thymidylate 5'-phosphatase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: thymidylate + H2O = thymidine + phosphate. [EC:3.1.3.35, MetaCyc:THYMIDYLATE-5-PHOSPHATASE-RXN]

Thymidylate 5'-phosphatase activity refers to the enzymatic hydrolysis of the phosphate group from the 5'-position of thymidylate, also known as deoxythymidine monophosphate (dTMP). This reaction is essential for the salvage pathway of nucleotide metabolism, specifically for the recycling of thymine.

The enzyme responsible for this activity, thymidylate 5'-phosphatase, plays a crucial role in maintaining a balanced pool of deoxyribonucleotides, which are the building blocks of DNA. By removing the phosphate group from dTMP, the enzyme converts it into deoxythymidine (dThd). This deoxynucleoside can then be phosphorylated by deoxythymidine kinase to form dTMP again, completing the salvage cycle.

The activity of thymidylate 5'-phosphatase is particularly important for cells that are actively dividing, as they have a high demand for dTMP for DNA synthesis. Defects in this enzyme can lead to impaired DNA replication and cell growth.

The molecular mechanism involves the enzyme binding to dTMP and catalyzing the hydrolysis of the phosphate ester bond using a water molecule. The process releases inorganic phosphate and dThd, which is then available for further processing. The precise catalytic mechanism may vary depending on the specific enzyme, but the overall function remains the same: the removal of the phosphate group from the 5'-position of dTMP.'
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Proteins (1)

Compounds (16)