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- W1451796677 abstract "Publisher Summary This chapter discusses the assay of thymidylate synthetase activity. During the conversion of deoxyuridylate to thymidylate, a new carbon-to-carbon bond is formed, a one-carbon unit is reduced to a methyl group, and a hydrogenated form of folic acid is oxidized. Various assays for thymidylate synthetase activity are based on these chemical events. The one-carbon unit can be supplied in the form of formaldehyde which reacts nonenzymatically with tetrahydrofolate to yield 5,10-ethylenetetrahydrofolate. Thymidylate synthetase catalyzes the transfer of the one-carbon moiety to the 5-position of deoxyuridylate and its reduction to a methyl group. Thymidylate kinase of E. coli catalyzes the phosphorylation of thymidylate by ATP but not of deoxyuridylate. The nuceloside monophosphates are susceptible to dephosphorylation by phosphomonoesterase and the nucleoside triphosphates are not. Thymidine triphosphate is adsorbed by charcoal, whereas inorganic orthophosphate is not. A direct method has been devised for the assay of thymidylate synthetase that depends on spectral changes associated with the oxidation of tetrahydrofolate to dihydrofolate." @default.
- W1451796677 created "2016-06-24" @default.
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- W1451796677 date "1963-01-01" @default.
- W1451796677 modified "2023-09-27" @default.
- W1451796677 title "[15] Assay of thymidylate synthetase activity" @default.
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- W1451796677 doi "https://doi.org/10.1016/0076-6879(63)06155-3" @default.
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