabolism of pyrimidines by a soil bacterium". The Journal of Biological Chemistry. 194 (2): 775–83. PMID   14927671.
  3. Wang TP, Lampen JO (February 1952). "Uracil oxidase and the isolation of barbituric acid from uracil oxidation". The Journal of Biological Chemistry. 194 (2): 785–91. PMID   14927672.
  4. Lara FJ (August 1952). "On the decomposition of pyrimidines by bacteria. II. Studies with cell-free enzyme preparations". Journal of Bacteriology. 64 (2): 279–85. PMC   169350 . PMID   14955523.
  5. Soong CL, Ogawa J, Shimizu S (August 2001). "Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase". Biochemical and Biophysical Research Communications. 286 (1): 222–6. doi:10.1006/bbrc.2001.5356. PMID   11485332.