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Enzyme Nomenclature
Information on EC 2.1.1.45 - thymidylate synthase
for references in articles please use BRENDA:EC2.1.1.45
Word Map on EC 2.1.1.45
- 2.1.1.45
- 5-fluorouracil
- thymidine
- colorectal
- carcinoma
- dihydrofolate
- antifolate
-
dihydropyrimidine
- methotrexate
- pyrimidine
-
regimen
-
chemotherapeutic
-
phosphorylase
-
fluoropyrimidine
-
fdump
- pemetrexed
- leucovorin
-
ribonucleotide
-
resect
- polyglutamates
-
non-small
-
5-fu-based
- uracil
- cisplatin
-
casey
- mthfr
- deoxyuridine
- oxaliplatin
-
antimetabolite
- capecitabine
-
folylpolyglutamate
- irinotecan
- orotate
- 5-fluoro-2'-deoxyuridine
- glycinamide
-
polyglutamylation
-
formyltransferase
- trimetrexate
- gemcitabine
-
tegafur
-
folinic
- quinazoline
- medicine
- dttp
- 2'-deoxyuridine
-
folate-dependent
- deoxycytidylate
- deoxythymidine
- aminopterin
- drug development
-
methotrexate-resistant
-
transformylase
-
cross-complementing
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.1.1.45
-
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RECOMMENDED NAME
GeneOntology No.
thymidylate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
-
-
-
-
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
O2 and methylenetetrahydrofolate compete for the reduced enzyme after dUMP binding. dUMP enhances the rate of the oxidative half reaction and while the oxidase reaction is faster than the reaction with methylenetetrahydrofolate, this cofactor slows down the consumption of NADPH in the presence of O2 in accordance with substrate competition. dUMP, the substrate of the oxidative half reaction does not affect the reductive half reaction. In the absence of the second substrate methylenetetrahydrofolate, dUMP enhances the reaction of molecular oxygen with the reduced enzyme
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehalogenation
-
-
-
-
methylene group transfer
-
-
-
-
reductive methylation
reductive methylation
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:dUMP C-methyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9031-61-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
encapsulated yeast-like fungus, GenBank accession No.
SwissProt
encapsulated yeast-like fungus, GenBank accession No.
SwissProt
-
485357, 485358, 485359, 485363, 485365, 485369, 485371, 485372, 485373, 485374, 485375, 485376, 485380, 485381, 485382, 485383, 485388, 485389, 485397, 485402, 485405, 485406, 485408, 485409, 485413, 485415, 485416, 485417, 485419, 485421, 485422, 485423, 485425, 485430, 485431, 688294, 693567, 705044, 705333, 706772, 711474
-
-
-
485359, 485364, 485384, 485387, 485407, 485413, 485415, 485428, 688294, 690892, 691522, 691614, 692015, 692016, 692158, 692480, 692655, 694481, 694482, 695129, 695194, 702155, 702996, 703257, 703391, 703950, 705044, 705451, 711474, 718866, 719078, 719649, 720965, 720995, 734453
-
-
human
-
-
-
485359, 485360, 485361, 485363, 485364, 485365, 485366, 485368, 485369, 485370, 485372, 485375, 485376, 485378, 485379, 485380, 485381, 485382, 485383, 485384, 485385, 485387, 485388, 485389, 485393, 485396, 485397, 485399, 485400, 485401, 485403, 485405, 485406, 485411, 485415, 485416, 485418, 485419, 485423, 485427, 485429, 485430, 485431
-
-
thymidylate synthase chemically synthesized based on the amino acid sequence of TS from Lactobacillus casei
-
-
bifunctional dihydrofolate reductase-thymidylate synthase
UniProt
Ehrlich ascites carcinoma cells
485360, 485361, 485363, 485365, 485368, 485369, 485375, 485384, 485390, 485393, 485398, 485402, 485404
-
-
wild type strain 8325-4 and trimethoprim-sulfamethoxazole-resistant thymidine-dependent small-colony variants 1-8
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
growth of single-knockout lines of dihydrofolate reductase-thymidylate synthase in vitro are identical to wild type cells, whereas double-knockout lines of dihydrofolate reductase-thymidylate synthase have an absolute requirement for thymidine
