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{{STRUCTURE_1hvy|PDB=1hvy|SCENE=}} | {{STRUCTURE_1hvy|PDB=1hvy|SCENE=}} | ||
=Thymidylate Synthase= | =Thymidylate Synthase= | ||
Thymidylate Synthase is a protein found in all organisms that make DNA. Thymidylate Synthase (TS) is the essential enzyme that catalyzes the formation of dTMP from dUMP, using 5,10-methylenetetrahydrofolate (mTHF) as a cosubstrate <ref name="paper1"> Huang, X., Gibson, L. M., Bell, B. J., Lovelace, L. L., Marjorette, M., Peña, O., et al. (2011). Replacement of Val3 in Human Thymidylate Synthase Affects its Kinetic Properties and Intracellular Stability. NIH Public Access, 49(11), 2475-2482. doi: 10.1021/bi901457e.Replacement.</ref>. | Thymidylate Synthase is a protein found in all organisms that make DNA <ref name="paper1"> Huang, X., Gibson, L. M., Bell, B. J., Lovelace, L. L., Marjorette, M., Peña, O., et al. (2011). Replacement of Val3 in Human Thymidylate Synthase Affects its Kinetic Properties and Intracellular Stability. NIH Public Access, 49(11), 2475-2482. doi: 10.1021/bi901457e.Replacement.</ref>. Thymidylate Synthase (TS) is the essential enzyme that catalyzes the formation of dTMP from dUMP, using 5,10-methylenetetrahydrofolate (mTHF) as a cosubstrate <ref name="paper1"> Huang, X., Gibson, L. M., Bell, B. J., Lovelace, L. L., Marjorette, M., Peña, O., et al. (2011). Replacement of Val3 in Human Thymidylate Synthase Affects its Kinetic Properties and Intracellular Stability. NIH Public Access, 49(11), 2475-2482. doi: 10.1021/bi901457e.Replacement.</ref>. | ||
==Overview== | ==Overview== | ||
Thymidylate Synthase catalyzes the reductive methylation of deoxyuridylic acid during the de novo synthesis of thymidylic acid <ref name="paper2"> Jenh, C. H., Rao, L. G., & Johnson, L. F. (1985). Regulation of thymidylate synthase enzyme synthesis in 5-fluorodeoxyuridine-resistant mouse fibroblasts during the transition from the resting to growing state. Journal of cellular physiology, 122(1), 149-54. doi: 10.1002/jcp.1041220122.</ref>. This reaction occurs primarily during the S phase of the cell cycle. Thymidylate synthase is an essential enzyme in proliferating cells that are not supplied with an alternate source of thymidine nucleotides <ref name="paper2"> Jenh, C. H., Rao, L. G., & Johnson, L. F. (1985). Regulation of thymidylate synthase enzyme synthesis in 5-fluorodeoxyuridine-resistant mouse fibroblasts during the transition from the resting to growing state. Journal of cellular physiology, 122(1), 149-54. doi: 10.1002/jcp.1041220122.</ref>. Research has shown that thymidylate synthase enzyme levels are much higher in rapidly proliferating cells than in non dividing cells <ref name="paper2"> Jenh, C. H., Rao, L. G., & Johnson, L. F. (1985). Regulation of thymidylate synthase enzyme synthesis in 5-fluorodeoxyuridine-resistant mouse fibroblasts during the transition from the resting to growing state. Journal of cellular physiology, 122(1), 149-54. doi: 10.1002/jcp.1041220122.</ref>. | Thymidylate Synthase catalyzes the reductive methylation of deoxyuridylic acid during the de novo synthesis of thymidylic acid <ref name="paper2"> Jenh, C. H., Rao, L. G., & Johnson, L. F. (1985). Regulation of thymidylate synthase enzyme synthesis in 5-fluorodeoxyuridine-resistant mouse fibroblasts during the transition from the resting to growing state. Journal of cellular physiology, 122(1), 149-54. doi: 10.1002/jcp.1041220122.</ref>. This reaction occurs primarily during the S phase of the cell cycle. Thymidylate synthase is an essential enzyme in proliferating cells that are not supplied with an alternate source of thymidine nucleotides <ref name="paper2"> Jenh, C. H., Rao, L. G., & Johnson, L. F. (1985). Regulation of thymidylate synthase enzyme synthesis in 5-fluorodeoxyuridine-resistant mouse fibroblasts during the transition from the resting to growing state. Journal of cellular physiology, 122(1), 149-54. doi: 10.1002/jcp.1041220122.</ref>. Research has shown that thymidylate synthase enzyme levels are much higher in rapidly proliferating cells than in non dividing cells <ref name="paper2"> Jenh, C. H., Rao, L. G., & Johnson, L. F. (1985). Regulation of thymidylate synthase enzyme synthesis in 5-fluorodeoxyuridine-resistant mouse fibroblasts during the transition from the resting to growing state. Journal of cellular physiology, 122(1), 149-54. doi: 10.1002/jcp.1041220122.</ref>. | ||