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Thymine (/ ˈ θ aɪ m ɪ n /) (symbol T or Thy) is one of the four nucleotide bases 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.
It has an S-shape with a length of 110 Å and a width of 60 Å. Each monomer is composed of 440 amino acids and is composed of a small α-helical domain and a large α/β domain. The surface of the enzyme is smooth except for a 10 Å deep and 8 Å wide cavity between the two domains that contains the thymine, thymidine, and phosphate binding ...
Thymine and uracil are distinguished by merely the presence or absence of a methyl group on the fifth carbon (C5) of these heterocyclic six-membered rings. [2] [page needed] In addition, some viruses have aminoadenine (Z) instead of adenine. It differs in having an extra amine group, creating a more stable bond to thymine. [3]
In its composition, deoxythymidine is a nucleoside composed of deoxyribose (a pentose sugar) joined to the pyrimidine base thymine. Deoxythymidine can be phosphorylated with one, two or three phosphoric acid groups, creating dTMP ( d eoxy t hymidine m ono p hosphate), dTDP , or dTTP (for the d i- and t ri- phosphates, respectively).
Two different classes of thymidine kinases have been identified [8] [9] and are included in this super family: one family groups together thymidine kinase from herpesvirus as well as cellular thymidylate kinases, the second family groups TK from various sources that include, vertebrates, bacteria, the bacteriophage T4, poxviruses, African swine fever virus (ASFV) and Fish lymphocystis disease ...
Deamination is the removal of an amino group from a molecule. [1] Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy.
The protein encoded by this gene belongs to the TDG/mug DNA glycosylase family. Thymine-DNA glycosylase (TDG) removes thymine moieties from G/T mismatches by hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of DNA and the mispaired thymine. With lower activity, this enzyme also removes thymine from C/T and T/T mispairings.
Thymidylate synthase is an enzyme of about 30 to 35 kDa in most species except in protozoan and plants where it exists as a bifunctional enzyme that includes a dihydrofolate reductase domain. [8] A cysteine residue is involved in the catalytic mechanism (it covalently binds the 5,6-dihydro-dUMP intermediate).