metabolism
physiological function
additional information
evolution
Leishmania braziliensis subsp. viannia
dihydrofolate reductase (DHFR) and thymidylate synthase (TS) have undergone a fusion event generating a single polypeptide but conserving the two functions in trypanosomatids
evolution
dihydrofolate reductase (DHFR) and thymidylate synthase (TS) have undergone a fusion event generating a single polypeptide but conserving the two functions in trypanosomatids
evolution
-
dihydrofolate reductase (DHFR) and thymidylate synthase (TS) have undergone a fusion event generating a single polypeptide but conserving the two functions in trypanosomatids
metabolism
-
ThyA is the sole catalyst for thymidylate biosynthesis in Corynebacterium glutamicum
metabolism
-
ThyA is the sole catalyst for thymidylate biosynthesis in Corynebacterium glutamicum
-
physiological function
-
thymidylate synthase plays an essential role in embryogenesis, embryos with their thymidylate synthase function inhibited show a retarded embryo development and irregular cell sizes
physiological function
thymidylate synthase is the only de novo source of dTMP and is essential for DNA replication
physiological function
thymidylate synthase is the only de novo source of dTMP and is essential for DNA replication
physiological function
-
the enzyme is essential for the de novo synthesis of DNA
physiological function
-
the enzyme is indispensable for DNA replication in actively dividing cells
physiological function
several parasitic protozoa, including Toxoplasma gondii, contain a unique bifunctional thymidylate synthase-dihydrofolate reductase (TS-DHFR) having the catalytic activities contained on a single polypeptide chain in contrast to the human enzyme. Three-dimensional structures of Toxoplasma gondii enzyme TS-DHFR and of a loop truncated TS-DHFR enzyme, removing several flexible surface loops in the DHFR domain, shows that the TS-DHFR homodimer includes a junctional region containing a linked crossover helix between the DHFR domains of the two adjacent monomers, a long linker connecting the TS and DHFR domains, and a DHFR domain that is positively charged. The crystal structure suggests that the positively charged DHFR domain governs this electrostatically mediated movement of dihydrofolate, preventing release from the enzyme. Importance of this region not only in DHFR catalysis but also in modulating the distal TS activity suggests a role for TS-DHFR interdomain interactions
physiological function
Leishmania braziliensis subsp. viannia
dihydrofolate reductase is an essential enzyme in the tetrahydrofolate pathway which catalyzes the NADPH-dependent reduction of 7,8-dihydrofolate (H2F) to the 5,6,7,8-tetrahydrofolate needed to maintain intracellular pools of tetrahydrofolate and its derivatives. These are essential cofactors in the biosynthesis of purines, pyrimidines and several amino acids
physiological function
dihydrofolate reductase is an essential enzyme in the tetrahydrofolate pathway which catalyzes the NADPH-dependent reduction of 7,8-dihydrofolate (H2F) to the 5,6,7,8-tetrahydrofolate needed to maintain intracellular pools of tetrahydrofolate and its derivatives. These are essential cofactors in the biosynthesis of purines, pyrimidines and several amino acids
physiological function
-
dihydrofolate reductase is an essential enzyme in the tetrahydrofolate pathway which catalyzes the NADPH-dependent reduction of 7,8-dihydrofolate (H2F) to the 5,6,7,8-tetrahydrofolate needed to maintain intracellular pools of tetrahydrofolate and its derivatives. These are essential cofactors in the biosynthesis of purines, pyrimidines and several amino acids
physiological function
DHFR-TS is essential for cell survival of Trypanosoma brucei
physiological function
-
