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5,10-methylenetetrahydrofolate + BrdUMP + FADH2
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
5,10-methylenetetrahydrofolate + dUMP + FADH2 + O2
dTMP + tetrahydrofolate + FAD + H2O2
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
5,10-methylenetetrahydrofolate + dUMP + NADPH
dTMP + tetrahydrofolate + NADP
5,10-methylenetetrahydrofolate + dUMP + NADPH + H+
dTMP + tetrahydrofolate + NADP+
additional information
?
-
5,10-methylenetetrahydrofolate + BrdUMP + FADH2
?
-
-
-
-
?
5,10-methylenetetrahydrofolate + BrdUMP + FADH2
?
-
-
-
?
5,10-methylenetetrahydrofolate + BrdUMP + FADH2
?
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
the flavin is oxidized after dUMP reacts with 5,10-methylenetetrahydrofolate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
dUMP binding accelerates the O2-insensitive half-reaction between NADPH and FAD by over four orders of magnitude to about 30 per s. Although dUMP does not have a direct role in FAD reduction, any turnover with molecular O2 requires its presence. Inversely, NADPH accommodation accelerates dUMP binding about 3fold and apparently precedes dUMP binding under physiological conditions. In the oxidative half-reaction, excess N5,N10-methylene-5,6,7,8-tetrahydrofolate reoxidizes FADH2 within 1 ms, thus very efficiently competing with FADH2 oxidation by O2
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
Paramecium bursaria Chlorella virus-1
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
Rhodobacter capsulatus ThyX is required for de novo thymidylate synthesis
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
Rhodobacter capsulatus ThyX is required for de novo thymidylate synthesis
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
dUMP dependent lag-phase for the single turnover reduction of FDTS bound FAD by NADPH
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FMNH2
dTMP + tetrahydrofolate + FMN
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + NADPH
dTMP + tetrahydrofolate + NADP
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + NADPH
dTMP + tetrahydrofolate + NADP
-
Rhodobacter capsulatus ThyX is required for de novo thymidylate synthesis
-
-
?
5,10-methylenetetrahydrofolate + dUMP + NADPH + H+
dTMP + tetrahydrofolate + NADP+
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + NADPH + H+
dTMP + tetrahydrofolate + NADP+
-
-
-
?
additional information
?
-
Paramecium bursaria Chlorella virus-1
-
oxidation of NAD(P)H is linked to the reduction of enzyme bound FAD, dUMP is required for efficient FAD reduction, omitting of 5,10-methylenetetrahydrofolate from reaction mixture increases oxidation activity by a factor of 7
-
-
?
additional information
?
-
-
mRNA binding traits
-
-
?
additional information
?
-
possesses RNA-binding activity, binds to the stemloop RNA structure
-
-
?
additional information
?
-
-
possesses RNA-binding activity, binds to the stemloop RNA structure
-
-
?
additional information
?
-
the enzyme is essential to DNA replication
-
-
?
additional information
?
-
-
the enzyme is essential to DNA replication
-
-
?
additional information
?
-
flavin-dependent thymidylate synthase can function as an oxidase, which catalyzes the reduction of O2 to H2O2, using reduced NADPH or other reducing agents and a sequential kinetic mechanism of substrate binding. Tetrahydrofolate competitively inhibits the oxidase activity, which indicates that tetrahydrofolate and O2 compete for the same reduced and dUMP-activated enzymatic complex
-
-
?
additional information
?
-
an initial activation of the pyrimidine substrate by reduced flavin is required for catalysis. A H/D exchange at C5 of dUMP in D2O requires the flavin to be reduced, as observed experimentally. Chemical trapping of reaction intermediates shows the unusual intermediates of further steps
-
-
?
additional information
?
-
an initial activation of the pyrimidine substrate by reduced flavin is required for catalysis. A H/D exchange at C5 of dUMP in D2O requires the flavin to be reduced, as observed experimentally. Chemical trapping of reaction intermediates shows the unusual intermediates of further steps
-
-
?
additional information
?
