|Related Categories||Cell Biology, Metabolic Pathways, Metabolites and Cofactors on the Metabolic Pathways Chart, Metabolomics, Nucleotide More...|
2′-Deoxyuridine 5′-monophosphate (dUMP) is used by the enzyme thymidylate synthetase (TS) (EC 188.8.131.52) for the de novo production of dTMP. dUMP is used as the reference substrate in studies of dUMP analogues in potential chemotherapy applications.
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The role of protein dynamics in thymidylate synthase catalysis: variants of conserved 2′-deoxyuridine 5′-monophosphate (dUMP)-binding Tyr-261. Newby Z, Lee TT, Morse RJ, et al. Biochemistry 45, 7415-7428, (2006)
The crystal structure of the Leishmania major deoxyuridine triphosphate nucleotidohydrolase in complex with nucleotide analogues, dUMP, and deoxyuridine. Hemsworth GR, Moroz OV, Fogg MJ, et al. J. Biol. Chem. 286, 16470-16481, (2011)
Interaction of nucleotide excision repair proteins with DNA containing bulky lesion and apurinic/apyrimidinic site. Skosareva LV, Lebedeva NA, Rechkunova NI, et al. Biochemistry. (Mosc.) 77(5), 524-31, (2012)
Human thymidylate synthase with loop 181-197 stabilized in an inactive conformation: ligand interactions, phosphorylation, and inhibition profiles. Luo B, Repalli J, Yousef AM, et al. Protein Sci. 20(1), 87-94, (2011)
Simultaneous quantification of 5-FU, 5-FUrd, 5-FdUrd, 5-FdUMP, dUMP and TMP in cultured cell models by LC-MS/MS. Carli D, Honorat M, Cohen S, et al. J. Chromatogr. B. Analyt. Technol. Biomed. Life Sci. 877, 2937-2944, (2009)
Functional identity of the active sites of crustacean and viral thymidylate synthases. Arvizu-Flores AA, Aispuro-Hernandez E, Garcia-Orozco KD, et al. Comp. Biochem. Physiol. C. Toxicol. Pharmacol. 150(3), 406-13, (2009)
The effect of 5-substitution in the pyrimidine ring of dUMP on the interaction with thymidylate synthase: molecular modeling and QSAR. Jarmuła A, Cieplak P, Krygowski TM, et al. Bioorg. Med. Chem. 15(6), 2346-58, (2007)
Crystal structures of thymidylate synthase mutant R166Q: structural basis for the nearly complete loss of catalytic activity. Sotelo-Mundo RR, Changchien L, Maley F, et al. J. Biochem. Mol. Toxicol. 20(2), 88-92, (2006)
Ultrafast real-time visualization of active site flexibility of flavoenzyme thymidylate synthase ThyX. Laptenok SP, Bouzhir-Sima L, Lambry JC, et al. Proc. Natl. Acad. Sci. U. S. A. 110(22), 8924-9, (2013)
Functional analysis of the Mycobacterium tuberculosis FAD-dependent thymidylate synthase, ThyX, reveals new amino acid residues contributing to an extended ThyX motif. Ulmer JE, Boum Y, Thouvenel CD, et al. J. Bacteriol. 190(6), 2056-64, (2008)
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