the human thymidylate synthase and dihydrofolate reductase catalyse two consecutive reactions in the folate metabolism pathway and are very likely to bind in the same multi-enzyme complex in vivo, substrate channeling occurs between the human thymidylate synthase and dihydrofolate reductase, analysis by protein-protein docking, electrostatics calculations, and Brownian dynamics, overview. The non-covalently bound human thymidylate synthase and dihydrofolate reductase are capable of substrate channeling and the formation of the surface electrostatic highway. The substrate channeling efficiency between the two can be reasonably high and comparable to that of the bifunctional protozoan enzyme
physiological function
-
thymidylate synthase plays an essential role in embryogenesis, embryos with their thymidylate synthase function inhibited show a retarded embryo development and irregular cell sizes
-
physiological function
-
DHFR-TS is essential for cell survival of Trypanosoma brucei
-
additional information
TS domain structure analysis, overview. The TS domain of the enzyme forms the largest portion of the dimerization interface mainly through a five-stranded beta-sheet from each monomer. The catalytic cysteine 489 is responsible for catalysis, te active site is comprised of residues from both monomers. Several conserved arginines bind dUMP, i.e. R344, R510 as well as R469 and R470 from the adjacent monomer
additional information
-
in vitro, one human thymidylate synthase dimer binds to up to six human dihydrofolate reductase monomers, protein-protein docking process, overview. Existence of bound-state conformations of the human DHFR and TS proteins where a continuous positive surface potential region, connecting the TS and DHFR active sites, is formed
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(-)-tetrahydropteroylglutamate + 2'-deoxyuridine 5'-monophosphate
7,8-dihydropteroylglutamate + thymidine phosphate
(6R)-N5,N10-methylene-5,6,7,8-tetrahydrofolate + 2'-deoxyuridylate
7,8-dihydrofolate + 5-methyl-2'-deoxyuridylate
(6S)-methylenetetrahydropteroylhexaglutamate + 2'-deoxyuridylate
7,8-dihydropteroylhexaglutamate + thymidine phosphate
-
-
-
-
r
(6S)-tetrahydropteroylglutamate + 2-deoxyuridylate
7,8-dihydropteroylglutamate + thymidine phosphate
(6S)-tetrahydropteroyltriglutamate + 2'-deoxyuridylate
7,8-dihydropteroyltriglutamate + thymidine phosphate
-
-
-
-
r
(R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + 2'-deoxycytidine 5'-monophosphate
dihydrofolate + cytidine phosphate
5,10-methylenetetrahydrofolate + 2'-fluoro-2'-deoxyuridine 5'-phosphate
7,8-dihydrofolate + ?
5,10-methylenetetrahydrofolate + 5'-fluoro-2'-deoxyuridine 5'-phosphate
7,8-dihydrofolate + ?
-
some mutants are capable of forming covalent thymidylate synthase-5-fluoro-dUMP-methylenetetrahydrofolate complex
-
-
?
5,10-methylenetetrahydrofolate + deoxyuridine monophosphate
7,8-dihydrofolate + deoxythymidine monophosphate
-
-
-
?
5,10-methylenetetrahydrofolylheptaglutamate + 2'-deoxyuridylate
7,8-dihydrofolylheptaglutamate + thymidine phosphate
-
-
-
-
r
5,10-methylenetetrahydrofolylpentaglutamate + 2'-deoxyuridylate
7,8-dihydrofolylpentaglutamate + thymidine phosphate
-
-
-
-
r
5,10-methylenetetrahydropteroylheptaglutamate + 2'-deoxyuridylate
7,8-dihydropteroylheptaglutamate + thymidine phosphate
5,10-methylenetetrahydropteroylpentaglutamate + 2'-deoxyuridylate
7,8-dihydropteroylpentaglutamate + thymidine phosphate
N5,10-methylenetetrahydrofolate + 2'-deoxyuridine 5'-dithiophosphate
7,8-dihydrofolate + ?
N5,10-methylenetetrahydrofolate + 5-hydroxy-2'-deoxyuridine 5'-monophosphate
7,8-dihydrofolate + ?
-
-
-
-
?
(-)-tetrahydropteroylglutamate + 2'-deoxyuridine 5'-monophosphate
7,8-dihydropteroylglutamate + thymidine phosphate
-
-
-
-
-
(-)-tetrahydropteroylglutamate + 2'-deoxyuridine 5'-monophosphate
7,8-dihydropteroylglutamate + thymidine phosphate
-
-
-
-
?
(-)-tetrahydropteroylglutamate + 2'-deoxyuridine 5'-monophosphate
7,8-dihydropteroylglutamate + thymidine phosphate
Escherichia coli B / ATCC 11303
-
-
-
-
-
(-)-tetrahydropteroylglutamate + 2'-deoxyuridine 5'-monophosphate
7,8-dihydropteroylglutamate + thymidine phosphate
Escherichia coli B / ATCC 11303
-
-
-
-
?