-
the enzyme is essential to DNA replication
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
5,10-methylenetetrahydrofolate + dUMP + FADH2 + O2
dTMP + tetrahydrofolate + FAD + H2O2
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + NADPH
dTMP + tetrahydrofolate + NADP
-
Rhodobacter capsulatus ThyX is required for de novo thymidylate synthesis
-
-
?
additional information
?
-
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
Rhodobacter capsulatus ThyX is required for de novo thymidylate synthesis
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
Rhodobacter capsulatus ThyX is required for de novo thymidylate synthesis
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
-
-
-
?
5,10-methylenetetrahydrofolate + dUMP + FADH2
dTMP + tetrahydrofolate + FAD
-
de novo synthesis of thymidylate
-
-
?
additional information
?
-
the enzyme is essential to DNA replication
-
-
?
additional information
?
-
-
the enzyme is essential to DNA replication
-
-
?
additional information
?
-
the enzyme is essential to DNA replication
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R)-2-[(3,5-dioxo-2,3,4,5-tetrahydro-1,2,4-triazin-6-yl)sulfanyl]propanoic acid
6% inhibition at 0.1 mM
(heptanoyl[[(4R)-2-phenyl-3-(phenylcarbonyl)-1,3-thiazolidin-4-yl]methyl] amino)acetic acid
-
10-methyl-5,8-dideazafolate
Paramecium bursaria Chlorella virus-1
-
0.2 mM, 90% inhibition
10-propargylfolate
Paramecium bursaria Chlorella virus-1
-
0.2 mM, 85% inhibition
2-(furan-2-yl)-3-hydroxynaphthalene-1,4-dione
inhibits the NADPH oxidation and 2'-deoxythymidine-5'-monophosphate-forming activities of ThyX in vitro
2-hydroxy-3-(4-methoxyphenyl)naphthalene-1,4-dione
inhibits the NADPH oxidation and 2'-deoxythymidine-5'-monophosphate-forming activities of ThyX in vitro
2-hydroxy-3-propylnaphthalene-1,4-dione
inhibits the NADPH oxidation and 2'-deoxythymidine-5'-monophosphate-forming activities of ThyX in vitro, significant decrease of 1.22 log (17fold) in the colonization loads with Helicobacter pylori of mice treated with the molecule
2-[4-fluoro-3-(trifluoromethyl)phenyl]-3-hydroxynaphthalene-1,4-dione
inhibits the NADPH oxidation and 2'-deoxythymidine-5'-monophosphate-forming activities of ThyX in vitro
4-(3-(3-oxo-2,3-dihydro-4H-pyrido[3,2-b][1,4]oxazin-4-yl)propanoyl)-N-phenylpiperazine-1-carboxamide
-
4-[3-(3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl)propanoyl]-N-phenylpiperazine-1-carboxamide
-
5,10-methylenetetrahydrofolate
Paramecium bursaria Chlorella virus-1
-
-
5-fluoro-2'-deoxyuridine 5'-monophosphate
-
FdUMP
5-fluorodeoxyuridine
Paramecium bursaria Chlorella virus-1
-
0.05 mM, 95% inhibition
5-undecyloxymethyl-2'-deoxyuridine 5'-monophosphate
8-aminopurinone deoxyribonucleoside 5'-phosphate
Paramecium bursaria Chlorella virus-1
-
0.05 mM, 50% inhibition
diethyldicarbonate
Paramecium bursaria Chlorella virus-1
-
decreases ThyX deprotonation activity at least 20fold, is partially reversible with hydroxylamine treatment
ethyl (4R)-2-phenyl-3-([(1-(3-2,2,2-trifluoroacetamido)propyl)-1H-1,2,3-triazol-4-yl]carbonyl)-1,3-thiazolidine-4-carboxylate
-
ethyl (4R)-2-phenyl-3-[[1-(2-thiophen-3-ylethyl)-1H-1,2,3-triazol-4-yl]carbonyl]-1,3-thiazolidine-4-carboxylate
-
ethyl (4R)-3-([1-[2-(4-fluorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]carbonyl)-2-phenyl-1,3-thiazolidine-4-carboxylate
-
ethyl (4R)-3-[[1-(7-hydroxyheptyl)-1H-1,2,3-triazol-4-yl]carbonyl]-2-phenyl-1,3-thiazolidine-4-carboxylate
-
N-methyl-2-[4-[3-(3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl)propanoyl]piperazin-1-yl]-N-phenylacetamide
-
N-[1-[3-(3-oxo-2,3-dihydro-4H-1,4-benzoxazin-4-yl)propanoyl]piperidin-4-yl]-N'-phenylurea
-
tetrahydrofolate
competitively inhibits the oxidase activity of the enzyme, which indicates that tetrahydrofolate and O2 compete for the same reduced and dUMP-activated enzymatic complex
5-undecyloxymethyl-2'-deoxyuridine 5'-monophosphate
-
no activity against classical thymidylate synthase ThyA, EC 2.1.1.45
5-undecyloxymethyl-2'-deoxyuridine 5'-monophosphate
compound lacks activity against isoform ThyA, EC 2.1.1.45
