Information on EC 2.1.1.45 - thymidylate synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.45
-
RECOMMENDED NAME
GeneOntology No.
thymidylate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehalogenation
-
-
-
-
methylene group transfer
-
-
-
-
reductive methylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
folate transformations II
-
-
Metabolic pathways
-
-
N10-formyl-tetrahydrofolate biosynthesis
-
-
One carbon pool by folate
-
-
pyrimidine deoxyribonucleosides salvage
-
-
pyrimidine deoxyribonucleotides biosynthesis from CTP
-
-
pyrimidine deoxyribonucleotides de novo biosynthesis I
-
-
pyrimidine deoxyribonucleotides de novo biosynthesis II
-
-
pyrimidine deoxyribonucleotides de novo biosynthesis IV
-
-
pyrimidine metabolism
-
-
Pyrimidine metabolism
-
-
superpathway of pyrimidine deoxyribonucleotides de novo biosynthesis (E. coli)
-
-
SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:dUMP C-methyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9031-61-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Abies sp.
pine
-
-
Manually annotated by BRENDA team
unicellular green algae
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
metastrongyloid nematode, synonym Parastrongylus
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Bristol N2
-
-
Manually annotated by BRENDA team
Caenorhabditis elegans Bristol N2
strain Bristol N2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
carrot, wild and culture form
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Escherichia coli EM 20031 K12
strain EM 20031 K12
-
-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
strain R2
-
-
Manually annotated by BRENDA team
strain TS N229D, TS N229C
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
AV19
-
-
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicum
-
-
-
Manually annotated by BRENDA team
isoform ThyA
UniProt
Manually annotated by BRENDA team
strain MS11
-
-
Manually annotated by BRENDA team
Neosartorya fischeri
-
-
-
Manually annotated by BRENDA team
tobacco
-
-
Manually annotated by BRENDA team
no activity in Aeropyrum pernix
-
-
-
Manually annotated by BRENDA team
no activity in Aquifex aeolicus
-
-
-
Manually annotated by BRENDA team
no activity in Pyrobaculum aerophilum
-
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus abyssi
-
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus furiosus
DSM 3638
-
-
Manually annotated by BRENDA team
no activity in Pyrococcus horikoshii
-
-
-
Manually annotated by BRENDA team
no activity in Sulfolobus solfataricus
-
-
-
Manually annotated by BRENDA team
no activity in Sulfolobus tokodaii
-
-
-
Manually annotated by BRENDA team
no activity in Thermoplasma acidophilum
-
-
-
Manually annotated by BRENDA team
no activity in Thermoplasma volcanium
-
-
-
Manually annotated by BRENDA team
no activity in Thermotoga maritima
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain TM4/8.2
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Wistar
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
industrial strain BMK
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-
Manually annotated by BRENDA team
pig
-
-
Manually annotated by BRENDA team
causes nagana, the equivalent disease of cattle
-
-
Manually annotated by BRENDA team
natural pathogen of rats
-
-
Manually annotated by BRENDA team
Trypanosoma rhodesiense
causes human sleeping sickness
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-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(-)-tetrahydropteroylglutamate + 2'-deoxyuridine 5'-monophosphate
7,8-dihydropteroylglutamate + thymidine phosphate
show the reaction diagram
(6R)-N5,N10-methylene-5,6,7,8-tetrahydrofolate + 2'-deoxyuridylate
7,8-dihydrofolate + 5-methyl-2'-deoxyuridylate
show the reaction diagram
(6S)-methylenetetrahydropteroylhexaglutamate + 2'-deoxyuridylate
7,8-dihydropteroylhexaglutamate + thymidine phosphate
show the reaction diagram
-
-
-
-
r
(6S)-tetrahydropteroylglutamate + 2-deoxyuridylate
7,8-dihydropteroylglutamate + thymidine phosphate
show the reaction diagram
(6S)-tetrahydropteroyltriglutamate + 2'-deoxyuridylate
7,8-dihydropteroyltriglutamate + thymidine phosphate
show the reaction diagram
-
-
-
-
r
(R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
show the reaction diagram
-
-
-
-
?
(R)-5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
show the reaction diagram
-
-
-
-
?