(6R)-N5,N10-methylene-5,6,7,8-tetrahydrofolate + 2'-deoxyuridylate
7,8-dihydrofolate + 5-methyl-2'-deoxyuridylate
-
-
-
r
(6R)-N5,N10-methylene-5,6,7,8-tetrahydrofolate + 2'-deoxyuridylate
7,8-dihydrofolate + 5-methyl-2'-deoxyuridylate
-
-
-
-
r
(6S)-tetrahydropteroylglutamate + 2-deoxyuridylate
7,8-dihydropteroylglutamate + thymidine phosphate
-
-
-
-
-
(6S)-tetrahydropteroylglutamate + 2-deoxyuridylate
7,8-dihydropteroylglutamate + thymidine phosphate
-
-
-
-
r
(6S)-tetrahydropteroylglutamate + 2-deoxyuridylate
7,8-dihydropteroylglutamate + thymidine phosphate
-
-
-
-
-
(6S)-tetrahydropteroylglutamate + 2-deoxyuridylate
7,8-dihydropteroylglutamate + thymidine phosphate
-
-
-
-
-
(6S)-tetrahydropteroylglutamate + 2-deoxyuridylate
7,8-dihydropteroylglutamate + thymidine phosphate
-
-
-
-
-
5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
-
?
5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
-
-
5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
-
?
5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
thymidylate synthase is the third enzyme in the methylene tetrahydrofolate cycle besides dihydrofolate reductase and serine hydroxymethyltransferase, in many organisms, thymidylate synthase is the only de novo source for dTMP required for DNA synthesis
-
-
?
5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
-
-
5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + 2'-deoxycytidine 5'-monophosphate
dihydrofolate + cytidine phosphate
-
only mutant TS N229D
-
-
?
5,10-methylenetetrahydrofolate + 2'-deoxycytidine 5'-monophosphate
dihydrofolate + cytidine phosphate
-
only mutant TS N229D
-
-
?
5,10-methylenetetrahydrofolate + 2'-fluoro-2'-deoxyuridine 5'-phosphate
7,8-dihydrofolate + ?
-
-
-
-
?
5,10-methylenetetrahydrofolate + 2'-fluoro-2'-deoxyuridine 5'-phosphate
7,8-dihydrofolate + ?
Escherichia coli B / ATCC 11303
-
-
-
-
?
5,10-methylenetetrahydrofolate + 2'-fluoro-2'-deoxyuridine 5'-phosphate
7,8-dihydrofolate + ?
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
thymidylate synthase is essential for de novo synthesis of dTMP and is a key enzyme involved in DNA synthesis and transcriptional regulation of organisms
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
inhibition of thymidylate synthase or of DHFR leads to thymineless death of eukaryotic organisms
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
it is a key enzyme for the synthesis of the DNA-specific nucleotide thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
thymidylate synthase catalyses the only de novo pathway to produce thymidylate for DNA replication and repair
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
thymidylate synthase is a key enzyme in the de novo synthesis of dTMP
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
TS is a key enzyme in folate metabolism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
mTHF, TS is the sole source of de novo thymidylate which is required for DNA synthesis
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
thymidylate synthase is an essential enzyme for de novo synthesis of thymidylate (dTMP), a precursor for DNA synthesis
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + TMP
-
during TS inhibition, TMP levels decrease with a subsequent increase in dUTP
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
reverse reaction is at least 630times slower than the forward reaction
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
485357, 485363, 485365, 485369, 485371, 485372, 485374, 485382, 485383, 485388, 485397, 485402, 485406, 485409, 485413, 485416, 485417
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
485357, 485359, 485363, 485365, 485369, 485371, 485372, 485373, 485374, 485375, 485376, 485380, 485381, 485382, 485383, 485388, 485389, 485397, 485402, 485405, 485406, 485408, 485409, 485413, 485415, 485416, 485417
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
reverse reaction is at least 630times slower than the forward reaction
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
