Thymidylate synthase
From Proteopedia
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| - | <StructureSection load='1tsv' size='450' side='right' caption='Thymidylate synthase complex with dUMP | + | <StructureSection load='1tsv' size='450' side='right' caption='Thymidylate synthase complex with dUMP (PDB entry [[1tsv]])' scene='49/493689/Cv/1'> |
== Function == | == Function == | ||
'''Thymidylate synthase''' (TS) catalyzes the methylation of dUMP to dTMP using 5,10-methylenetetrahydrofolate as a cofactor. TS is essential for DNA replication and repair<ref>PMID:2243092</ref>. In protozoa, dihydrofolate reductase (DHFR) and TS are expressed as a bifunctional monomeric enzyme ('''DHFR-TS)''' with the DHFR entity at the N terminal. DHFR and TS catalyze consecutive reactions in the dTMP biosynthesis. There are two different types of TS – '''ThyA''' and '''ThyX'''. The types differ in their activity and structure. The TS ThyX are flavin-dependent enzymes. | '''Thymidylate synthase''' (TS) catalyzes the methylation of dUMP to dTMP using 5,10-methylenetetrahydrofolate as a cofactor. TS is essential for DNA replication and repair<ref>PMID:2243092</ref>. In protozoa, dihydrofolate reductase (DHFR) and TS are expressed as a bifunctional monomeric enzyme ('''DHFR-TS)''' with the DHFR entity at the N terminal. DHFR and TS catalyze consecutive reactions in the dTMP biosynthesis. There are two different types of TS – '''ThyA''' and '''ThyX'''. The types differ in their activity and structure. The TS ThyX are flavin-dependent enzymes. | ||
Revision as of 13:01, 14 September 2016
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3D structures of thymidylate synthase
Updated on 14-September-2016
References
- ↑ Kaneda S, Nalbantoglu J, Takeishi K, Shimizu K, Gotoh O, Seno T, Ayusawa D. Structural and functional analysis of the human thymidylate synthase gene. J Biol Chem. 1990 Nov 25;265(33):20277-84. PMID:2243092
- ↑ Rahman L, Voeller D, Rahman M, Lipkowitz S, Allegra C, Barrett JC, Kaye FJ, Zajac-Kaye M. Thymidylate synthase as an oncogene: a novel role for an essential DNA synthesis enzyme. Cancer Cell. 2004 Apr;5(4):341-51. PMID:15093541
- ↑ Finer-Moore JS, Fauman EB, Morse RJ, Santi DV, Stroud RM. Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase. Protein Eng. 1996 Jan;9(1):69-75. PMID:9053905
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