NADPH
excess NADPH decreases enzyme activity
NADPH
-
inhibits FDTS at high concentrations at all temperatures, NADPH may not be the natural reducing agent of FDTS
additional information
-
functional evidence for active site location of tetrameric thymidylate synthase X at the interphase of three monomers. The active-site configurations of ThyX proteins, present in many human pathogenic bacteria, and of human thymidylate synthase A (EC 2.1.1.45) are different.
-
additional information
Paramecium bursaria Chlorella virus-1
-
no inhibition by 10-propargyl-5,6-dideazafolate, 10-methylfolate, 8-azapurinone deoxyribonucleoside 5-phosphate
-
additional information
Paramecium bursaria Chlorella virus-1
-
5-fluorouracil is not a potential inhibitor
-
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H48Q
-
inactive mutant enzyme
H48Q/S84A
-
inactive mutant enzyme
H48Q/S84C
-
inactive mutant enzyme
R74A
-
the KM-value for dUMP is 5.1fold higher than the wild-type value, the turnover-number is 4.6fold lower than the wild-type value
R74K
-
the KM-value for dUMP is nearly identical to wild-type value, the turnover-number is 6.6fold lower than the wild-type value
S84A
-
the KM-value for dUMP is 5.3fold higher than the wild-type value, the turnover-number is 2.1fold lower than the wild-type value. Mutation abolishes thymidylate synthase activity in vivo
S84A/S85A
-
inactive mutant enzyme
S84C
-
mutation abolishes thymidylate synthase activity in vivo
S84Y
-
the KM-value for dUMP is 1.9fold higher than the wild-type value, the turnover-number is 1.6fold lower than the wild-type value
Y87F
-
the KM-value for dUMP is 1.8fold lower than the wild-type value, the turnover-number is nearly identical to the wild-type value
H69E
-
fails to complement the Escherichia coli chi2913 cells
I65M
-
no impaired enzyme activity, encodes proteins supporting the growth of Escherichia coli chi2913 strain
K165A
-
fails to complement the Escherichia coli chi2913 cells
L175M
-
no impaired enzyme activity, encodes proteins supporting the growth of Escherichia coli chi2913 strain
R168A
-
fails to complement the Escherichia coli chi2913 cells
R95A
-
fails to complement the Escherichia coli chi2913 cells
R95D
-
fails to complement the Escherichia coli chi2913 cells
R95K
-
supports growth of Escherichia coli chi2913 cells
S105E
-
fails to complement the Escherichia coli chi2913 cells
Y108F
-
complemens the growth of Escherichia coli chi2913 cells
I65M/L175M
-
produces active ThyX enzyme
-
H177K
Paramecium bursaria Chlorella virus-1
-
does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, 9.5% oxidation activity
H177Q
Paramecium bursaria Chlorella virus-1
-
confers thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, 31% oxidation activity
H53K
Paramecium bursaria Chlorella virus-1
-
does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, produces insoluble protein
H53Q
Paramecium bursaria Chlorella virus-1
-
does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, produces insoluble protein
H79K
Paramecium bursaria Chlorella virus-1
-
does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA
H79Q
Paramecium bursaria Chlorella virus-1
-
confers thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, 94% oxidation activity
R182A
Paramecium bursaria Chlorella virus-1
-
does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, does not copurify with oxidized FAD, but is able to oxidize NADPH in the presence of 0.4 mM FAD
R90A
Paramecium bursaria Chlorella virus-1
-
does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, looses 44% of its oxidation activity and shows no measurable deprotonation activity
H53D
residue H53 is involved in folate binding. Crystal structures of the H53D-FAD and H53D-FAD-dUMP complexes
S88A
mutant retains activity. Residue S88 is not required for catalysis
S88C
mutant retains activity. Residue S88 is not required for catalysis
S88W
no binding of dUMP observed
Y91F
similar to wild-type, at saturating FAD conditions dUMP binding to the protein/FAD complex leads to additional stabilization by about 7 degrees
H53D
-
residue H53 is involved in folate binding. Crystal structures of the H53D-FAD and H53D-FAD-dUMP complexes
-
S88W
-
no binding of dUMP observed
-
Y91F
-
similar to wild-type, at saturating FAD conditions dUMP binding to the protein/FAD complex leads to additional stabilization by about 7 degrees
-
I65M/L175M
-
produces active ThyX enzyme
I65M/L175M
produces active ThyX enzyme
E190G
Paramecium bursaria Chlorella virus-1
-
no detectable activity
E190G
Paramecium bursaria Chlorella virus-1
-
does not confer thymidine-independent growth to an Escherichia coli strain lacking thymidylate synthase ThyA, is capable of binding FAD at a wild-type level, but lacks detectable oxidation and deprotonation
additional information
analysis of 67 site-directed mutants and identification of the extended motif Y44X(24)H69X(25)R95HRX(87)S105XRYX(90)R199 of amino acids essential to enzyme activity. Residue H69 is the catalytic residue, S105 the nucleophile
additional information
-
analysis of 67 site-directed mutants and identification of the extended motif Y44X(24)H69X(25)R95HRX(87)S105XRYX(90)R199 of amino acids essential to enzyme activity. Residue H69 is the catalytic residue, S105 the nucleophile
additional information
-
analysis of 67 site-directed mutants and identification of the extended motif Y44X(24)H69X(25)R95HRX(87)S105XRYX(90)R199 of amino acids essential to enzyme activity. Residue H69 is the catalytic residue, S105 the nucleophile
-
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drug development
unexpected observation that NADP+ competes with both FAD and substrate for the binding site in ThyX and displaces both molecules from the active site, opens avenues for the design of tight-binding inhibitors of ThyX enzymes from a variety of organisms
drug development
-
unexpected observation that NADP+ competes with both FAD and substrate for the binding site in ThyX and displaces both molecules from the active site, opens avenues for the design of tight-binding inhibitors of ThyX enzymes from a variety of organisms
-
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
promising medical target, thyX is present in a number of pathogenic bacteria but absent in human
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low cross-reactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low crossreactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low crossreactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
-
specific and selective inhibitors for thy1 can provide highly effective tools for therapeutic intervention with low crossreactivity against mammalian thyA enzymes, EC 2.1.1.45
medicine
the unique mechanism of FDTS makes it an attractive target for antibiotic drug development
medicine
-
antibiotic target
medicine
-
thymidylate synthase as a target for antitubercular drugs
medicine
-
the unique mechanism of FDTS makes it an attractive target for antibiotic drug development
-
additional information
autoregulates its own translation, RNA stem-loop structure acts as an inhibitory regulator of translation by preventing the binding of its Shine-Dalgarno-like sequence by positioning it in the stem region, addition of Thy1 into the in vitro translation system also inhibits translation
additional information
-
autoregulates its own translation, RNA stem-loop structure acts as an inhibitory regulator of translation by preventing the binding of its Shine-Dalgarno-like sequence by positioning it in the stem region, addition of Thy1 into the in vitro translation system also inhibits translation
additional information
-
complements the Escherichia coli chi2913 strain that lacks its conventional TS activity, residues Lys165 and Arg168 play critical roles in ThyX activity, possibly by governing access to the carbon atom to be methylated of a totally buried substrate dUMP
additional information
Paramecium bursaria Chlorella virus-1
-
residues His53, Glu190, Arg90, and Arg182 are essential for TS activity
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Myllykallio, H.; Lipowski, G.; Leduc, D.; Filee, J.; Forterre, P.; Liebl, U.
An alternative flavin-dependent mechanism for thymidylate synthesis
Science
297
105-107
2002
Borreliella burgdorferi, Campylobacter jejuni, Chlamydia sp., Dictyostelium discoideum, Helicobacter pylori (Q9ZJ93), Mycobacterium tuberculosis, Pyrococcus abyssi (Q9UZ51), Pyrococcus horikoshii, Rickettsia prowazekii, Saccharolobus solfataricus, Treponema pallidum
brenda
Giladi, M.; Bitan-Banin, G.; Mevarech, M.; Ortenberg, R.
Genetic evidence for a novel thymidylate synthase in the halophilic archaeon Halobacterium salinarum and in Campylobacter jejuni
FEMS Microbiol. Lett.
216
105-109
2002
Campylobacter jejuni, Halobacterium salinarum
brenda
Montfort, W.R.
Complementing thymidylate synthase
Structure
11
607-608
2003
Dictyostelium discoideum, Thermotoga maritima (Q9WYT0)
brenda
Mathews, I.I.; Deacon, A.M.; Canaves, J.M.; McMullan, D.; Lesley, S.A.; Agarwalla, S.; Kuhn, P.
Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein
Structure
11
677-690
2003
Bacillus anthracis, Borreliella burgdorferi, Campylobacter jejuni, Chlamydia pneumoniae, Chlamydia psittaci, Chlamydia trachomatis, Clostridium botulinum, Clostridioides difficile, Clostridium perfringens, Corynebacterium diphtheriae, Dictyostelium discoideum, Ehrlichia chaffeensis, Helicobacter pylori, Helicobacter pylori (Q9ZJ93), Mycobacterium tuberculosis, Mycobacterium avium, Mycobacterium tuberculosis variant bovis, Mycobacterium leprae, Rhodococcus sp., Rickettsia conorii, Rickettsia prowazekii, Treponema denticola, Treponema pallidum, Thermotoga maritima (Q9WYT0), Thermotoga maritima DSM 3109 (Q9WYT0)
brenda
Leduc, D.; Graziani, S.; Meslet-Cladiere, L.; Sodolescu, A.; Liebl, U.; Myllykallio, H.
Two distinct pathways for thymidylate (dTMP) synthesis in (hyper)thermophilic bacteria and archaea
Biochem. Soc. Trans.
32
231-235
2004
Aeropyrum pernix, Aquifex aeolicus, no activity in Methanocaldococcus jannaschii, Pyrobaculum aerophilum, Pyrococcus abyssi, Pyrococcus furiosus, Pyrococcus horikoshii, Saccharolobus solfataricus, Thermoplasma acidophilum, Thermoplasma volcanium, Thermotoga maritima, no activity in Archaeoglobus fulgidus, no activity in Methanopyrus kandleri, no activity in Methanothermobacter thermoautotrophicus, Sulfurisphaera tokodaii, no activity in Methanopyrus kandleri AV19
brenda
Agrawal, N.; Lesley, S.A.; Kuhn, P.; Kohen, A.
Mechanistic studies of a flavin-dependent thymidylate synthase
Biochemistry
43
10295-10301
2004
Thermotoga maritima (Q9WYT0), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9WYT0)
brenda
Gattis, S.G.; Palfey, B.A.
Direct observation of the participation of flavin in product formation by thyX-encoded thymidylate synthase
J. Am. Chem. Soc.
127
832-833
2005
Campylobacter jejuni
brenda
Liu, X.Q.; Yang, J.
Bacterial thymidylate synthase with intein, group II Intron, and distinctive ThyX motifs
J. Bacteriol.
186
6316-6319
2004
Trichodesmium erythraeum
brenda
Graziani, S.; Xia, Y.; Gurnon, J.R.; Van Etten, J.L.; Leduc, D.; Skouloubris, S.; Myllykallio, H.; Liebl, U.
Functional analysis of FAD-dependent thymidylate synthase ThyX from Paramecium bursaria Chlorella virus-1
J. Biol. Chem.
279
54340-54347
2004
Paramecium bursaria Chlorella virus-1
brenda
Leduc, D.; Graziani, S.; Lipowski, G.; Marchand, C.; Le Marechal, P.; Liebl, U.; Myllykallio, H.
Functional evidence for active site location of tetrameric thymidylate synthase X at the interphase of three monomers
Proc. Natl. Acad. Sci. USA
101
7252-7257
2004
Helicobacter pylori
brenda
Chernyshev, A.; Fleischmann, T.; Kohen, A.
Thymidyl biosynthesis enzymes as antibiotic targets
Appl. Microbiol. Biotechnol.
74
282-289
2007
Bacillus anthracis, Chlamydia trachomatis, Clostridium botulinum, Helicobacter pylori, Mycobacterium leprae, no activity in Homo sapiens, Pyrococcus furiosus, Rickettsia sp., Thermotoga maritima, Paramecium bursaria Chlorella virus-1, Treponema palladium, Mycobacterium tuberculosis (P9WG57), Mycobacterium tuberculosis H37Rv (P9WG57)
brenda
Kanai, A.; Sato, A.; Imoto, J.; Tomita, M.
Archaeal Pyrococcus furiosus thymidylate synthase 1 is an RNA-binding protein
Biochem. J.
393
373-379
2006
Pyrococcus furiosus (Q8U3C9), Pyrococcus furiosus
brenda
Mason, A.; Agrawal, N.; Washington, M.T.; Lesley, S.A.; Kohen, A.
A lag-phase in the reduction of flavin dependent thymidylate synthase (FDTS) revealed a mechanistic missing link
Chem. Commun. (Camb. )
16
1781-1783
2006
Thermotoga maritima
brenda
Graziani, S.; Bernauer, J.; Skouloubris, S.; Graille, M.; Zhou, C.Z.; Marchand, C.; Decottignies, P.; van Tilbeurgh, H.; Myllykallio, H.; Liebl, U.
Catalytic mechanism and structure of viral flavin-dependent thymidylate synthase ThyX
J. Biol. Chem.
281
24048-24057
2006
Paramecium bursaria Chlorella virus-1
brenda
Sampathkumar, P.; Turley, S.; Ulmer, J.E.; Rhie, H.G.; Sibley, C.H.; Hol, W.G.
Structure of the Mycobacterium tuberculosis flavin dependent thymidylate synthase (MtbThyX) at 2.0A resolution
J. Mol. Biol.
352
1091-1104
2005
Mycobacterium tuberculosis
brenda
Sampathkumar, P.; Turley, S.; Sibley, C.H.; Hol, W.G.
NADP+ expels both the co-factor and a substrate analog from the Mycobacterium tuberculosis ThyX active site: opportunities for anti-bacterial drug design
J. Mol. Biol.
360
1-6
2006
Mycobacterium tuberculosis (P9WG57), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WG57)
brenda
Esra Onen, F.; Boum, Y.; Jacquement, C.; Spanedda, M.V.; Jaber, N.; Scherman, D.; Myllykallio, H.; Herscovici, J.
Design, synthesis and evaluation of potent thymidylate synthase X inhibitors
Bioorg. Med. Chem. Lett.
18
3628-3631
2008
Paramecium bursaria Chlorella virus 1 (O41156)
brenda
Chernyshev, A.; Fleischmann, T.; Koehn, E.M.; Lesley, S.A.; Kohen, A.
The relationships between oxidase and synthase activities of flavin dependent thymidylate synthase (FDTS)
Chem. Commun. (Camb. )
27
2861-2863
2007
Thermotoga maritima
brenda
Leduc, D.; Escartin, F.; Nijhout, H.F.; Reed, M.C.; Liebl, U.; Skouloubris, S.; Myllykallio, H.
Flavin-dependent thymidylate synthase ThyX activity: implications for the folate cycle in bacteria
J. Bacteriol.
189
8537-8545
2007
Rhodobacter capsulatus, Rhodobacter capsulatus MT1131
brenda
Hunter, J.H.; Gujjar, R.; Pang, C.K.; Rathod, P.K.
Kinetics and ligand-binding preferences of Mycobacterium tuberculosis thymidylate synthases, ThyA and ThyX
PLoS ONE
3
e2237
2008
Mycobacterium tuberculosis
brenda
Wang, Z.; Chernyshev, A.; Koehn, E.M.; Manuel, T.D.; Lesley, S.A.; Kohen, A.
Oxidase activity of a flavin-dependent thymidylate synthase
FEBS J.
276
2801-2810
2009
Thermotoga maritima (Q9WYT0)
brenda
Ulmer, J.E.; Boum, Y.; Thouvenel, C.D.; Myllykallio, H.; Sibley, C.H.
Functional analysis of the Mycobacterium tuberculosis FAD-dependent thymidylate synthase, ThyX, reveals new amino acid residues contributing to an extended ThyX motif
J. Bacteriol.
190
2056-2064
2008
Mycobacterium tuberculosis (P9WG57), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WG57)
brenda
Koehn, E.M.; Fleischmann, T.; Conrad, J.A.; Palfey, B.A.; Lesley, S.A.; Mathews, I.I.; Kohen, A.
An unusual mechanism of thymidylate biosynthesis in organisms containing the thyX gene
Nature
458
919-923
2009
Thermotoga maritima (Q9WYT0)
brenda
Escartin, F.; Skouloubris, S.; Liebl, U.; Myllykallio, H.
Flavin-dependent thymidylate synthase X limits chromosomal DNA replication
Proc. Natl. Acad. Sci. USA
105
9948-9952
2008
Helicobacter pylori, Paramecium bursaria Chlorella virus 1
brenda
Kan, S.C.; Liu, J.S.; Hu, H.Y.; Chang, C.M.; Lin, W.D.; Wang, W.C.; Hsu, W.H.
Biochemical characterization of two thymidylate synthases in Corynebacterium glutamicum NCHU 87078
Biochim. Biophys. Acta
1804
1751-1759
2010
no activity in Corynebacterium glutamicum strain NCHU 87078
brenda
Mishanina, T.V.; Koehn, E.M.; Conrad, J.A.; Palfey, B.A.; Lesley, S.A.; Kohen, A.
Trapping of an intermediate in the reaction catalyzed by flavin-dependent thymidylate synthase
J. Am. Chem. Soc.
134
4442-4448
2012
Thermotoga maritima (Q9WYT0), Thermotoga maritima ATCC 43589 (Q9WYT0)
brenda
Zhang, X.; Zhang, J.; Guo, G.; Mao, X.; Hu, Y.; Zou, Q.
Crystal structure of a flavin-dependent thymidylate synthase from Helicobacter pylori strain 26695
Protein Pept. Lett.
19
1225-1230
2012
Helicobacter pylori
brenda
Wang, K.; Wang, Q.; Chen, J.; Chen, L.; Jiang, H.; Shen, X.
Crystal structure and enzymatic characterization of thymidylate synthase X from Helicobacter pylori strain SS1
Protein Sci.
20
1398-1410
2011
Helicobacter pylori (Q5UVJ4), Helicobacter pylori, Helicobacter pylori SS1 (Q5UVJ4)
brenda
Becker, H.F.; Djaout, K.; Lamarre, I.; Ulmer, J.E.; Schaming, D.; Balland, V.; Liebl, U.; Myllykallio, H.; Vos, M.H.
Substrate interaction dynamics and oxygen control in the active site of thymidylate synthase ThyX
Biochem. J.
459
37-45
2014
Paramecium bursaria Chlorella virus 1 (O41156)
brenda
Alexandrova, L.A.; Chekhov, V.O.; Shmalenyuk, E.R.; Kochetkov, S.N.; El-Asrar, R.A.; Herdewijn, P.
Synthesis and evaluation of C-5 modified 2-deoxyuridine monophosphates as inhibitors of M. tuberculosis thymidylate synthase
Bioorg. Med. Chem.
23
7131-7137
2015
Mycobacterium tuberculosis
brenda
Mishanina, T.V.; Corcoran, J.M.; Kohen, A.
Substrate activation in flavin-dependent thymidylate synthase
J. Am. Chem. Soc.
136
10597-10600
2014
Thermotoga maritima (Q9WYT0), Thermotoga maritima ATCC 43589 (Q9WYT0)
brenda
Mathews, I.I.
Flavin-dependent thymidylate synthase as a drug target for deadly microbes: mutational study and a strategy for inhibitor design
J. Bioterror Biodef.
Suppl 12
004
2013
Thermotoga maritima (Q9WYT0), Thermotoga maritima ATCC 43589 (Q9WYT0)
brenda
Ogawa, A.; Sampei, G.; Kawai, G.
Crystal structure of the flavin-dependent thymidylate synthase Thy1 from Thermus thermophilus with an extra C-terminal domain
Acta Crystallogr. Sect. F
75
450-455
2019
Thermus thermophilus (Q5SJB8), Thermus thermophilus, Thermus thermophilus DSM 579 (Q5SJB8)
brenda
Alexandrova, L.A.; Chekhov, V.O.; Shmalenyuk, E.R.; Kochetkov, S.N.; El-Asrar, R.A.; Herdewijn, P.
Synthesis and evaluation of C-5 modified 2-deoxyuridine monophosphates as inhibitors of M. tuberculosis thymidylate synthase
Bioorg. Med. Chem.
23
7131-7137
2015
Mycobacterium tuberculosis (P9WG57), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 (P9WG57)
brenda
Modranka, J.; Li, J.; Parchina, A.; Vanmeert, M.; Dumbre, S.; Salman, M.; Myllykallio, H.; Becker, H.F.; Vanhoutte, R.; Margamuljana, L.; Nguyen, H.; Abu El-Asrar, R.; Rozenski, J.; Herdewijn, P.; De Jonghe, S.; Lescrinier, E.
Synthesis and structure-activity relationship studies of benzo[b][1,4]oxazin-3(4H)-one analogues as inhibitors of mycobacterial thymidylate synthase X
ChemMedChem
14
645-662
2019
Mycobacterium tuberculosis (P9WG57), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WG57)
brenda
Krumova, S.; Todinova, S.; Tileva, M.; Bouzhir-Sima, L.; Vos, M.H.; Liebl, U.; Taneva, S.G.
Thermal stability and binding energetics of thymidylate synthase ThyX
Int. J. Biol. Macromol.
91
560-567
2016
Paramecium bursaria Chlorella virus 1 (O41156), Paramecium bursaria Chlorella virus 1, Thermotoga maritima (Q9WYT0), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9WYT0)
brenda
Luciani, R.; Saxena, P.; Surade, S.; Santucci, M.; Venturelli, A.; Borsari, C.; Marverti, G.; Ponterini, G.; Ferrari, S.; Blundell, T.L.; Costi, M.P.
Virtual screening and X-ray crystallography identify non-substrate analog inhibitors of flavin-dependent thymidylate synthase
J. Med. Chem.
59
9269-9275
2016
Thermotoga maritima (Q9WYT0), Thermotoga maritima DSM 3109 (Q9WYT0)
brenda
Skouloubris, S.; Djaout, K.; Lamarre, I.; Lambry, J.C.; Anger, K.; Briffotaux, J.; Liebl, U.; de Reuse, H.; Myllykallio, H.
Targeting of Helicobacter pylori thymidylate synthase ThyX by non-mitotoxic hydroxy-naphthoquinones
Open Biology
5
150015
2015
Helicobacter pylori (O26061), Helicobacter pylori, Helicobacter pylori 26695 (O26061)
brenda