485382, 485387, 485393, 485398, 485407, 485413, 485426, 485428, 485429, 702996, 703391, 703950, 705044, 706625, 711474, 718866, 719078, 719649, 720965, 720995
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
485359, 485364, 485375, 485376, 485381, 485382, 485384, 485387, 485389, 485393, 485395, 485398, 485400, 485403, 485404, 485407, 485408, 485413, 485415, 485419, 485422, 485423, 485426, 485428, 485429, 485430
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
reverse reaction is at least 630times slower than the forward reaction
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
485358, 485359, 485364, 485375, 485376, 485381, 485384, 485395, 485403, 485404, 485408, 485415, 485423, 485430
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
485359, 485360, 485363, 485364, 485365, 485366, 485368, 485369, 485370, 485372, 485376, 485377, 485378, 485379, 485380, 485382, 485383, 485384, 485387, 485388, 485393, 485396, 485397, 485399, 485401, 485403, 485406, 485409, 485410, 485411, 485415, 485416, 485418, 485423, 485427, 485429, 485430, 485431
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
485359, 485360, 485361, 485363, 485364, 485365, 485366, 485368, 485369, 485370, 485372, 485375, 485376, 485377, 485378, 485379, 485380, 485381, 485382, 485383, 485384, 485385, 485387, 485388, 485389, 485393, 485396, 485397, 485399, 485400, 485401, 485403, 485405, 485406, 485409, 485410, 485411, 485415, 485416, 485418, 485419, 485423, 485427, 485429, 485430, 485431
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Leishmania braziliensis subsp. viannia
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
392255, 485359, 485360, 485363, 485365, 485368, 485369, 485382, 485383, 485384, 485386, 485387, 485390, 485391, 485393, 485398, 485402, 485403, 485413, 485415, 485426, 485427, 485430, 704570
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
392255, 485359, 485360, 485361, 485363, 485365, 485368, 485369, 485373, 485375, 485382, 485383, 485384, 485386, 485387, 485390, 485391, 485393, 485398, 485400, 485402, 485403, 485404, 485413, 485415, 485426, 485427, 485430
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
dUMP substrate binding structure analysis
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Trypanosoma rhodesiense
-
-
-
-
?, r
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
tetrahydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
tetrahydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
tetrahydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
tetrahydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + uridine 5'-phosphate
dihydrofolate + TMP
-
-
-
-
r
5,10-methylenetetrahydrofolate + uridine 5'-phosphate
dihydrofolate + TMP
-
-
-
-
r
5,10-methylenetetrahydropteroylheptaglutamate + 2'-deoxyuridylate
7,8-dihydropteroylheptaglutamate + thymidine phosphate
-
-
-
-
r
5,10-methylenetetrahydropteroylheptaglutamate + 2'-deoxyuridylate
7,8-dihydropteroylheptaglutamate + thymidine phosphate
-
-
-
-
r
5,10-methylenetetrahydropteroylpentaglutamate + 2'-deoxyuridylate
7,8-dihydropteroylpentaglutamate + thymidine phosphate
-
-
-
-
r
5,10-methylenetetrahydropteroylpentaglutamate + 2'-deoxyuridylate
7,8-dihydropteroylpentaglutamate + thymidine phosphate
-
-
-
-
r
5-bromo-2'-deoxyuridine 5'-monophosphate + ?
?
-
dehalogenation
-
-
?
5-bromo-2'-deoxyuridine 5'-monophosphate + ?
?
-
dehalogenation does not require methylenetetrahydrofolate as cosubstrate
-
-
?
5-bromo-2'-deoxyuridine 5'-monophosphate + ?
?
-
dehalogenation
-
-
?
5-bromo-2'-deoxyuridine 5'-monophosphate + ?
?
-
dehalogenated by recombinant rat hepatoma enzyme
-
-
?
5-iodo-2'-deoxyuridine 5'-monophosphate + ?
?
-
dehalogenated by recombinant rat hepatoma enzyme
-
-
?
N5,10-methylenetetrahydrofolate + 2'-deoxyuridine 5'-dithiophosphate
7,8-dihydrofolate + ?
-
-
-
-
?
N5,10-methylenetetrahydrofolate + 2'-deoxyuridine 5'-dithiophosphate
7,8-dihydrofolate + ?
-
-
-
-
?
N5,10-methylenetetrahydrofolate + 2'-deoxyuridine 5'-thiophosphate
7,8-dihydrofolate + ?
-
-
-
-
?
N5,10-methylenetetrahydrofolate + 2'-deoxyuridine 5'-thiophosphate
7,8-dihydrofolate + ?