5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
show the reaction diagram
5,10-methylenetetrahydrofolate + 2'-deoxycytidine 5'-monophosphate
dihydrofolate + cytidine phosphate
show the reaction diagram
5,10-methylenetetrahydrofolate + 2'-fluoro-2'-deoxyuridine 5'-phosphate
7,8-dihydrofolate + ?
show the reaction diagram
5,10-methylenetetrahydrofolate + 5'-fluoro-2'-deoxyuridine 5'-phosphate
7,8-dihydrofolate + ?
show the reaction diagram
-
some mutants are capable of forming covalent thymidylate synthase-5-fluoro-dUMP-methylenetetrahydrofolate complex
-
-
?
5,10-methylenetetrahydrofolate + 6-fluoro-dUMP
?
show the reaction diagram
-
-
-
-
?
5,10-methylenetetrahydrofolate + deoxyuridine monophosphate
7,8-dihydrofolate + deoxythymidine monophosphate
show the reaction diagram
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
show the reaction diagram
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + TMP
show the reaction diagram
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
show the reaction diagram
5,10-methylenetetrahydrofolate + dUMP
tetrahydrofolate + dTMP
show the reaction diagram
5,10-methylenetetrahydrofolate + uridine 5'-phosphate
dihydrofolate + TMP
show the reaction diagram
5,10-methylenetetrahydrofolylheptaglutamate + 2'-deoxyuridylate
7,8-dihydrofolylheptaglutamate + thymidine phosphate
show the reaction diagram
-
-
-
-
r
5,10-methylenetetrahydrofolylpentaglutamate + 2'-deoxyuridylate
7,8-dihydrofolylpentaglutamate + thymidine phosphate
show the reaction diagram
-
-
-
-
r
5,10-methylenetetrahydropteroylheptaglutamate + 2'-deoxyuridylate
7,8-dihydropteroylheptaglutamate + thymidine phosphate
show the reaction diagram
5,10-methylenetetrahydropteroylpentaglutamate + 2'-deoxyuridylate
7,8-dihydropteroylpentaglutamate + thymidine phosphate
show the reaction diagram
5-bromo-2'-deoxyuridine 5'-monophosphate + ?
?
show the reaction diagram
5-iodo-2'-deoxyuridine 5'-monophosphate + ?
?
show the reaction diagram
N5,10-methylenetetrahydrofolate + 2'-deoxyuridine 5'-dithiophosphate
7,8-dihydrofolate + ?
show the reaction diagram
N5,10-methylenetetrahydrofolate + 2'-deoxyuridine 5'-thiophosphate
7,8-dihydrofolate + ?
show the reaction diagram
N5,10-methylenetetrahydrofolate + 5-hydroxy-2'-deoxyuridine 5'-monophosphate
7,8-dihydrofolate + ?
show the reaction diagram
-
-
-
-
?
N5,N10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + TMP
show the reaction diagram
[6R,S]-5,10-methylenetetrahydropteroylglutamate + 2'-deoxyuridylate
?
show the reaction diagram
[6R]-methylenetetrahydropteroylglutamate + 2'-deoxyuridylate
?
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
show the reaction diagram
-
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
show the reaction diagram
B5U9U8
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + dTMP
show the reaction diagram
5,10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + TMP
show the reaction diagram
-
during TS inhibition, TMP levels decrease with a subsequent increase in dUTP
-
-
?
5,10-methylenetetrahydrofolate + dUMP
dihydrofolate + dTMP
show the reaction diagram
N5,N10-methylenetetrahydrofolate + dUMP
7,8-dihydrofolate + TMP
show the reaction diagram
-
during thymidylate synthase inhibition, TMP levels decrease with a subsequent increase in dUTP
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+)-methylenetetrahydrofolate
(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate
-
-
methenyltetrahydrofolate
methenyltetrahydropteroylglutamate
-
-
methylenetetrahydrofolate
-
-
N5,N10-methylenetetrahydrofolate
NADPH
-
absolute requirement
additional information
-
the enzyme is FAD-independent
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
-
stimulates activity
INHIBITORS
ORGANISM
UNIPROT