-
-
-
-
?
N5,N10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + TMP
-
during thymidylate synthase inhibition, TMP levels decrease with a subsequent increase in dUTP
-
-
?
[6R,S]-5,10-methylenetetrahydropteroylglutamate + 2'-deoxyuridylate
?
-
-
-
-
-
additional information
?
-
-
thymidylate synthase form ThyX has no activity in Corynebacterium glutamicum
-
-
-
additional information
?
-
-
thymidylate synthase form ThyX has no activity in Corynebacterium glutamicum
-
-
-
additional information
?
-
-
the enzyme is specifically bound with its cognate mRNA in vitro and in vivo
-
-
-
additional information
?
-
-
UMP, dCMP and deoxyuridine are no substrates
-
-
-
additional information
?
-
-
nucleotides with large substituents on the 2' position are no substrates
-
-
-
additional information
?
-
-
enzyme catalyzes the exchange of a hydrogen atom between water and position 5 of dUMP, occurrence of reactions other than a methyl-group transfer during the interaction of the enzyme with its 2 substrates
-
-
-
additional information
?
-
-
chemical conversion takes place preferentially via a concerted mechanism where the hydride transfer is conjugated to thiol-elimination from the product. The substrate-enzyme covalent bond established between the C6 of the nucleotide substrate and a conserved cysteine residue is of labile character
-
-
-
additional information
?
-
Escherichia coli B / ATCC 11303
-
nucleotides with large substituents on the 2' position are no substrates
-
-
-
additional information
?
-
Escherichia coli B / ATCC 11303
-
enzyme catalyzes the exchange of a hydrogen atom between water and position 5 of dUMP, occurrence of reactions other than a methyl-group transfer during the interaction of the enzyme with its 2 substrates
-
-
-
additional information
?
-
-
nucleotides with large substituents on the 2' position are no substrates
-
-
-
additional information
?
-
-
enzyme catalyzes the exchange of a hydrogen atom between water and position 5 of dUMP, occurrence of reactions other than a methyl-group transfer during the interaction of the enzyme with its 2 substrates
-
-
-
additional information
?
-
recombinant protein is able to bind its own RNA
-
-
-
additional information
?
-
-
recombinant protein is able to bind its own RNA
-
-
-
additional information
?
-
-
inhibitors targeted at human TS designed from structures of bacterial TS may not be optimal
-
-
-
additional information
?
-
-
dCMP is no substrate, exception mutant TS N229D
-
-
-
additional information
?
-
-
dCMP is no substrate, exception mutant TS N229D
-
-
-
additional information
?
-
-
bifunctional enzyme dihydrofolate reductase-thymidylate synthase
-
-
-
additional information
?
-
-
bifunctional enzyme dihydrofolate reductase-thymidylate synthase
-
-
-
additional information
?
-
-
bifunctional enzyme dihydrofolate reductase-thymidylate synthase
-
-
-
additional information
?
-
-
bifunctional enzyme dihydrofolate reductase-thymidylate synthase
-
-
-
additional information
?
-
-
bifunctional enzyme dihydrofolate reductase-thymidylate synthase
-
-
-
additional information
?
-
-
uridylate, cytidylate and deoxycytidylate are not substrates
-
-
-
additional information
?
-
-
bifunctional enzyme thymidilate synthase-dihydrofolate reductase, not possible to separate the 2 activities
-
-
-
additional information
?
-
-
bifunctional enzyme dihydrofolate reductase-thymidylate synthase
-
-
-
additional information
?
-
-
bifunctional enzyme dihydrofolate reductase-thymidylate synthase
-
-
-
additional information
?
-
molecular mechanism of the distinct differences in substrate channeling behavior between Toxoplasma gondii TS-DHFR and Cryptosporidium hominis TS-DHFR, overview
-
-
-
additional information
?
-
the bifunctional folate and pyrimidine-metabolising enzyme dihydrofolate reductase-thymidylate synthase dihydrofolate reductase-thymidylate synthase is expressed from a single gene as a homodimer comprising of an N-terminal DHFR domain fused via a linker peptide to a thymidylate synthase domain at the C-terminus
-
-
-
additional information
?
-
no activity with folic acid and the structurally related pterins (biopterin, dihydrobiopterin, sepiapterin and neopterin) as substrates by enzyme DHFR-TS
-
-
-
additional information
?
-
the bifunctional folate and pyrimidine-metabolising enzyme dihydrofolate reductase-thymidylate synthase dihydrofolate reductase-thymidylate synthase is expressed from a single gene as a homodimer comprising of an N-terminal DHFR domain fused via a linker peptide to a thymidylate synthase domain at the C-terminus
-
-
-
additional information
?
-
no activity with folic acid and the structurally related pterins (biopterin, dihydrobiopterin, sepiapterin and neopterin) as substrates by enzyme DHFR-TS
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
thymidylate synthase is the third enzyme in the methylene tetrahydrofolate cycle besides dihydrofolate reductase and serine hydroxymethyltransferase, in many organisms, thymidylate synthase is the only de novo source for dTMP required for DNA synthesis
-
-
?
5,10-methylenetetrahydrofolate + deoxyuridine monophosphate
7,8-dihydrofolate + deoxythymidine monophosphate
B5U9U8
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + TMP
-
during TS inhibition, TMP levels decrease with a subsequent increase in dUTP
-
-
?
N5,N10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + TMP
-
during thymidylate synthase inhibition, TMP levels decrease with a subsequent increase in dUTP
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
A6M9A2
thymidylate synthase is essential for de novo synthesis of dTMP and is a key enzyme involved in DNA synthesis and transcriptional regulation of organisms
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
inhibition of thymidylate synthase or of DHFR leads to thymineless death of eukaryotic organisms
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
it is a key enzyme for the synthesis of the DNA-specific nucleotide thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
thymidylate synthase catalyses the only de novo pathway to produce thymidylate for DNA replication and repair
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
thymidylate synthase is a key enzyme in the de novo synthesis of dTMP
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
TS is a key enzyme in folate metabolism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
-
thymidylate synthase is an essential enzyme for de novo synthesis of thymidylate (dTMP), a precursor for DNA synthesis
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
P9WFR9
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
P0CS13
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
P0CS13
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
P0CS13
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
P0CS13
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
A0A0S4TER9
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
485357, 485363, 485365, 485369, 485371, 485372, 485374, 485382, 485383, 485388, 485397, 485402, 485406, 485409, 485413, 485416, 485417
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Escherichia coli B / ATCC 11303
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
485358, 485359, 485364, 485375, 485376, 485381, 485384, 485395, 485403, 485404, 485408, 485415, 485423, 485430
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
P04818
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
485359, 485360, 485363, 485364, 485365, 485366, 485368, 485369, 485370, 485372, 485376, 485377, 485378, 485379, 485380, 485382, 485383, 485384, 485387, 485388, 485393, 485396, 485397, 485399, 485401, 485403, 485406, 485409, 485410, 485411, 485415, 485416, 485418, 485423, 485427, 485429, 485430, 485431
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
Leishmania braziliensis subsp. viannia
A4H4P8
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
S5M3K7
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
392255, 485359, 485360, 485363, 485365, 485368, 485369, 485382, 485383, 485384, 485386, 485387, 485390, 485391, 485393, 485398, 485402, 485403, 485413, 485415, 485426, 485427, 485430
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
key function in DNA synthesis, repair and cell division
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
P13100
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
biosynthesis of thymidylic acid, only de novo source of thymidine, crucial for DNA replication in every organism
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
-
-
-
-
?
additional information
?
-
A6M9A2
recombinant protein is able to bind its own RNA
-
-
-
additional information
?
-
-
recombinant protein is able to bind its own RNA
-
-
-
additional information
?
-
Q27783
the bifunctional folate and pyrimidine-metabolising enzyme dihydrofolate reductase-thymidylate synthase dihydrofolate reductase-thymidylate synthase is expressed from a single gene as a homodimer comprising of an N-terminal DHFR domain fused via a linker peptide to a thymidylate synthase domain at the C-terminus
-
-
-
additional information
?
-
Q27783
the bifunctional folate and pyrimidine-metabolising enzyme dihydrofolate reductase-thymidylate synthase dihydrofolate reductase-thymidylate synthase is expressed from a single gene as a homodimer comprising of an N-terminal DHFR domain fused via a linker peptide to a thymidylate synthase domain at the C-terminus
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE