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Information on EC 2.7.4.9 - dTMP kinase
for references in articles please use BRENDA:EC2.7.4.9
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.4 Phosphotransferases with a phosphate group as acceptor
2.7.4.9 dTMP kinase
The enzyme appears in viruses and cellular organisms
showSynonyms
tmpk, dtmp kinase, tmpkmt, thymidine monophosphate kinase, tmp kinase, pftmk, dtmpk, thymidylate monophosphate kinase, s. aureus thymidylate kinase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cdc8
-
Cdc8 exhibits both deoxythymidine monophosphate and diphosphate kinase activities
deoxythymidine 5'-monophosphate kinase
-
-
-
-
deoxythymidine monophosphate kinase
dTMP kinase
dTMPK
-
-
-
-
kinase, thymidine monophosphate (phosphorylating)
-
-
-
-
kinase, thymidylate (phosphorylating)
-
-
-
-
thymidine 5'-monophosphate kinase
-
-
-
-
thymidine monophosphate kinase
thymidylate kinase
thymidylate monophosphate kinase
-
-
-
-
thymidylic acid kinase
-
-
-
-
thymidylic kinase
-
-
-
-
TMK
TMP kinase
TMPK
TMPKmt
TTHA1607
dTMP kinase
-
-
-
-
thymidine monophosphate kinase
-
-
-
-
thymidylate kinase
-
-
-
-
TMK
-
-
-
-
TMP kinase
-
-
-
-
TMPK
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + dTMP = ADP + dTDP
addition of substrates to the enzyme is random, while release of the products is ordered
-
ATP + dTMP = ADP + dTDP
binding of D-dTMP is through a network of hydrogen bonds to the pyrimidine ring involving residues R70, S97, and Q101, and the base is stacked by residue Y66. The phosphate group is tightly coordinated by residues R34, D91, and R92
ATP + dTMP = ADP + dTDP
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
Phosphorylation
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
pyrimidine deoxyribonucleotide phosphorylation, pyrimidine deoxyribonucleotides biosynthesis from CTP, pyrimidine deoxyribonucleotides de novo biosynthesis I, pyrimidine deoxyribonucleotides de novo biosynthesis II, pyrimidine deoxyribonucleotides de novo biosynthesis III, pyrimidine deoxyribonucleotides de novo biosynthesis IV, superpathway of pyrimidine deoxyribonucleotides de novo biosynthesis (E. coli)
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SYSTEMATIC NAME
IUBMB Comments
ATP:dTMP phosphotransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9014-43-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (E)-5-(2-bromovinyl)-deoxyuridine monophosphate
?
Substrates: 5% of the TMP efficiency
Products: -
Products: -
?
ATP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-monophosphate
ADP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-diphosphate
ATP + 2',3'-dideoxy-2',3'-didehydrothymidine 5'-monophosphate
ADP + 2',3'-dideoxy-2',3'-didehydrothymidine 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + 3'-amino-3'-deoxythymidine 5'-monophosphate
ADP + 3'-amino-3'-deoxythymidine 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + 3'-azido-2',3'-dideoxythymidine monophosphate
ADP + 3'-azido-2',3'-dideoxythymidine diphosphate
Substrates: -
Products: -
Products: -
?
ATP + 3'-azido-3'-deoxythymidine 5'-monophosphate
ADP + 3'-azido-3'-deoxythymidine 5'-diphosphate
ATP + 3'-azido-3'-deoxythymidine monophosphate
ADP + 3'-azido-3'-deoxythymidine diphosphate
ATP + 3'-fluoro-3'-deoxythymidine 5'-monophosphate
ADP + 3'-fluoro-3'-deoxythymidine 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + 5-bromo-2'-deoxyuridine 5'-monophosphate
ADP + 5-bromo-2'-deoxyuridine 5'-diphosphate
ATP + 5-fluorodeoxyuridine 5'-monophosphate
ADP + 5-fluorodeoxyuridine 5'-diphosphate
Substrates: poor substrate
Products: -
Products: -
?
ATP + 5-iodo-2'-dUMP
ADP + 5-iodo-2'-dUDP
-
Substrates: 60% of the maximal activity with dTMP
Products: -
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?
ATP + 5-iodo-dUMP
ADP + 5-iodo-dUDP
-
Substrates: 34% of the activity with dTMP
Products: -
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?
ATP + AMP
ADP + ADP
Substrates: 3.7% of the activity with dTMP
Products: -
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?
ATP + D-2'-fluoroarabinosyl-5-methyldeoxyuridine 5'-monophosphate
ADP + D-2'-fluoroarabinosyl-5-methyldeoxyuridine 5'-diphosphate
Substrates: 172% of the activity with dTMP
Products: -
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?
ATP + dAMP
ADP + dADP
Substrates: 2.7% of the activity with dTMP
Products: -
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?
ATP + dGMP
?
Substrates: 5% of the TMP efficiency
Products: -
Products: -
?
ATP + dIMP
ADP + dIDP
-
Substrates: 15% of the activity with dTMP
Products: -
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?
ATP + GMP
ADP + GDP
-
Substrates: 1.5% of the activity with dTMP
Products: -
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?
ATP + IMP
ADP + IDP
Substrates: 1% of the activity with dTMP
Products: -
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?
ATP + L-2'-fluoroarabinosyl-5-methyldeoxyuridine 5'-monophosphate
ADP + L-2'-fluoroarabinosyl-5-methyldeoxyuridine 5'-diphosphate
Substrates: poor substrate
Products: -
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?
ATP + N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-thymine
ADP + ?
Substrates: -
Products: -
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?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
ADP + ?
Substrates: -
Products: -
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?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-fluorouracil
ADP + ?
Substrates: -
Products: -
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?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-thymine
ADP + ?
Substrates: -
Products: -
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?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-uracil
ADP + ?
Substrates: -
Products: -
Products: -
?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-bromouracil
ADP + ?
Substrates: -
Products: -
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?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-chlorouracil
ADP + ?
Substrates: -
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?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-fluorouracil
ADP + ?
Substrates: -
Products: -
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?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-thymine
ADP + ?
Substrates: -
Products: -
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?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-uracil
ADP + ?
Substrates: -
Products: -
Products: -
?
dTMP + ATP
dTDP + ADP
-
Substrates: TMPK catalyzes the conversion of dTMP to dTDP, using ATP as its preferred phosphoryl donor. Part of the biosynthetic pathway for deoxythymidine triphosphate (dTTP).
Products: -
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?
thymidine monophosphate + ATP
thymidine diphosphate + ADP
-
Substrates: Thymidylate kinase (TMK) (E.C. 2.7.4.9) is a member of the NMP kinase family and catalyzes the phosphoryl transfer from the preferred phosphoryl donor, ATP, to thymidine monophosphate (TMP), yielding thymidine diphosphate (TDP). The TMK reaction is positioned at the junction of the de novo and salvage pathway of thymidine triphosphate (dTTP) synthesis, with TMK being the last specific enzyme for dTTP synthesis.
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?
ATP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-monophosphate
ADP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-monophosphate
ADP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-diphosphate
Substrates: -
Products: -
Products: -
?
ATP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-monophosphate
ADP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + 3'-azido-3'-deoxythymidine 5'-monophosphate
ADP + 3'-azido-3'-deoxythymidine 5'-diphosphate
-
Substrates: good substrate
Products: -
Products: -
?
ATP + 3'-azido-3'-deoxythymidine 5'-monophosphate
ADP + 3'-azido-3'-deoxythymidine 5'-diphosphate
Substrates: -
Products: -
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?
ATP + 3'-azido-3'-deoxythymidine 5'-monophosphate
ADP + 3'-azido-3'-deoxythymidine 5'-diphosphate
-
Substrates: i.e. AZT
Products: -
Products: -
?
ATP + 3'-azido-3'-deoxythymidine 5'-monophosphate
ADP + 3'-azido-3'-deoxythymidine 5'-diphosphate
-
Substrates: no activity
Products: -
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?
ATP + 3'-azido-3'-deoxythymidine 5'-monophosphate
ADP + 3'-azido-3'-deoxythymidine 5'-diphosphate
-
Substrates: Vmax is 100 times lower than with dTMP
Products: -
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?
ATP + 3'-azido-3'-deoxythymidine monophosphate
ADP + 3'-azido-3'-deoxythymidine diphosphate
Substrates: -
Products: -
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?
ATP + 3'-azido-3'-deoxythymidine monophosphate
ADP + 3'-azido-3'-deoxythymidine diphosphate
Substrates: -
Products: -
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?
ATP + 3'-azido-3'-deoxythymidine monophosphate
ADP + 3'-azido-3'-deoxythymidine diphosphate
-
Substrates: -
Products: -
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?
ATP + 3'-azido-3'-deoxythymidine monophosphate
ADP + 3'-azido-3'-deoxythymidine diphosphate
Substrates: -
Products: -
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?
ATP + 5-bromo-2'-deoxyuridine 5'-monophosphate
ADP + 5-bromo-2'-deoxyuridine 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + 5-bromo-2'-deoxyuridine 5'-monophosphate
ADP + 5-bromo-2'-deoxyuridine 5'-diphosphate
-
Substrates: -
Products: -
Products: -
?
ATP + dCMP
ADP + dCDP
Substrates: 1% of the activity with dTMP
Products: -
Products: -
?
ATP + dGMP
ADP + dGDP
-
Substrates: 86% of the activity with dTMP
Products: -
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?
ATP + dGMP
ADP + dGDP
-
Substrates: dGMP is unable to displace TMP from its binding site
Products: -
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r
ATP + dTMP
ADP + dTDP
-
Substrates: involved in dTTP metabolism, essential for cell proliferation
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
-
Substrates: involved in TTP metabolism, required for the activation of clinically relevant thymidine analogs such as anti-HIV and anti-cancer prodrugs
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
-
Substrates: -
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
Substrates: involved in dTTP metabolism, essential for cell proliferation
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
Substrates: involved in dTTP metabolism, essential for cell proliferation
Products: -
Products: -
r
ATP + dTMP
ADP + dTDP
-
Substrates: involved in dTTP metabolism, essential for cell proliferation
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
-
Substrates: -
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
-
Substrates: reaction in both the de novo and salvage pathways of dTTP synthesis
Products: -
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?
ATP + dTMP
ADP + dTDP
Substrates: specificity to the natural substrates ATP and dTMP
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
Substrates: specificity to the natural substrates ATP and dTMP
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
Substrates: -
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
Substrates: -
Products: -
Products: -
?
ATP + dUMP
ADP + dUDP
Substrates: 10.7% of the activity with dTMP
Products: -
Products: -
?
ATP + dUMP
ADP + dUDP
-
Substrates: at 15% of the activity with dTMP
Products: -
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?
ATP + dUMP
ADP + dUDP
Escherichia coli B / ATCC 11303
-
Substrates: at 15% of the activity with dTMP
Products: -
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?
ATP + dUMP
ADP + dUDP
-
Substrates: 43% of the activity with dTMP
Products: -
Products: -
?
ATP + dUMP
ADP + dUDP
-
Substrates: 31% of the activity with dTMP
Products: -
Products: -
?
ATP + dUMP
ADP + dUDP
-
Substrates: 15% of the activity with dTMP
Products: -
Products: -
?
ATP + dUMP
ADP + dUDP
Substrates: -
Products: 12% of the activity with dTMP
Products: 12% of the activity with dTMP
?
ATP + dUMP
ADP + dUDP
Substrates: -
Products: 12% of the activity with dTMP
Products: 12% of the activity with dTMP
?
ATP + TMP
ADP + TDP
Substrates: involved in TTP metabolism
Products: -
Products: -
?
ATP + TMP
ADP + TDP
-
Substrates: TMP is able to partially displace dGMP from the binding site
Products: -
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r
CTP + dTMP
CDP + dTDP
-
Substrates: about 30% of the activity with ATP
Products: -
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?
CTP + dTMP
CDP + dTDP
Escherichia coli B / ATCC 11303
-
Substrates: about 30% of the activity with ATP
Products: -
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?
CTP + dTMP
CDP + dTDP
-
Substrates: 26% of the activity with ATP
Products: -
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?
CTP + dTMP
CDP + dTDP
-
Substrates: 20% of the activity with ATP
Products: -
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?
dATP + dTMP
dADP + dTDP
Substrates: dATP, 83% of the activity with ATP
Products: -
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?
dATP + dTMP
dADP + dTDP
-
Substrates: about 80% of the activity with ATP
Products: -
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?
dATP + dTMP
dADP + dTDP
Escherichia coli B / ATCC 11303
-
Substrates: about 80% of the activity with ATP
Products: -
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?
dATP + dTMP
dADP + dTDP
-
Substrates: 99% of the activity with ATP
Products: -
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?
dATP + dTMP
dADP + dTDP
-
Substrates: 70.1% of the activity with ATP
Products: -
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r
dATP + dTMP
dADP + dTDP
-
Substrates: dATP, 64% of the activity with ATP
Products: -
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?
dATP + dTMP
dADP + dTDP
-
Substrates: 92% of the activity with ATP
Products: -
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?
dATP + dTMP
dADP + dTDP
-
Substrates: 80% of the activity with ATP
Products: -
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?
dATP + dTMP
dADP + dTDP
Substrates: 26.9% of the activity with ATP
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?
dATP + dTMP
dADP + dTDP
Substrates: 26.9% of the activity with ATP
Products: -
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?
dCTP + dTMP
dCDP + dTDP
-
Substrates: about 20% of the activity with ATP
Products: -
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?
dCTP + dTMP
dCDP + dTDP
-
Substrates: 45% of the activity with ATP
Products: -
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?
dCTP + dTMP
dCDP + dTDP
-
Substrates: 49% of the activity ATP
Products: -
Products: -
?
dGTP + dTMP
dGDP + dTDP
-
Substrates: about 10% of maximal activity with ATP
Products: -
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?
dGTP + dTMP
dGDP + dTDP
Escherichia coli B / ATCC 11303
-
Substrates: about 10% of maximal activity with ATP
Products: -
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?
dGTP + dTMP
dGDP + dTDP
-
Substrates: 42% of the activity with ATP
Products: -
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?
dGTP + dTMP
dGDP + dTDP
-
Substrates: 59% of the activity with ATP
Products: -
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?
dGTP + dTMP
dGDP + dTDP
-
Substrates: 42% of the activity with ATP
Products: -
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?
dTTP + dTMP
dTDP
-
Substrates: about 3% of the activity with ATP
Products: -
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?
GTP + dTMP
GDP + dTDP
-
Substrates: 35% of the activity with ATP
Products: -
Products: -
?
ITP + dTMP
IDP + dTDP
-
Substrates: 2% of the activity with ATP and TMP
Products: -
Products: -
?
ITP + dTMP
IDP + dTDP
-
Substrates: 1% of the activity with ATP and TMP
Products: -
Products: -
?
UTP + dTMP
UDP + dTDP
-
Substrates: 13% of the activity with ATP and TMP
Products: -
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?
UTP + dTMP
UDP + dTDP
-
Substrates: 36% of the activity with ATP
Products: -
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?
UTP + dTMP
UDP + dTDP
-
Substrates: 2.5% of the activity with ATP and TMP
Products: -
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?
additional information
?
-
Substrates: no substrate: 3'-azidothymidine 5'-monophosphate
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?
additional information
?
-
-
Substrates: no substrate: 3'-azidothymidine 5'-monophosphate
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?
additional information
?
-
-
Substrates: multifunctional enzyme which also phosphorylates pyrimidine nucleosides, pyrimidine nucleoside monophosphates, and several nucleoside analogues
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?
additional information
?
-
-
Substrates: key enzyme in nucleotide synthesis
Products: -
Products: -
?
additional information
?
-
Herpes simplex virus
-
Substrates: multifunctional enzyme which also phosphorylates pyrimidine nucleosides, pyrimidine nucleoside monophosphates, and several nucleoside analogues
Products: -
Products: -
?
additional information
?
-
Substrates: direct correlation between the rate of phosphorylation of an NMP and its ability to induce a closing of the enzymes phosphate-binding loop
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Products: -
?
additional information
?
-
-
Substrates: direct correlation between the rate of phosphorylation of an NMP and its ability to induce a closing of the enzymes phosphate-binding loop
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with cidofovir, N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-uracil, N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-5-chlorouracil, N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-5-bromouracil, N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-5-fluoro-uracil, and N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-thymine
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with cidofovir, N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-uracil, N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-5-chlorouracil, N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-5-bromouracil, N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-5-fluoro-uracil, and N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-thymine
Products: -
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?
additional information
?
-
-
Substrates: thymidine/thymidylate multifunctional kinase
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?
additional information
?
-
-
Substrates: Cdc8 does not phosphorylate dAMP, dGMP and dCMP
Products: -
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?
additional information
?
-
-
Substrates: poxvirus thymidylate kinase can also accept bulky analogues such as dGMP or 5-bromo-vinyl-dUMP as substrates
Products: -
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?
additional information
?
-
-
Substrates: sequential ordered bi-bi reaction mechanism. The enzyme additionally shows nucleoside-diphosphate kinase activity, reaction of EC 2.7.4.6, using dTDP as a substrate to produce dTTP
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?
additional information
?
-
Substrates: maximal activity is achieved at equimolar concentrations of ATP and Mg2+
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?
additional information
?
-
Substrates: maximal activity is achieved at equimolar concentrations of ATP and Mg2+
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?
additional information
?
-
-
Substrates: key enzyme in nucleotide synthesis
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dTMP + ATP
dTDP + ADP
-
Substrates: TMPK catalyzes the conversion of dTMP to dTDP, using ATP as its preferred phosphoryl donor. Part of the biosynthetic pathway for deoxythymidine triphosphate (dTTP).
Products: -
Products: -
?
thymidine monophosphate + ATP
thymidine diphosphate + ADP
-
Substrates: Thymidylate kinase (TMK) (E.C. 2.7.4.9) is a member of the NMP kinase family and catalyzes the phosphoryl transfer from the preferred phosphoryl donor, ATP, to thymidine monophosphate (TMP), yielding thymidine diphosphate (TDP). The TMK reaction is positioned at the junction of the de novo and salvage pathway of thymidine triphosphate (dTTP) synthesis, with TMK being the last specific enzyme for dTTP synthesis.
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
-
Substrates: involved in dTTP metabolism, essential for cell proliferation
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
-
Substrates: involved in TTP metabolism, required for the activation of clinically relevant thymidine analogs such as anti-HIV and anti-cancer prodrugs
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
Substrates: involved in dTTP metabolism, essential for cell proliferation
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
Substrates: involved in dTTP metabolism, essential for cell proliferation
Products: -
Products: -
r
ATP + dTMP
ADP + dTDP
-
Substrates: involved in dTTP metabolism, essential for cell proliferation
Products: -
Products: -
?
ATP + dTMP
ADP + dTDP
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Substrates: reaction in both the de novo and salvage pathways of dTTP synthesis
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ATP + TMP
ADP + TDP
Substrates: involved in TTP metabolism
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additional information
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Substrates: multifunctional enzyme which also phosphorylates pyrimidine nucleosides, pyrimidine nucleoside monophosphates, and several nucleoside analogues
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additional information
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Substrates: key enzyme in nucleotide synthesis
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additional information
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Herpes simplex virus
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Substrates: multifunctional enzyme which also phosphorylates pyrimidine nucleosides, pyrimidine nucleoside monophosphates, and several nucleoside analogues
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additional information
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Substrates: key enzyme in nucleotide synthesis
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Ni2+
additional information
presence of a divalent cation is required. In presence of Ca2+, Cu2+, less than 10% of maximum activity, no activity with Zn2+
Mg2+
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absolute requirement for divalent cation. When Mg2+ is equal to ATP, the rate of dTMP kinase reaction is maximal
Mg2+
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requirement of a Mg2+:ATP ratio greater than 1.0 and for optimal activity there is a requirement of an additional 2-3 mM Mg2+ above the concentration of ATP
Mg2+
-
required, concentration range for maximal activity is From Mg:ATP ratios of 1 to 3 with an optimum around 1.3 to 1.5
Mg2+
bound to enzyme, displacement of Mg2+ might be responsible for inhibitory effect of the enzyme inhibitors
Mg2+
bound to enzyme, displacement of Mg2+ is responsible for inhibitory effect of 3-azido-3-deoxythymidine 5'-monophosphate
Mg2+
bound to enzyme, displacement of Mg2+ might be responsible for inhibitory effect of the enzyme inhibitors
Mg2+
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activity is maximal in presence of 2-5 mM ATP and 10 mM MgCl2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+/-)(Z)-5-acetamido-1-(4-(thymin-1-yl)but-2-enyl)-5,6-dihydro-1H-imidazo[4,5,1-ij]quinolin-2(4H)-one
-
-
(+/-)(Z)-5-amino-1-(4-(thymin-1-yl)but-2-enyl)-5,6-dihydro-1H-imidazo[4,5,1-ij]quinolin-2(4H)-one
-
-
(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
(3E)-4-[4-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]but-3-enoic acid
(4E)-1-(4-hydroxy-3-methoxyphenyl)dec-4-en-3-one
i.e. [6]-shogaol, isolated from Zingiber officinale
(R)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
(S)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
(S)-1-(1-(3-(3,5-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
(S)-1-(1-(3-(3-chloro-4-methylphenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
(S)-1-(1-(3-(3-chloro-5-fluorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
(S)-2-(3-bromophenoxy)-4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)methyl)benzoic acid
(S)-2-(3-fluorophenoxy)-4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)methyl)benzoic acid
(S)-4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-piperidin-1-yl)methyl)-2-(m-tolyloxy)benzoic acid
(Z)-1-(4-(thymin-1-yl)but-2-enyl)-1H-benzo[c,d]indol-2(1H)one
-
(Z)-1-(4-(thymin-1-yl)but-2-enyl)-5,6-dihydro-1H-imidazo[4,5,1-ij]quinolin-2(4H)-one
-
-
(Z)-2-(4-(5-bromouracil-1-yl)but-2-enyl)-1H-benzo[d,e] isoquinoline-1,3(2H)-dione
-
(Z)-2-(4-(thymin-1-yl)but-2-enyl)-1H-benzo[d,e]isoquinoline-1,3(2H)-dione
-
(Z)-2-(4-(thymin-1-yl)but-2-enyl)-2,3-dihydro-1H-benzo-[d,e]isoquinolin-1-one
-
(Z)-2-(4-(thymin-1-yl)but-2-enyl)-2H-naphtho[1,8 cd]isothiazole-1,1-dioxide
-
(Z)-2-(4-(thymin-1-yl)but-2-enyl)-6-nitrobenzo[c,d]indol-2(1H)one
-
(Z)-8-acetamido-1-(4-(thymin-1-yl)but-2-enyl)-5,6-dihydro-1H-imidazo[4,5,1-ij]quinolin-2(4H)-one
-
-
(Z)-8-amino-1-(4-(thymin-1-yl)but-2-enyl)-5,6-dihydro-1H-imidazo[4,5,1-ij]quinolin-2(4H)-one
-
-
1,3-bis[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]urea
-
1,3-bis[[(2S,3R,5R)-2-methyl-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]urea
1-(((2R,3S,5S)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl)methyl)-3-(((2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl)methyl)urea
-
-
1-((2R,4S,5R)-4-hydroxy-5-(2-(methylsulfonyl)ethyl)tetrahydrofuran-2-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-((2R,4S,5R)-5-(2-(1H-tetrazol-5-yl)ethyl)-4-hydroxytetrahydrofuran-2-yl)-5-(hydroxymethyl)pyrimidine-2,4(1H,3H)-dione
-
-
1-((2R,4S,5R)-5-(2-(1H-tetrazol-5-yl)ethyl)-4-hydroxytetrahydrofuran-2-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-(1-(4-hydroxy-3-methoxyphenyl)-3-oxodecan-5-yl)-5-methylpyrimidine-2,4-(1H,3H)-dione
i.e. shogaol with thymine head group
1-(1-benzylpiperidin-4-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-(1-[[4-(3-chlorophenoxy)quinolin-2-yl]methyl]piperidin-4-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-(1-[[4-(dimethylamino)phenyl]methyl]piperidin-4-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-(3,4-dichlorophenyl)-3-[[(2R,3R,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
-
1-(3,4-dichlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
1-(3,4-dichlorophenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
comparison with inhibition of human enzyme
1-(3-amino-3-deoxy-2-O,3-N-(thiocarbonyl)-beta-D-ribofuranosyl)thymine
-
IC99: 500 microg/ml
1-(3-aminomethyl-3,5-dideoxy-2-O,6-N-(thiocarbonyl)-beta-D-ribofuranosyl)thymine
-
IC99: 100 microg/ml
1-(3-chloro-4-trifluoromethylphenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
1-(4-benzyloxyphenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
comparison with inhibition of human enzyme
1-(4-bromobenzyl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
comparison with inhibition of human enzyme
1-(4-chlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
1-(4-chlorophenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
comparison with inhibition of human enzyme
1-methyl-6-(pyrimidin-5-yl)-1H-imidazo[4,5-b]pyridin-2(3H)-one
-
1-[(1'R,4'S)-4'-((S)-2-fluoro-1-hydroxyethyl)cyclopent-2'-enyl]-1H-thymine
-
-
1-[(1R,2R,3S,4R)-2,3-dihydroxy-4-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-[(1R,2R,4R,5S)-4-(hydroxymethyl)-6-oxabicyclo[3.1.0]hex-2-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
1-[(1R,2S,3R,4R)-2,3-dihydroxy-4-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-[(1R,3S,4R)-3-hydroxy-4-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-[(1R,4S)-4-(hydroxymethyl)cyclopent-2-en-1-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-[(1S,3R)-3-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-[(2E)-4-(5,6-dimethoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)but-2-en-1-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
inhibitor identified by 3D-QSAR pharmacophore generation
1-[(2E)-4-[5,6-bis(hydroxymethyl)-2-oxobenzo[cd]indol-1(2H)-yl]but-2-en-1-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
inhibitor identified by 3D-QSAR pharmacophore generation
1-[(2S,4S,5R)-5-(aminomethyl)-4-hydroxytetrahydrofuran-2-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[(2S,4S,5R)-5-(azidomethyl)-4-hydroxytetrahydrofuran-2-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[(2Z)-(4-(5-bromouracil-1-yl)but-2-enyl)]-5,6-dihydro-1H,4H-1,2,5-thiadiazolo[4,3,2-ij]quinolin-2,2-dioxide
-
-
1-[(2Z)-4-(1,1-dioxido-2H-naphtho[1,8-cd][1,2]thiazol-2-yl)but-2-en-1-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-oxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-thioxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
1-[(4aR,5S,7R,7aS)-5-(hydroxymethyl)-2-thioxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[(Z)-(4-(thymin-1-yl)but-2-enyl)]-5,6-dihydro-1H,4H-1,2,5-thiadiazolo[4,3,2-ij]quinolin-2,2-dioxide
-
-
1-[1-(cyclohexylmethyl)piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[1-[(1-benzofuran-2-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[1-[(3,4-dichlorophenyl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[1-[(4-chlorophenyl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[1-[(4-methoxyphenyl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[1-[(7-chloro-4-phenoxyquinolin-2-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[1-[(furan-2-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[1-[(furan-3-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[1-[(isoquinolin-1-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[1-[(isoquinolin-3-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[1-[(isoquinolin-4-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[2,5-dideoxy-5-[([4-[(2-fluorophenyl)methoxy]phenyl]carbamoyl)amino]-alpha-D-erythro-pentofuranosyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[2,5-dideoxy-5-[([4-[(2-methoxyphenyl)methoxy]phenyl]carbamoyl)amino]-alpha-D-erythro-pentofuranosyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[2-ammonio-3-(4-hydroxyphenyl)propanoyl]-N-[1-(4-hydroxyphenyl)-3-oxoniopropan-2-yl]prolinamide
-
1-[2-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]ethyl]-3-phenylthiourea
-
1-[3-aminomethyl-3,5-dideoxy-2-O,6-N-(thiocarbonyl)-beta-D-ribofuranosyl]thymine
-
-
1-[4-chloro-3-(trifluoromethyl)phenyl]-3-[2-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methoxy]ethyl]thiourea
-
1-[4-chloro-3-(trifluoromethyl)phenyl]-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
1-[4-chloro-3-(trifluoromethyl)phenyl]-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]urea
-
1-[5-([[4-chloro-3-(trifluoromethyl)phenyl]carbamothioyl]amino)-2,5-dideoxy-a-D-erythro-pentofuranosyl]-5-methyl-4-thioxo-3,4-dihydropyrimidin-2(1H)-one
-
-
1-[5-[([4-[(2-chlorophenyl)methoxy]phenyl]carbamoyl)amino]-2,5-dideoxy-alpha-D-erythro-pentofuranosyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[N-[2-ammonio-3-(1H-indol-3-yl)propanoyl]tyrosyl]pyrrolidine-2-carboxylate
-
1-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]-3-(4-methoxyphenyl)thiourea
-
1-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]-3-(4-methylphenyl)thiourea
-
1-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]-3-phenylthiourea
-
1-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]-3-pyridin-3-ylthiourea
-
1-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]-3-phenylthiourea
-
2',5'-dideoxy-5'-(4-phenyl-1H-1,2,3-triazol-1-yl)-3,4-dihydrothymidine
-
-
2',5'-dideoxy-5'-([[3-(trifluoromethyl)phenyl]carbamoyl]amino)-3,4-dihydrothymidine
-
-
2-((2R,3S,5R)-3-((tert-butyldimethylsilyl)oxy)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl)-N-methylethanesulfonamide
-
-
2-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamido)acetic acid
-
2-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamido)ethanesulfonic acid
-
2-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamido)propanoic acid
-
2-(3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamido)propyl)benzoic acid
-
2-(3-bromophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
2-(3-bromophenoxy)-4-((R)-3-ethyl-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
2-(3-bromophenoxy)-4-((S)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
2-(3-bromophenoxy)-4-(R)-(2-(1-adamantane)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
2-(3-chlorophenoxy)-3-methoxy-4-[(1S)-1-[(3S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl]propyl]benzoic acid
-
2 g/ml MIC against methicillin-resistant Staphylococcus aureus. The compound exhibits a striking inverted chiral preference for binding relative to earlier compounds and also has improved physical properties and pharmacokinetics
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)-2-(tetrahydro-2H-pyran-4-yl)ethyl)benzoic acid
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1-(2H)-yl)piperidin-1-yl)butyl)benzoic acid
2-(3-chlorophenoxy)-4-((R)-2-cyclohexyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
2-(3-chlorophenoxy)-4-((R)-3-ethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
2-(3-chlorophenoxy)-4-((R)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
2-(3-chlorophenoxy)-4-((S)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
2-([1-[2-ammonio-3-(1H-indol-3-yl)propanoyl]prolyl]amino)-3-(1H-indol-3-yl)propanoate
-
2-([1-[2-ammonio-3-(1H-indol-3-yl)propanoyl]prolyl]amino)-3-(4-methylphenyl)propanoate
-
2-([1-[2-ammonio-3-(1H-indol-3-yl)propanoyl]prolyl]amino)-3-hydroxypropanoate
-
2-([1-[2-ammonio-3-(1H-indol-3-yl)propanoyl]prolyl]amino)pentanedioate
-
2-([1-[2-ammonio-3-(4-hydroxyphenyl)propanoyl]prolyl]amino)-3-(1H-indol-3-yl)propanoate
-
2-([N-[2-ammonio-3-(1H-indol-3-yl)propanoyl]tyrosyl]amino)-3-(4-hydroxyphenyl)propanoate
-
2-([N-[2-ammonio-3-(1H-indol-3-yl)propanoyl]tyrosyl]amino)-3-hydroxybutanoate
-
2-([N-[2-ammonio-3-(1H-indol-3-yl)propanoyl]tyrosyl]amino)-3-hydroxypropanoate
-
2-([N-[2-ammonio-3-(1H-indol-3-yl)propanoyl]tyrosyl]amino)-4-carboxybutanoate
-
2-([N-[2-ammonio-3-(1H-indol-3-yl)propanoyl]tyrosyl]amino)butanedioate
-
2-benzyl-3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]-pyridin-6-yl)benzamido)propanoic acid
-
2-[(4aS,5R,7R,7aR)-5-[5-(hydroxymethyl)-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl]-2,2-dioxidooctahydrocyclopenta[c][1,2,6]thiadiazin-7-yl]-N-methylethanesulfonamide
-
-
2-[([1-[2-ammonio-3-(1H-indol-3-yl)propanoyl]pyrrolidin-2-yl]methyl)amino]butanedioate
-
2-[([1-[2-ammonio-3-(4-hydroxyphenyl)propanoyl]pyrrolidin-2-yl]acetyl)amino]-3-hydroxybutanoate
-
2-[([1-[2-ammonio-3-(4-hydroxyphenyl)propanoyl]pyrrolidin-2-yl]acetyl)amino]-3-hydroxypropanoate
-
2-{[3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzoyl]amino}-4-phenylbutanoic acid
-
3'-(4-chlorophenyl-1,2,3-triazol-1-yl)-3'-deoxy-4-thio-beta-D-thymidine
-
-
3'-(4-chlorophenyl-1,2,3-triazol-1-yl)-3'-deoxy-alpha-D-thymidine
-
-
3'-([[(4-chlorophenyl)carbamothioyl]amino]methyl)-3'-deoxythymidine
-
3'-deoxy-3'-([[(3,4-dichlorophenyl)carbamothioyl]amino]methyl)thymidine
-
3'-deoxy-3'-([[(4-methoxyphenyl)carbamothioyl]amino]methyl)thymidine
-
3'-deoxy-3'-([[(4-methylphenyl)carbamothioyl]amino]methyl)thymidine
-
3'-[([[4-(benzyloxy)phenyl]carbamothioyl]amino)methyl]-3'-deoxythymidine
-
3'-[([[4-chloro-3-(trifluoromethyl)phenyl]carbamothioyl]amino)methyl]-2',3'-dideoxy-3,4-dihydrothymidine
-
-
3'-[([[4-chloro-3-(trifluoromethyl)phenyl]carbamothioyl]amino)methyl]-3'-deoxythymidine
-
3-((2R,3S,5R)-3-hydroxy-5-(5-(hydroxymethyl)-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl)propanenitrile
-
-
3-((2R,3S,5R)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl)propanenitrile
-
-
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamide
-
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzenesulfonamide
-
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzonitrile
-
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(2-(pyridin-4-yl)ethyl)benzamide
-
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(3-(4-(trifluoromethyl)phenyl)propyl)benzamide
-
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(3-(pyridin-3-yl)propyl)benzamide
-
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(3-morpholinopropyl)benzamide
-
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(3-phenylpropyl)benzamide
-
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(pyridin-2-ylmethyl)benzamide
-
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-phenethylbenzamide
-
3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamido)propanoic acid
-
3-(3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamido)propyl)benzoic acid
-
3-([1-[2-ammonio-3-(4-hydroxyphenyl)propanoyl]prolyl]amino)-4-oxoniobutanoate
-
4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-piperidin-1-yl)methyl)-2-(3-(trifluoromethyl)phenoxy)benzoic acid
4-(1-methyl -2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamide
-
4-(3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamido)propyl)benzoic acid
-
4-([1-[2-ammonio-3-(4-hydroxyphenyl)propanoyl]prolyl]amino)-5-oxoniopentanoate
-
4-[3-cyano-2-oxo-7-(1H-pyrazol-4-yl)-5,6-dihydro-1H-benzo[h]quinolin-4-yl]benzoic acid
compound shows showed cellular activity against Mycobacterium tuberculosis
4-[3-cyano-6-(3-methoxyphenyl)-2-oxo-1H-pyridin-4-yl]benzoic acid
compound shows showed cellular activity against Mycobacterium tuberculosis, MIC value above 32 microg/ml
4-[4-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
-
comparison with inhibition of human enzyme
4-[[4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl]methyl]benzoic acid
-
4-[[4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl]methyl]benzonitrile
-
5'-(4-benzyl-1H-1,2,3-triazol-1-yl)-2',5'-dideoxy-3,4-dihydrothymidine
-
-
5'-(4-chlorophenyl-1,2,3-triazol-1-yl)-5'-deoxy-alpha-D-thymidine
-
-
5'-(4-chlorophenyl-1,2,3-triazol-1-yl)-5'-deoxy-beta-D-thymidine
-
-
5'-([[4-chloro-3-(trifluoromethyl)benzyl]carbamothioyl]amino)-5'-deoxythymidine
-
5'-([[4-chloro-3-(trifluoromethyl)phenyl]carbamothioyl]amino)-2',5'-dideoxy-3,4-dihydro-alpha-thymidine
-
-
5'-([[4-chloro-3-(trifluoromethyl)phenyl]carbamoyl]amino)-2',5'-dideoxy-3,4-dihydrothymidine
-
-
5'-deoxy-5'-([[2-(3,4-dichlorophenyl)ethyl]carbamothioyl]amino)thymidine
-
5'-deoxy-5'-[(tricyclo[3.3.1.13,7]dec-1-ylcarbamothioyl)amino]thymidine
-
5'-deoxy-5'-[2-(methylsulfonyl)benzenesulfonylamido]thymidine
-
91% inhibition
5'-deoxy-5'-[4-(4-fluorophenyl)-(1,2,3)triazol-1-yl]thymidine
-
87% inhibition of enzyme activity, inhibition of Bacillus anthracis Sterne growth
5'-deoxy-5'-[4-(methylsulfonyl)benzenesulfonylamido]thymidine
-
94% inhibition
5'-deoxy-5'-[[(2-phenylethyl)carbamothioyl]amino]thymidine
-
5'-deoxy-5'-[[(3,4-dichlorophenyl)carbamoyl]amino]thymidine
-
5'-deoxy-5'-[[(4-morpholin-4-ylphenyl)carbamothioyl]amino]thymidine
-
5'-deoxy-5'-[[(diphenylmethyl)carbamothioyl]amino]thymidine
-
5'-deoxy-5'-[[(phenylcarbonyl)carbamothioyl]amino]thymidine
-
5'-deoxy-5'-[[2-(methylthio)anilinothiocarbonyl]amino]thymidine
-
84% inhibition
5'-deoxy-5'-[[3-(methylthio)anilinothiocarbonyl]amino]thymidine
-
69% inhibition of enzyme activity, inhibition of Bacillus anthracis Sterne growth
5'-[([[9-(2-carboxyphenyl)-3-oxo-2,3-dihydro-1H-xanthen-6-yl]oxy]carbamothioyl)amino]-5'-deoxythymidine
-
5'-[4-(4-chlorophenyl)-1H-1,2,3-triazol-1-yl]-2',5'-dideoxy-3,4-dihydrothymidine
-
-
5'-[5-(2-aminobenzyl)-1H-1,2,3-triazol-1-yl]-2',5'-dideoxy-3,4-dihydrothymidine
-
-
5'-[5-amino-4-[4-chloro-3-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-1-yl]-2',5'-dideoxy-3,4-dihydrothymidine
-
-
5-(5'-amino-5'-deoxy-beta-D-thymidin-5'-N-yl)-1-(4-chloro-3-trifluoromethylphenyl)-tetrazole
-
-
5-bromo-1-(1-(4-hydroxy-3-methoxyphenyl)-3-oxodecan-5-yl)-pyrimidine-2,4-(1H,3H)-dione
i.e. shogaol with bromouracil head group
5-methoxy-2-[(2E)-4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)but-2-en-1-yl]-1H-isoindole-1,3(2H)-dione
inhibitor identified by 3D-QSAR pharmacophore generation
5-methyl-1-(1-(3-(3-(trifluoromethyl)phenoxy)benzyl)piperidin-3-yl)pyrimidine-2,4(1H,3H)-dione
5-methyl-1-(1-[[4-(1H-tetrazol-5-yl)phenyl]methyl]piperidin-4-yl)pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-(2-[methyl[(3-phenoxyphenyl)methyl]amino]ethyl)pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[(2Z)-4-(2-oxobenzo[cd]indol-1(2H)-yl)but-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
-
-
5-methyl-1-[(3S)-1-[(3-phenoxyphenyl)methyl]piperidin-3-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-(2-phenylethyl)piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-(3-phenoxybenzoyl)piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-(4-phenoxybenzoyl)piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(3-methylphenyl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(3-phenoxyphenyl)methyl]azetidin-3-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(3-phenoxyphenyl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(4-methylphenyl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(4-phenoxyphenyl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(4-phenoxyquinolin-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(naphthalen-1-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(naphthalen-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(pyridin-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(pyridin-3-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(pyridin-4-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(quinolin-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(quinolin-3-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[(quinolin-4-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[2-(3-phenoxyphenyl)ethyl]azetidin-3-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[2-(3-phenoxyphenyl)ethyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
-
5-methyl-1-[1-[3-(3-phenoxyphenyl)propyl]azetidin-3-yl]pyrimidine-2,4(1H,3H)-dione
-
5-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]pentanoic acid
-
comparison with inhibition of human enzyme
5-[[4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl]methyl]pyridine-2-carboxylic acid
-
6-(3-(aminomethyl)phenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
-
6-(3-(hydroxymethyl)phenyl)-1-methyl-1H-imidazo[4,5-b]-pyridin-2(3H)-one
-
6-(3-acetylphenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
-
6-(3-aminophenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
-
6-(3-fluorophenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
-
6-(3-hydroxyphenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
-
6-(4-(aminomethyl)phenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
-
6-(4-hydroxyphenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
-
6-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]hexanamide
-
comparison with inhibition of human enzyme
6-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]hexanamide
-
comparison with inhibition of human enzyme
6-[4-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]hexanamide
-
comparison with inhibition of human enzyme
guanidine hydrochloride
guanidine hydrochloride-induced unfolding of thymidylate kinase is noncooperative and influences the functional properties of the enzyme much less than their Cm values. Complete inhibition at 0.4 M
methyl 2-(3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]-pyridin-6-yl)benzamido)propyl)benzoate
-
N,N-dimethyl-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]-pyridin-6-yl)benzamide
-
N-((1H-benzo[d]imidazol-2-yl)methyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
-
N-(2-(1H-benzo[d]imidazol-2-yl)ethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
-
N-(2-(1H-imidazol-5-yl)ethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
-
N-(2-amino-2-oxoethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
-
N-(2-aminoethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo-[4,5-b]pyridin-6-yl)benzamide
-
N-(2-hydroxyethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo-[4,5-b]pyridin-6-yl)benzamide
-
N-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)phenyl)acetamide
-
N-(3-(1H-imidazol-4-yl)propyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
-
N-(3-(1H-indol-3-yl)propyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
-
N-(3-(3-(aminomethyl)phenyl)propyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
-
N-(3-(4-(aminomethyl)phenyl)propyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
-
N-(3-(4-fluorophenyl)propyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
-
N-(3-cyclopentylpropyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
-
N-(5'-deoxy-4-thio-alpha-D-thymidin-5'-yl)-N'-(3-trifluoromethyl-4-chlorophenyl)thiourea
-
-
N-(5'-deoxy-alpha-thymidin-5'-yl)-N'-[4-(2-chlorobenzyloxy)phenyl]urea
-
N-(cyanomethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo-[4,5-b]pyridin-6-yl)benzamide
-
N-benzyl-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]-pyridin-6-yl)benzamide
-
N-methyl-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]-pyridin-6-yl)benzamide
-
N-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]benzamide
-
Urea
urea-induced unfolding of thymidylate kinase is noncooperative and influences the functional properties of the enzyme much less than their Cm values. Complete inhibition at 1.0 M
[(1S,4R)-4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)cyclopent-2-en-1-yl]methyl acetate
-
-
(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
-
-
(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
-
-
(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
-
-
(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
-
-
(3E)-4-[4-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]but-3-enoic acid
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
(3E)-4-[4-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]but-3-enoic acid
-
comparison with inhibition of human enzyme
(R)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(R)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(R)-1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(R)-1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3,5-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3,5-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3-bromophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3-bromophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3-chloro-4-methylphenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3-chloro-4-methylphenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3-chloro-5-fluorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3-chloro-5-fluorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3-fluorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(3-fluorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
(S)-2-(3-bromophenoxy)-4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)methyl)benzoic acid
-
-
(S)-2-(3-bromophenoxy)-4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)methyl)benzoic acid
-
-
(S)-2-(3-fluorophenoxy)-4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)methyl)benzoic acid
-
-
(S)-2-(3-fluorophenoxy)-4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)methyl)benzoic acid
-
-
(S)-4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-piperidin-1-yl)methyl)-2-(m-tolyloxy)benzoic acid
-
-
(S)-4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-piperidin-1-yl)methyl)-2-(m-tolyloxy)benzoic acid
-
-
(S)-5-methyl-1-(1-(3-(m-tolyloxy)benzyl)piperidin-3-yl)-pyrimidine-2,4(1H,3H)-dione
-
-
(S)-5-methyl-1-(1-(3-(m-tolyloxy)benzyl)piperidin-3-yl)-pyrimidine-2,4(1H,3H)-dione
-
-
1,3-bis[[(2S,3R,5R)-2-methyl-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]urea
-
-
1,3-bis[[(2S,3R,5R)-2-methyl-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]urea
-
1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-(1-(3-(4-methoxyphenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-(1-(3-(4-methoxyphenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-(3,4-dichlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
1-(3,4-dichlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
comparison with inhibition of human enzyme
1-(3,4-dichlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
-
1-(3-chloro-4-trifluoromethylphenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
1-(3-chloro-4-trifluoromethylphenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
comparison with inhibition of human enzyme
1-(4-chlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
1-(4-chlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
comparison with inhibition of human enzyme
1-(4-chlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
-
1-[(1R,2R,4R,5S)-4-(hydroxymethyl)-6-oxabicyclo[3.1.0]hex-2-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-[(1R,2R,4R,5S)-4-(hydroxymethyl)-6-oxabicyclo[3.1.0]hex-2-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-oxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-oxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-thioxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-thioxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-thioxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
1-[4-chloro-3-(trifluoromethyl)phenyl]-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
1-[4-chloro-3-(trifluoromethyl)phenyl]-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
comparison with inhibition of human enzyme
1-[4-chloro-3-(trifluoromethyl)phenyl]-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
-
2-(3-bromophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
-
-
2-(3-bromophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
-
-
2-(3-bromophenoxy)-4-((R)-3-ethyl-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
-
-
2-(3-bromophenoxy)-4-((R)-3-ethyl-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
-
-
2-(3-bromophenoxy)-4-((S)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
-
-
2-(3-bromophenoxy)-4-((S)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
-
-
2-(3-bromophenoxy)-4-(R)-(2-(1-adamantane)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
-
-
2-(3-bromophenoxy)-4-(R)-(2-(1-adamantane)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)-2-(tetrahydro-2H-pyran-4-yl)ethyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)-2-(tetrahydro-2H-pyran-4-yl)ethyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1-(2H)-yl)piperidin-1-yl)butyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1-(2H)-yl)piperidin-1-yl)butyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-2-cyclohexyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-2-cyclohexyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-3-ethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-3-ethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((R)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((S)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
-
-
2-(3-chlorophenoxy)-4-((S)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
-
-
3'-azido-3'-deoxythymidine
specific inhibitory effect on the enzyme activity, and these effect is in good association with binding interactions and the scoring functions
3'-azido-3'-deoxythymidine 5'-monophosphate
-
potent competitive inhibitor
3'-azido-3'-deoxythymidine 5'-monophosphate
potential inhibitor
3'-azido-3'-deoxythymidine 5'-monophosphate
potential inhibitor of the bacterial enzyme, not inhibitory in human
4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-piperidin-1-yl)methyl)-2-(3-(trifluoromethyl)phenoxy)benzoic acid
-
-
4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-piperidin-1-yl)methyl)-2-(3-(trifluoromethyl)phenoxy)benzoic acid
-
-
4-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanamide
-
not inhibitory up to 2 mM, inhibitory to Mycobacterium tuberculosis enzyme
4-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanamide
-
comparison with inhibition of human enzyme
4-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
4-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
-
comparison with inhibition of human enzyme
4-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanamide
-
not inhibitory up to 2 mM, inhibitory to Mycobacterium tuberculosis enzyme
4-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanamide
-
comparison with inhibition of human enzyme
4-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
4-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
-
comparison with inhibition of human enzyme
5-bromo-2'-deoxyuridine
-
potential inhibitor with high selectivity between bacterial and human enzyme
5-bromo-2'-deoxyuridine
specific inhibitory effect on the enzyme activity, and these effect is in good association with binding interactions and the scoring functions
5-chloro-2'-deoxyuridine
-
potential inhibitor with high selectivity between bacterial and human enzyme
5-chloro-2'-deoxyuridine
specific inhibitory effect on the enzyme activity, and these effect is in good association with binding interactions and the scoring functions
5-fluoro-2'-deoxyuridine
-
potential inhibitor with high selectivity between bacterial and human enzyme
5-iodo-2'-deoxyuridine
-
potential inhibitor with high selectivity between bacterial and human enzyme
5-methyl-1-(1-(3-(3-(trifluoromethyl)phenoxy)benzyl)piperidin-3-yl)pyrimidine-2,4(1H,3H)-dione
-
-
5-methyl-1-(1-(3-(3-(trifluoromethyl)phenoxy)benzyl)piperidin-3-yl)pyrimidine-2,4(1H,3H)-dione
-
-
5-methyl-1-[1-(3-phenoxybenzyl)piperidin-3-yl]pyrimidine-2,4(1H,3H)-dione
-
-
5-methyl-1-[1-(3-phenoxybenzyl)piperidin-3-yl]pyrimidine-2,4(1H,3H)-dione
-
-
5-methyl-1-[1-[3-(4-methylphenoxy)benzyl]piperidin-3-yl]-pyrimidine-2,4(1H,3H)-dione
-
-
5-methyl-1-[1-[3-(4-methylphenoxy)benzyl]piperidin-3-yl]-pyrimidine-2,4(1H,3H)-dione
-
-
5-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]pentanoic acid
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
5-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]pentanoic acid
-
comparison with inhibition of human enzyme
ADP
-
ADP*Mg2+ product inhibition, competitive versus MgATP2-, noncompetitive versus thymidylate
deoxythymidine
-
potential inhibitor with high selectivity between bacterial and human enzyme
N-(3,4-dichlorophenyl)-N'-(5'-deoxy-alpha-D-thymidin-5'-yl)-urea
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
N-(3,4-dichlorophenyl)-N'-(5'-deoxy-alpha-D-thymidin-5'-yl)-urea
comparison with inhibition of human enzyme
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(3,4-dichlorophenylethyl)thiourea
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(3,4-dichlorophenylethyl)thiourea
comparison with inhibition of human enzyme
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(3-trifluoromethyl-4-chlorobenzyl)thiourea
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(3-trifluoromethyl-4-chlorobenzyl)thiourea
comparison with inhibition of human enzyme
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(4-chloro-3-(trifluoromethyl)phenylethyl)urea
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(4-chloro-3-(trifluoromethyl)phenylethyl)urea
comparison with inhibition of human enzyme
TK-666
-
i.e. 2-(3-bromophenoxy)-4-((R)-3,3-dimethyl-1-((S)-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1-(2H)-yl)piperidin-1-yl)butyl)benzoic acid
TK-666
-
i.e. 2-(3-bromophenoxy)-4-((R)-3,3-dimethyl-1-((S)-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1-(2H)-yl)piperidin-1-yl)butyl)benzoic acid
additional information
-
3-azido-3-deoxythymidine monophosphate is not inhibitory, various thymine derivatives tested and found to inhibit activity to different extents
-
additional information
-
acyclic nucleoside analogues (Z)-2-(4-(thymin-1-yl)but-2-enyl)-1H-benzo[d,e]isoquinoline-1,3(2H)-dione and (Z)-2-(4-(thymin-1-yl)but-2-enyl)-2,3-dihydro-1H-benzo-[d,e]isoquinolin-1-one are not inhibitory up to 0.02 mM
-
additional information
several different TMP analogues tested and found to be inhibitory
-
additional information
-
several different TMP analogues tested and found to be inhibitory
-
additional information
3'-(aminomethyl)-3'-deoxy-2'-fluorothymidine is not inhibitory at 1 mM; 3-azido-3-deoxythymidine monophosphate is not inhibitory, various thymine derivatives tested and found to inhibit activity to different extents
-
additional information
-
3'-(aminomethyl)-3'-deoxy-2'-fluorothymidine is not inhibitory at 1 mM; 3-azido-3-deoxythymidine monophosphate is not inhibitory, various thymine derivatives tested and found to inhibit activity to different extents
-
additional information
-
not inhibited by N-(5'-deoxy-4-thio-alpha-D-thymidin-5'-yl)-N'-phenylthiourea
-
additional information
-
not inhibited by 3-((2R,3S,5R)-3-hydroxy-5-(5-(hydroxymethyl)-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl)propanenitrile and 1-((2R,4S,5R)-5-(2-(1H-tetrazol-5-yl)ethyl)-4-hydroxytetrahydrofuran-2-yl)-5-(hydroxymethyl)pyrimidine-2,4(1H,3H)-dione
-
additional information
-
not inhibitory: 2-mercaptoethanol up to 5 mM, AMP, CMP, dCMP, GMP and dGMP and
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
freezing at -70°C and then thawing results in an increase in activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-thymidyl) pentaphosphate (TP5A) at 2.0 A resolution: implications for catalysis and AZT activation.
Anthrax
Synthesis and biological evaluation of inhibitors of thymidine monophosphate kinase from Bacillus anthracis.
Ataxia Telangiectasia
Thymidylate kinase is critical for DNA repair via ATM-dependent Tip60 complex formation.
Carcinoma, Hepatocellular
Growth inhibition of Kirkman-Robbins hepatoma by 1-(1,3-dihydroxy-2-propoxymethyl)-5,6-tetramethyleneuracil and possible mechanism of its biological activity.
Carcinoma, Hepatocellular
Metabolism of 5-fluorouracil in sensitive and resistant tumor cells.
Carcinoma, Hepatocellular
Purification and properties of thymidine monophosphate kinase from mouse hepatoma.
Colonic Neoplasms
Synthetic lethality by lentiviral short hairpin RNA silencing of thymidylate kinase and doxorubicin in colon cancer cells regardless of the p53 status.
Embryo Loss
Enzymatic activities leading to pyrimidine nucleotide biosynthesis from cell-free extracts of Rickettsia typhi.
Herpes Simplex
An optimized thymidylate kinase assay, based on enzymatically synthesized 5-[125I]iododeoxyuridine monophosphate and its application to an immunological study of herpes simplex virus thymidine-thymidylate kinases.
HIV Infections
Decrease in thymidylate kinase activity in peripheral blood mononuclear cells from HIV-infected individuals.
Hypersensitivity
Substitution of an alanine residue for glycine 146 in TMP kinase from Escherichia coli is responsible for bacterial hypersensitivity to bromodeoxyuridine.
Infections
Vaccinia virus encodes a thymidylate kinase gene: sequence and transcriptional mapping.
Latent Infection
Low levels of herpes simplex virus thymidine- thymidylate kinase are not limiting for sensitivity to certain antiviral drugs or for latency in a mouse model.
Neoplasms
Activities of various enzymes of pyrimidine nucleotide and DNA syntheses in normal and neoplastic human tissues.
Neoplasms
An optimized thymidylate kinase assay, based on enzymatically synthesized 5-[125I]iododeoxyuridine monophosphate and its application to an immunological study of herpes simplex virus thymidine-thymidylate kinases.
Neoplasms
Crystal structure of poxvirus thymidylate kinase: an unexpected dimerization has implications for antiviral therapy.
Neoplasms
Growth inhibition of Kirkman-Robbins hepatoma by 1-(1,3-dihydroxy-2-propoxymethyl)-5,6-tetramethyleneuracil and possible mechanism of its biological activity.
Neoplasms
Metabolism of pyrimidine nucleotides in various tissues and tumor cells from rodents.
Neoplasms
The engineered thymidylate kinase (TMPK)/AZT enzyme-prodrug axis offers efficient bystander cell killing for suicide gene therapy of cancer.
Neoplasms
Tumor cells require thymidylate kinase to prevent dUTP incorporation during DNA repair.
Neuroblastoma
Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth.
Prostatic Neoplasms
The engineered thymidylate kinase (TMPK)/AZT enzyme-prodrug axis offers efficient bystander cell killing for suicide gene therapy of cancer.
Pseudorabies
Equine herpes virus 1 and pseudorabies virus resistance to 2'-fluoropyrimidine analogs and to bromovinyldeoxyuridine: implications for dTMP kinase activity.
Tuberculosis
1-(1-Arylethylpiperidin-4-yl)thymine Analogs as Antimycobacterial TMPK Inhibitors.
Tuberculosis
1-(Piperidin-3-yl)thymine amides as inhibitors of M. tuberculosis thymidylate kinase.
Tuberculosis
3'-C-branched-chain-substituted nucleosides and nucleotides as potent inhibitors of Mycobacterium tuberculosis thymidine monophosphate kinase.
Tuberculosis
3D-QSAR studies on antitubercular thymidine monophosphate kinase inhibitors based on different alignment methods.
Tuberculosis
A new family of inhibitors of Mycobacterium tuberculosis thymidine monophosphate kinase.
Tuberculosis
A virtual screening approach for thymidine monophosphate kinase inhibitors as antitubercular agents based on docking and pharmacophore models.
Tuberculosis
Comparative study of purine and pyrimidine nucleoside analogues acting on the thymidylate kinases of Mycobacterium tuberculosis and of humans.
Tuberculosis
Computer-assisted combinatorial design of bicyclic thymidine analogs as inhibitors of Mycobacterium tuberculosis thymidine monophosphate kinase.
Tuberculosis
Design of Mycobacterium tuberculosis thymidine monophosphate kinase inhibitors.
Tuberculosis
Design of Thymidine Analogues Targeting Thymidilate Kinase of Mycobacterium tuberculosis.
Tuberculosis
Design, synthesis and inhibitory activity against Mycobacterium tuberculosis thymidine monophosphate kinase of acyclic nucleoside analogues with a distal imidazoquinolinone.
Tuberculosis
Discovery of bicyclic thymidine analogues as selective and high-affinity inhibitors of Mycobacterium tuberculosis thymidine monophosphate kinase.
Tuberculosis
Drug design and identification of potent leads against Mycobacterium tuberculosis thymidine monophosphate kinase.
Tuberculosis
Enzymatic and structural analysis of inhibitors designed against Mycobacterium tuberculosis thymidylate kinase. New insights into the phosphoryl transfer mechanism.
Tuberculosis
Exploring acyclic nucleoside analogues as inhibitors of Mycobacterium tuberculosis thymidylate kinase.
Tuberculosis
Identification of novel antimycobacterial chemical agents through the in silico multi-conformational structure-based drug screening of a large-scale chemical library.
Tuberculosis
Knowledge based identification of potent antitubercular compounds using structure based virtual screening and structure interaction fingerprints.
Tuberculosis
Mycobacterium tuberculosis thymidylate kinase: structural studies of intermediates along the reaction pathway.
Tuberculosis
Optimization of Structure Based Virtual Screening Protocols Against Thymidine Monophosphate Kinase Inhibitors as Antitubercular Agents.
Tuberculosis
Pharmacophore optimization and design of competitive inhibitors of Thymidine Monophosphate Kinase through molecular modeling studies.
Tuberculosis
Rational Design and 3D-Pharmacophore Mapping of 5'-Thiourea-Substituted alpha-Thymidine Analogues as Mycobacterial TMPK Inhibitors.
Tuberculosis
Rational Design of 5'-Thiourea-Substituted alpha-Thymidine Analogues as Thymidine Monophosphate Kinase Inhibitors Capable of Inhibiting Mycobacterial Growth.
Tuberculosis
Structural and chemical basis for enhanced affinity to a series of mycobacterial thymidine monophosphate kinase inhibitors: fragment-based QSAR and QM/MM docking studies.
Tuberculosis
Structure Guided Lead Generation toward Nonchiral M. tuberculosis Thymidylate Kinase Inhibitors.
Tuberculosis
Structure-based in-silico rational design of a selective peptide inhibitor for thymidine monophosphate kinase of mycobacterium tuberculosis.
Tuberculosis
Substituted benzyl-pyrimidines targeting thymidine monophosphate kinase of Mycobacterium tuberculosis: synthesis and in vitro anti-mycobacterial activity.
Tuberculosis
Synthesis and biological evaluation of bicyclic nucleosides as inhibitors of M. tuberculosis thymidylate kinase.
Tuberculosis
Synthesis and evaluation of 5'-modified thymidines and 5-hydroxymethyl-2'-deoxyuridines as Mycobacterium tuberculosis thymidylate kinase inhibitors.
Tuberculosis
Synthesis and Evaluation of 6-Aza-2'-deoxyuridine Monophosphate Analogs as Inhibitors of Thymidylate Synthases, and as Substrates or Inhibitors of Thymidine Monophosphate Kinase in Mycobacterium tuberculosis.
Tuberculosis
Synthesis and evaluation of thymidine-5'-O-monophosphate analogues as inhibitors of Mycobacterium tuberculosis thymidylate kinase.
Tuberculosis
Synthesis and inhibitory activity of thymidine analogues targeting Mycobacterium tuberculosis thymidine monophosphate kinase.
Tuberculosis
Synthesis of sulfamide analogues of deoxthymidine monophosphate as potential inhibitors of mycobacterial cell wall biosynthesis.
Tuberculosis
Tetrahydro-2-furanyl-2,4(1H,3H)-pyrimidinedione derivatives as novel antibacterial compounds against
Tuberculosis
Thymidine and thymidine-5'-O-monophosphate analogues as inhibitors of Mycobacterium tuberculosis thymidylate kinase.
Tuberculosis
X-ray structure of TMP kinase from Mycobacterium tuberculosis complexed with TMP at 1.95 A resolution.
Vaccinia
Crystal structure of poxvirus thymidylate kinase: an unexpected dimerization has implications for antiviral therapy.
Vaccinia
Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast.
Vaccinia
Phosphorylation of dGMP analogs by vaccinia virus TMP kinase and human GMP kinase.
Vaccinia
Preventing the return of smallpox: molecular modeling studies on thymidylate kinase from Variola virus.
Vaccinia
Vaccinia virus encodes a thymidylate kinase gene: sequence and transcriptional mapping.
Vaccinia
Vaccinia virus encodes an active thymidylate kinase that complements a cdc8 mutant of Saccharomyces cerevisiae.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
5-bromo-dUMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.0044
D-2'-fluoroarabinosyl-5-methyldeoxyuridine 5'-monophosphate
pH 7.6, 37°C
0.167
L-2'-fluoroarabinosyl-5-methyldeoxyuridine 5'-monophosphate
pH 7.6, 37°C
1
N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-thymine
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
1
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-fluorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.024
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-thymine
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
1.7
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-uracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.16
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-bromouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.15
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-chlorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
1.9
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-fluorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.1
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-thymine
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
2.5
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-uracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.012
2',3'-didehydro-2',3'-dideoxythymidine 5'-monophosphate
pH 7.5, 25°C
0.0038
3'-azido-3'-deoxythymidine monophosphate
pH and temperature not specified in the publication, mutant enzyme F105Y
0.0045
3'-azido-3'-deoxythymidine monophosphate
pH 7.4, temperature not specified in the publication, NADH coupled assay
0.012
3'-azido-3'-deoxythymidine monophosphate
pH and temperature not specified in the publication, wild-type enzyme
0.08
5-bromo-2'-deoxyuridine 5'-monophosphate
-
pH 7.4, 30°C, wild-type enzyme
0.28
5-bromo-2'-deoxyuridine 5'-monophosphate
-
pH 7.4, 30°C, mutant enzyme G146A
0.027
ATP
pH 7.5, 25°C, reaction with 3'-fluoro-3'-deoxythymidine 5'-monophosphate
0.033
ATP
pH 7.5, 25°C, reaction with 2',3'-didehydro-2',3'-dideoxythymidine 5'-monophosphate
0.066
ATP
pH 7.4, temperature not specified in the publication
0.069
ATP
pH 7.5, 25°C, reaction with 3'-azido-3'-deoxythymidine 5'-monophosphate
0.1008
ATP
-
wild-type enzyme, pH 7.4, temperature not specified in the publication
0.00107
dGMP
pH 7.4, temperature not specified in the publication, NADH coupled assay
0.0362
dGMP
-
wild-type enzyme, pH 7.4, temperature not specified in the publication
0.0476
dGMP
-
mutant enzyme S108A, pH 7.4, temperature not specified in the publication
0.0784
dGMP
-
mutant enzyme S108T, pH 7.4, temperature not specified in the publication
0.0969
dGMP
-
mutant enzyme Y153F, pH 7.4, temperature not specified in the publication
0.0045
dTMP
-
in 50 mM Tris-HCl pH 7.4, 50 mM KCl, 2 mM MgCl2, temperature not specified in the publication
0.017
dTMP
pH 7.4, temperature not specified in the publication
0.02
dTMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.17
dUMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.02
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.13
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.0042
TMP
pH and temperature not specified in the publication, mutant enzyme F105Y
0.0062
TMP
pH 7.4, temperature not specified in the publication, NADH coupled assay
0.0063
TMP
pH and temperature not specified in the publication, wild-type enzyme
0.0242
TMP
-
mutant enzyme S108T, pH 7.4, temperature not specified in the publication
0.0255
TMP
-
wild-type enzyme, pH 7.4, temperature not specified in the publication
0.0258
TMP
-
mutant enzyme S108A, pH 7.4, temperature not specified in the publication
0.0659
TMP
-
mutant enzyme Y153F, pH 7.4, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
2',3'-didehydro-2',3'-dideoxythymidine 5'-monophosphate
pH 7.5, 25°C
1.2
5-bromo-dUMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.6
N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-thymine
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.73
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-fluorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.84
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-thymine
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.48
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-uracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.058
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-bromouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.1
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-chlorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.09
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-fluorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.32
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-thymine
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.074
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-uracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.003
3'-azido-3'-deoxythymidine 5'-monophosphate
-
wild-type enzyme fused to the protein transduction domain of Tat
0.17
3'-azido-3'-deoxythymidine 5'-monophosphate
-
mutant F105Y fused to the protein transduction domain of Tat
1.5
3'-azido-3'-deoxythymidine 5'-monophosphate
-
mutant carrying a substitution of the LID domain in human enzyme by the Escherichia coli LID sequence and mutation of the P-loop Arg residue to Gly and fused to the protein transduction domain of Tat
1.7
3'-azido-3'-deoxythymidine 5'-monophosphate
-
mutant carrying a substitution of the LID domain in human enzyme by the Escherichia coli LID sequence and mutation of the P-loop Arg residue to Gly
0.012
3'-azido-3'-deoxythymidine monophosphate
pH and temperature not specified in the publication, wild-type enzyme
0.25
3'-azido-3'-deoxythymidine monophosphate
pH and temperature not specified in the publication, mutant enzyme F105Y
0.3
3'-azido-3'-deoxythymidine monophosphate
pH 7.4, temperature not specified in the publication, NADH coupled assay
0.5
3'-azido-3'-deoxythymidine monophosphate
pH 7.4, temperature not specified in the publication, NMR assay
3.3
ATP
-
wild-type enzyme, pH 7.4, temperature not specified in the publication
38.1
ATP
pH 7.4, temperature not specified in the publication
0.006
dGMP
pH 7.4, temperature not specified in the publication, NMR assay
0.008
dGMP
pH 7.4, temperature not specified in the publication, NADH coupled assay
1
dGMP
-
mutant enzyme Y153F, pH 7.4, temperature not specified in the publication
1.3
dGMP
-
mutant enzyme S108A, pH 7.4, temperature not specified in the publication
1.3
dGMP
-
mutant enzyme S108T, pH 7.4, temperature not specified in the publication
2.4
dGMP
-
wild-type enzyme, pH 7.4, temperature not specified in the publication
0.83
dTMP
-
mutant carrying a substitution of the LID domain in human enzyme by the Escherichia coli LID sequence and mutation of the P-loop Arg residue to Gly and fused to the protein transduction domain of Tat
1.1
dTMP
-
mutant carrying a substitution of the LID domain in human enzyme by the Escherichia coli LID sequence and mutation of the P-loop Arg residue to Gly
3
dTMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
4.8
dUMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.5
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.9
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.17
TMP
pH and temperature not specified in the publication, mutant enzyme F105Y
0.73
TMP
pH and temperature not specified in the publication, wild-type enzyme
1.2
TMP
-
mutant enzyme Y153F, pH 7.4, temperature not specified in the publication
3.1
TMP
-
wild-type enzyme, pH 7.4, temperature not specified in the publication
3.2
TMP
-
mutant enzyme S108T, pH 7.4, temperature not specified in the publication
3.3
TMP
-
mutant enzyme S108A, pH 7.4, temperature not specified in the publication
6.9
TMP
pH 7.4, temperature not specified in the publication, NADH coupled assay
8.7
TMP
pH 7.4, temperature not specified in the publication, NMR assay
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
120
5-bromo-dUMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
28
dUMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.6
N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-thymine
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.73
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-fluorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
35
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-thymine
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.28
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-uracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.36
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-bromouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.66
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-chlorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.047
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-fluorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
3.2
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-thymine
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.03
N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-uracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
577
ATP
pH 7.4, temperature not specified in the publication
150
dTMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
2240
dTMP
pH 7.4, temperature not specified in the publication
4.1
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
45
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0058
(+/-)(Z)-5-acetamido-1-(4-(thymin-1-yl)but-2-enyl)-5,6-dihydro-1H-imidazo[4,5,1-ij]quinolin-2(4H)-one
-
in 50 mM Tris-HCl pH 7.4, 50 mM KCl, 2 mM MgCl2, temperature not specified in the publication
0.00707
(+/-)(Z)-5-amino-1-(4-(thymin-1-yl)but-2-enyl)-5,6-dihydro-1H-imidazo[4,5,1-ij]quinolin-2(4H)-one
-
in 50 mM Tris-HCl pH 7.4, 50 mM KCl, 2 mM MgCl2, temperature not specified in the publication
0.039 - 0.252
(3E)-4-[4-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]but-3-enoic acid
0.0108
(4E)-1-(4-hydroxy-3-methoxyphenyl)dec-4-en-3-one
pH 7.4, temperature not specified in the publication
0.00042
(Z)-1-(4-(thymin-1-yl)but-2-enyl)-1H-benzo[c,d]indol-2(1H)one
pH 7.4
0.00116
(Z)-1-(4-(thymin-1-yl)but-2-enyl)-5,6-dihydro-1H-imidazo[4,5,1-ij]quinolin-2(4H)-one
-
in 50 mM Tris-HCl pH 7.4, 50 mM KCl, 2 mM MgCl2, temperature not specified in the publication
0.0011
(Z)-2-(4-(5-bromouracil-1-yl)but-2-enyl)-1H-benzo[d,e] isoquinoline-1,3(2H)-dione
pH 7.4
0.0019
(Z)-2-(4-(thymin-1-yl)but-2-enyl)-1H-benzo[d,e]isoquinoline-1,3(2H)-dione
pH 7.4
0.0014
(Z)-2-(4-(thymin-1-yl)but-2-enyl)-2,3-dihydro-1H-benzo-[d,e]isoquinolin-1-one
pH 7.4
0.00027
(Z)-2-(4-(thymin-1-yl)but-2-enyl)-2H-naphtho[1,8 cd]isothiazole-1,1-dioxide
pH 7.4
0.00075
(Z)-2-(4-(thymin-1-yl)but-2-enyl)-6-nitrobenzo[c,d]indol-2(1H)one
pH 7.4
0.00093
(Z)-8-acetamido-1-(4-(thymin-1-yl)but-2-enyl)-5,6-dihydro-1H-imidazo[4,5,1-ij]quinolin-2(4H)-one
-
in 50 mM Tris-HCl pH 7.4, 50 mM KCl, 2 mM MgCl2, temperature not specified in the publication
0.00246
(Z)-8-amino-1-(4-(thymin-1-yl)but-2-enyl)-5,6-dihydro-1H-imidazo[4,5,1-ij]quinolin-2(4H)-one
-
in 50 mM Tris-HCl pH 7.4, 50 mM KCl, 2 mM MgCl2, temperature not specified in the publication
0.029
1,3-bis[[(2S,3R,5R)-2-methyl-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]urea
-
0.037
1-(((2R,3S,5S)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl)methyl)-3-(((2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl)methyl)urea
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.34
1-((2R,4S,5R)-4-hydroxy-5-(2-(methylsulfonyl)ethyl)tetrahydrofuran-2-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
pH and temperature not specified in the publication
0.07
1-((2R,4S,5R)-5-(2-(1H-tetrazol-5-yl)ethyl)-4-hydroxytetrahydrofuran-2-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
-
pH and temperature not specified in the publication
0.0066
1-(1-(4-hydroxy-3-methoxyphenyl)-3-oxodecan-5-yl)-5-methylpyrimidine-2,4-(1H,3H)-dione
pH 7.4, temperature not specified in the publication
0.001 - 0.274
1-(3,4-dichlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
0.0072
1-(3,4-dichlorophenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
pH 7.4
0.008
1-(3-amino-3-deoxy-2-O,3-N-(thiocarbonyl)-beta-D-ribofuranosyl)thymine
-
-
0.0023
1-(3-aminomethyl-3,5-dideoxy-2-O,6-N-(thiocarbonyl)-beta-D-ribofuranosyl)thymine
-
-
0.005 - 1
1-(3-chloro-4-trifluoromethylphenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
0.012
1-(4-benzyloxyphenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
pH 7.4
0.0032 - 1
1-(4-chlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
0.021
1-(4-chlorophenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
pH 7.4
0.067 - 2.5
1-[(1R,2R,3S,4R)-2,3-dihydroxy-4-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
0.055 - 0.208
1-[(1R,2R,4R,5S)-4-(hydroxymethyl)-6-oxabicyclo[3.1.0]hex-2-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
1.54
1-[(1R,2S,3R,4R)-2,3-dihydroxy-4-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
with dGMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
0.103 - 0.355
1-[(1R,3S,4R)-3-hydroxy-4-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
0.007 - 0.02
1-[(1R,4S)-4-(hydroxymethyl)cyclopent-2-en-1-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
0.089 - 0.246
1-[(1S,3R)-3-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
0.000004
1-[(2E)-4-(5,6-dimethoxy-1-oxo-1,3-dihydro-2H-isoindol-2-yl)but-2-en-1-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
predicted value, pH not specified in the publication, temperature not specified in the publication
0.000004
1-[(2E)-4-[5,6-bis(hydroxymethyl)-2-oxobenzo[cd]indol-1(2H)-yl]but-2-en-1-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
predicted value, pH not specified in the publication, temperature not specified in the publication
0.0003
1-[(2Z)-(4-(5-bromouracil-1-yl)but-2-enyl)]-5,6-dihydro-1H,4H-1,2,5-thiadiazolo[4,3,2-ij]quinolin-2,2-dioxide
-
in 50 mM Tris-HCl pH 7.4, 50 mM KCl, 2 mM MgCl2, temperature not specified in the publication
0.00027
1-[(2Z)-4-(1,1-dioxido-2H-naphtho[1,8-cd][1,2]thiazol-2-yl)but-2-en-1-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
in 50 mM Tris-HCl pH 7.4, 50 mM KCl, 2 mM MgCl2, temperature not specified in the publication
0.0135 - 1.1
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-oxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
0.0035 - 0.7
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-thioxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
0.00057
1-[(Z)-(4-(thymin-1-yl)but-2-enyl)]-5,6-dihydro-1H,4H-1,2,5-thiadiazolo[4,3,2-ij]quinolin-2,2-dioxide
-
in 50 mM Tris-HCl pH 7.4, 50 mM KCl, 2 mM MgCl2, temperature not specified in the publication
0.0205
1-[2,5-dideoxy-5-[([4-[(2-fluorophenyl)methoxy]phenyl]carbamoyl)amino]-alpha-D-erythro-pentofuranosyl]-5-methylpyrimidine-2,4(1H,3H)-dione
pH and temperature not specified in the publication
0.22
1-[2,5-dideoxy-5-[([4-[(2-methoxyphenyl)methoxy]phenyl]carbamoyl)amino]-alpha-D-erythro-pentofuranosyl]-5-methylpyrimidine-2,4(1H,3H)-dione
pH and temperature not specified in the publication
0.0023
1-[3-aminomethyl-3,5-dideoxy-2-O,6-N-(thiocarbonyl)-beta-D-ribofuranosyl]thymine
-
-
0.0006 - 0.362
1-[4-chloro-3-(trifluoromethyl)phenyl]-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
0.00017
1-[5-([[4-chloro-3-(trifluoromethyl)phenyl]carbamothioyl]amino)-2,5-dideoxy-a-D-erythro-pentofuranosyl]-5-methyl-4-thioxo-3,4-dihydropyrimidin-2(1H)-one
-
pH and temperature not specified in the publication
0.225
1-[5-[([4-[(2-chlorophenyl)methoxy]phenyl]carbamoyl)amino]-2,5-dideoxy-alpha-D-erythro-pentofuranosyl]-5-methylpyrimidine-2,4(1H,3H)-dione
pH and temperature not specified in the publication
0.0042
2',5'-dideoxy-5'-(4-phenyl-1H-1,2,3-triazol-1-yl)-3,4-dihydrothymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.0028
2',5'-dideoxy-5'-([[3-(trifluoromethyl)phenyl]carbamoyl]amino)-3,4-dihydrothymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.24
2-((2R,3S,5R)-3-((tert-butyldimethylsilyl)oxy)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl)-N-methylethanesulfonamide
-
pH and temperature not specified in the publication
0.00029
2-[(4aS,5R,7R,7aR)-5-[5-(hydroxymethyl)-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl]-2,2-dioxidooctahydrocyclopenta[c][1,2,6]thiadiazin-7-yl]-N-methylethanesulfonamide
-
pH and temperature not specified in the publication
0.00043
2-[([1-[2-ammonio-3-(1H-indol-3-yl)propanoyl]pyrrolidin-2-yl]methyl)amino]butanedioate
pH and temperature not specified in the publication
0.028
3',5'-diazido-2',3',5'-trideoxy-3,4-dihydrothymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.015
3'-(4-chlorophenyl-1,2,3-triazol-1-yl)-3'-deoxy-4-thio-beta-D-thymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.035
3'-(4-chlorophenyl-1,2,3-triazol-1-yl)-3'-deoxy-alpha-D-thymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.1
3'-azido-3'-deoxy-4-thio-beta-D-thymidine
-
Ki above 0.1 mM, in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.006
3'-azido-3'-deoxy-alpha-D-thymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.027
3'-Deoxythymidine
pH and temperature not specified in the publication
0.005
3'-[([[4-chloro-3-(trifluoromethyl)phenyl]carbamothioyl]amino)methyl]-2',3'-dideoxy-3,4-dihydrothymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.048
3-((2R,3S,5R)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl)propanenitrile
-
pH and temperature not specified in the publication
0.039
4-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanamide
-
-
0.01 - 0.293
4-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
0.039
4-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanamide
-
-
0.0065 - 0.79
4-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
0.013
4-[4-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
-
-
0.0027
5'-(4-benzyl-1H-1,2,3-triazol-1-yl)-2',5'-dideoxy-3,4-dihydrothymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.009
5'-(4-chlorophenyl-1,2,3-triazol-1-yl)-5'-deoxy-alpha-D-thymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.201
5'-(4-chlorophenyl-1,2,3-triazol-1-yl)-5'-deoxy-beta-D-thymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.0006
5'-([[4-chloro-3-(trifluoromethyl)phenyl]carbamothioyl]amino)-2',5'-dideoxy-3,4-dihydro-alpha-thymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.0099
5'-([[4-chloro-3-(trifluoromethyl)phenyl]carbamoyl]amino)-2',5'-dideoxy-3,4-dihydrothymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.0265
5'-azido-2',5'-dideoxy-3,4-dihydrothymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.0021
5'-[4-(4-chlorophenyl)-1H-1,2,3-triazol-1-yl]-2',5'-dideoxy-3,4-dihydrothymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.0023
5'-[5-(2-aminobenzyl)-1H-1,2,3-triazol-1-yl]-2',5'-dideoxy-3,4-dihydrothymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.045
5'-[5-amino-4-[4-chloro-3-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-1-yl]-2',5'-dideoxy-3,4-dihydrothymidine
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.073
5-(5'-amino-5'-deoxy-beta-D-thymidin-5'-N-yl)-1-(4-chloro-3-trifluoromethylphenyl)-tetrazole
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.0083
5-bromo-1-(1-(4-hydroxy-3-methoxyphenyl)-3-oxodecan-5-yl)-pyrimidine-2,4-(1H,3H)-dione
pH 7.4, temperature not specified in the publication
0.11
5-hydroxymethyl-dUMP
-
pH and temperature not specified in the publication
0.000004
5-methoxy-2-[(2E)-4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)but-2-en-1-yl]-1H-isoindole-1,3(2H)-dione
predicted value, pH not specified in the publication, temperature not specified in the publication
0.00042
5-methyl-1-[(2Z)-4-(2-oxobenzo[cd]indol-1(2H)-yl)but-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
-
in 50 mM Tris-HCl pH 7.4, 50 mM KCl, 2 mM MgCl2, temperature not specified in the publication
0.038
5-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]pentanoic acid
-
-
0.016 - 0.122
5-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]pentanoic acid
0.0195
6-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]hexanamide
-
-
0.026
6-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]hexanamide
-
-
0.0265
6-[4-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]hexanamide
-
-
0.21
ATP
pH 7.4, temperature not specified in the publication
0.00017
N-(5'-deoxy-4-thio-alpha-D-thymidin-5'-yl)-N'-(3-trifluoromethyl-4-chlorophenyl)thiourea
-
in 50 mM Tris-HCl, pH 7.4, 50 mM KCl, 2 mM MgCl2, at 37°C
0.0026 - 0.05
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(3-trifluoromethyl-4-chlorobenzyl)thiourea
0.0019 - 0.166
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(4-chloro-3-(trifluoromethyl)phenylethyl)urea
0.036 - 0.206
[(1S,4R)-4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)cyclopent-2-en-1-yl]methyl acetate
0.039
(3E)-4-[4-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]but-3-enoic acid
-
-
0.252
(3E)-4-[4-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]but-3-enoic acid
-
-
0.001
1-(3,4-dichlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
pH 7.4
0.274
1-(3,4-dichlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
-
pH 7.4
0.005
1-(3-chloro-4-trifluoromethylphenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
pH 7.4
1
1-(3-chloro-4-trifluoromethylphenyl)-3-[[(2S,3R,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]methyl]thiourea
-
pH 7.4
0.0032
1-(4-chlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
pH 7.4
1
1-(4-chlorophenyl)-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
-
pH 7.4
0.014
1-[(1'R,4'S)-4'-((S)-2-fluoro-1-hydroxyethyl)cyclopent-2'-enyl]-1H-thymine
-
substrate TMP, pH 7.2, 30°C
0.02
1-[(1'R,4'S)-4'-((S)-2-fluoro-1-hydroxyethyl)cyclopent-2'-enyl]-1H-thymine
-
substrate dGMP, pH 7.2, 30°C
0.067
1-[(1R,2R,3S,4R)-2,3-dihydroxy-4-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
with dGMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
2.5
1-[(1R,2R,3S,4R)-2,3-dihydroxy-4-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
with TMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
0.055
1-[(1R,2R,4R,5S)-4-(hydroxymethyl)-6-oxabicyclo[3.1.0]hex-2-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
with dGMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
0.208
1-[(1R,2R,4R,5S)-4-(hydroxymethyl)-6-oxabicyclo[3.1.0]hex-2-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
with TMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
0.103
1-[(1R,3S,4R)-3-hydroxy-4-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
with dGMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
0.355
1-[(1R,3S,4R)-3-hydroxy-4-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
with TMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
0.007
1-[(1R,4S)-4-(hydroxymethyl)cyclopent-2-en-1-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
with dGMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
0.02
1-[(1R,4S)-4-(hydroxymethyl)cyclopent-2-en-1-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
with TMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
0.089
1-[(1S,3R)-3-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
with dGMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
0.246
1-[(1S,3R)-3-(hydroxymethyl)cyclopentyl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
with TMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
0.0135
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-oxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
1.1
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-oxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
0.0035
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-thioxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
0.0035
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-thioxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
pH and temperature not specified in the publication
0.7
1-[(4aR,5S,7R,7aR)-5-(hydroxymethyl)-2-thioxohexahydro-2H-furo[3,4-e][1,3]oxazin-7-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
0.0006
1-[4-chloro-3-(trifluoromethyl)phenyl]-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
pH 7.4
0.362
1-[4-chloro-3-(trifluoromethyl)phenyl]-3-[[(2R,3S,5S)-3-hydroxy-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-2-yl]methyl]thiourea
-
pH 7.4
0.024
3'-azido-3'-deoxythymidine
pH 7.4, temperature not specified in the publication
0.01
4-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
-
-
0.293
4-[4-[(5-bromo-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
-
-
0.0065
4-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
-
-
0.79
4-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]butanoic acid
-
-
0.042
5-bromo-2'-deoxyuridine
pH 7.4, temperature not specified in the publication
0.02
5-chloro-2'-deoxyuridine
pH 7.4, temperature not specified in the publication
0.016
5-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]pentanoic acid
-
-
0.122
5-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]pentanoic acid
-
-
0.23
dTDP
pH 7.4, temperature not specified in the publication
0.0011
N-(3,4-dichlorophenyl)-N'-(5'-deoxy-alpha-D-thymidin-5'-yl)-urea
pH 7.4
0.0116
N-(3,4-dichlorophenyl)-N'-(5'-deoxy-alpha-D-thymidin-5'-yl)-urea
-
pH 7.4
0.0022
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(3,4-dichlorophenylethyl)thiourea
pH 7.4
0.079
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(3,4-dichlorophenylethyl)thiourea
-
pH 7.4
0.0026
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(3-trifluoromethyl-4-chlorobenzyl)thiourea
pH 7.4
0.05
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(3-trifluoromethyl-4-chlorobenzyl)thiourea
-
pH 7.4
0.0019
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(4-chloro-3-(trifluoromethyl)phenylethyl)urea
pH 7.4
0.166
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(4-chloro-3-(trifluoromethyl)phenylethyl)urea
-
pH 7.4
0.0175
P1-(adenosine 5')-P4-(thymidine 5')-tetraphosphate
-
pH 7.5, 37°C, with dTMP as variable substrate and ATP as cosubstrate
0.0209
P1-(adenosine 5')-P4-(thymidine 5')-tetraphosphate
-
pH 7.5, 37°C, with ATP as variable substrate and dTMP as cosubstrate
0.00047
P1-(adenosine 5')-P5-(thymidine 5')-pentaphosphate
-
pH 7.5, 37°C, with dTMP as variable substrate and ATP as cosubstrate
0.0006
P1-(adenosine 5')-P5-(thymidine 5')-pentaphosphate
-
pH 7.5, 37°C, with ATP as variable substrate and dTMP as cosubstrate
0.00018
P1-(Adenosine 5')-P6-(thymidine 5')-hexaphosphate
-
pH 7.5, 37°C, with dTMP as variable substrate and ATP as cosubstrate
0.0002
P1-(Adenosine 5')-P6-(thymidine 5')-hexaphosphate
-
pH 7.5, 37°C, with ATP as variable substrate and dTMP as cosubstrate
0.036
[(1S,4R)-4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)cyclopent-2-en-1-yl]methyl acetate
-
with dGMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
0.206
[(1S,4R)-4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)cyclopent-2-en-1-yl]methyl acetate
-
with TMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000003 - 0.0000137
(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
0.0000003 - 0.0000183
(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
0.018 - 0.2
(R)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.0051 - 0.2
(R)-1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.0004 - 0.0026
(S)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.0004 - 0.0015
(S)-1-(1-(3-(3,5-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.0001 - 0.0006
(S)-1-(1-(3-(3-bromophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.001 - 0.0019
(S)-1-(1-(3-(3-chloro-4-methylphenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.0001 - 0.0021
(S)-1-(1-(3-(3-chloro-5-fluorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.00015 - 0.0012
(S)-1-(1-(3-(3-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.0004 - 0.0032
(S)-1-(1-(3-(3-fluorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.0004 - 0.0085
(S)-1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.000028
(S)-2-(3-bromophenoxy)-4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)methyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.00001
(S)-4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-piperidin-1-yl)methyl)-2-(m-tolyloxy)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0003 - 0.0027
(S)-5-methyl-1-(1-(3-(m-tolyloxy)benzyl)piperidin-3-yl)-pyrimidine-2,4(1H,3H)-dione
0.0013 - 0.035
1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.009 - 0.143
1-(1-(3-(4-methoxyphenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.138
1-(1-benzylpiperidin-4-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.00095 - 0.00096
1-(1-[[4-(3-chlorophenoxy)quinolin-2-yl]methyl]piperidin-4-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
0.328
1-(1-[[4-(dimethylamino)phenyl]methyl]piperidin-4-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.066
1-methyl-6-(pyridin-3-yl)-1H-imidazo[4,5-b]pyridin-2(3H)-one
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.152
1-methyl-6-(pyridin-4-yl)-1H-imidazo[4,5-b]pyridin-2(3H)-one
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.2
1-methyl-6-(pyrimidin-5-yl)-1H-imidazo[4,5-b]pyridin-2(3H)-one
Pseudomonas aeruginosa
IC50 above 0.2 mM, in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.058
1-methyl-6-phenyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
1.115
1-[1-(cyclohexylmethyl)piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.023
1-[1-[(1-benzofuran-2-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.0071 - 0.06045
1-[1-[(3,4-dichlorophenyl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
0.04
1-[1-[(4-chlorophenyl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.113
1-[1-[(4-methoxyphenyl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.0018
1-[1-[(7-chloro-4-phenoxyquinolin-2-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.114
1-[1-[(furan-2-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.254
1-[1-[(furan-3-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.027
1-[1-[(isoquinolin-1-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.026
1-[1-[(isoquinolin-3-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.025
1-[1-[(isoquinolin-4-yl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.00088
2-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamido)acetic acid
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0013
2-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamido)ethanesulfonic acid
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.005
2-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamido)propanoic acid
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.002
2-(3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamido)propyl)benzoic acid
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0000001 - 0.0000005
2-(3-bromophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
0.0000003 - 0.0000013
2-(3-bromophenoxy)-4-((R)-3-ethyl-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
0.0000006 - 0.0000028
2-(3-bromophenoxy)-4-((S)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
0.0000001 - 0.0000011
2-(3-bromophenoxy)-4-(R)-(2-(1-adamantane)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
0.000003
2-(3-chlorophenoxy)-3-methoxy-4-[(1S)-1-[(3S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl]propyl]benzoic acid
Staphylococcus aureus
-
temperature not specified in the publication, pH not specified in the publication
0.0000001 - 0.0000016
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)-2-(tetrahydro-2H-pyran-4-yl)ethyl)benzoic acid
0.000001 - 0.0000025
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
0.0000006 - 0.0000083
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1-(2H)-yl)piperidin-1-yl)butyl)benzoic acid
0.0000001 - 0.0000007
2-(3-chlorophenoxy)-4-((R)-2-cyclohexyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
0.0000003 - 0.0000007
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
0.0000003 - 0.000001
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
0.0000001 - 0.000003
2-(3-chlorophenoxy)-4-((R)-3-ethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
0.0000006 - 0.0000012
2-(3-chlorophenoxy)-4-((R)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
0.0000002 - 0.000018
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
0.0000006 - 0.0000293
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
0.0000002 - 0.0000135
2-(3-chlorophenoxy)-4-((S)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
0.00025
2-benzyl-3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]-pyridin-6-yl)benzamido)propanoic acid
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.012
2-{[3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzoyl]amino}-4-phenylbutanoic acid
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.00044
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.2
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzenesulfonamide
Pseudomonas aeruginosa
IC50 above 0.2 mM, in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.2
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzonitrile
Pseudomonas aeruginosa
IC50 above 0.2 mM, in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.002
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(2-(pyridin-4-yl)ethyl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.00016
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(3-(4-(trifluoromethyl)phenyl)propyl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.00051
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(3-(pyridin-3-yl)propyl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0058
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(3-morpholinopropyl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.00012
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(3-phenylpropyl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0062
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-(pyridin-2-ylmethyl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0029
3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-N-phenethylbenzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0026
3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamido)propanoic acid
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0024
3-(3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamido)propyl)benzoic acid
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0000003
4-((3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-piperidin-1-yl)methyl)-2-(3-(trifluoromethyl)phenoxy)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.2
4-(1-methyl -2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)-benzamide
Pseudomonas aeruginosa
IC50 above 0.2 mM, in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0027
4-(3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamido)propyl)benzoic acid
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.000002
4-[3-cyano-2-oxo-7-(1H-pyrazol-4-yl)-5,6-dihydro-1H-benzo[h]quinolin-4-yl]benzoic acid
Mycobacterium tuberculosis
pH 7.5, 37°C
0.00042
4-[3-cyano-6-(3-methoxyphenyl)-2-oxo-1H-pyridin-4-yl]benzoic acid
Mycobacterium tuberculosis
pH 7.5, 37°C
0.141
4-[[4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl]methyl]benzoic acid
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.035
4-[[4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl]methyl]benzonitrile
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.015 - 0.024
5-methyl-1-(1-(3-(3-(trifluoromethyl)phenoxy)benzyl)piperidin-3-yl)pyrimidine-2,4(1H,3H)-dione
0.142
5-methyl-1-(1-[[4-(1H-tetrazol-5-yl)phenyl]methyl]piperidin-4-yl)pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.72
5-methyl-1-(2-[methyl[(3-phenoxyphenyl)methyl]amino]ethyl)pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.01
5-methyl-1-[(3S)-1-[(3-phenoxyphenyl)methyl]piperidin-3-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.129
5-methyl-1-[1-(2-phenylethyl)piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.235
5-methyl-1-[1-(3-phenoxybenzoyl)piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.353
5-methyl-1-[1-(4-phenoxybenzoyl)piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.072
5-methyl-1-[1-[(3-methylphenyl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.944
5-methyl-1-[1-[(3-phenoxyphenyl)methyl]azetidin-3-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.0061
5-methyl-1-[1-[(3-phenoxyphenyl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.168
5-methyl-1-[1-[(4-methylphenyl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.029
5-methyl-1-[1-[(4-phenoxyphenyl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.0011 - 0.03251
5-methyl-1-[1-[(4-phenoxyquinolin-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
0.038
5-methyl-1-[1-[(naphthalen-1-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.02
5-methyl-1-[1-[(naphthalen-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.098
5-methyl-1-[1-[(pyridin-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.075
5-methyl-1-[1-[(pyridin-3-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.049
5-methyl-1-[1-[(pyridin-4-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.009
5-methyl-1-[1-[(quinolin-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.017
5-methyl-1-[1-[(quinolin-3-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.025
5-methyl-1-[1-[(quinolin-4-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
1.91
5-methyl-1-[1-[2-(3-phenoxyphenyl)ethyl]azetidin-3-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.011
5-methyl-1-[1-[2-(3-phenoxyphenyl)ethyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
1.14
5-methyl-1-[1-[3-(3-phenoxyphenyl)propyl]azetidin-3-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.006 - 0.059
5-methyl-1-[1-[3-(4-methylphenoxy)benzyl]piperidin-3-yl]-pyrimidine-2,4(1H,3H)-dione
0.143
5-[[4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl]methyl]pyridine-2-carboxylic acid
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.2
6-(3-(aminomethyl)phenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
Pseudomonas aeruginosa
IC50 above 0.2 mM, in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.037
6-(3-(hydroxymethyl)phenyl)-1-methyl-1H-imidazo[4,5-b]-pyridin-2(3H)-one
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.013
6-(3-acetylphenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.063
6-(3-aminophenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.2
6-(3-fluorophenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
Pseudomonas aeruginosa
IC50 above 0.2 mM, in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.011
6-(3-hydroxyphenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0049
6-(4-(aminomethyl)phenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.021
6-(4-hydroxyphenyl)-1-methyl-1H-imidazo[4,5-b]pyridin-2(3H)-one
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.14
albendazole
Wolbachia endosymbiont of Brugia malayi
pH 7.4, temperature not specified in the publication
0.02
deoxy-fluorothymidine
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.75
diethylcarbamazine
Wolbachia endosymbiont of Brugia malayi
pH 7.4, temperature not specified in the publication
0.15
ivermectin
Wolbachia endosymbiont of Brugia malayi
pH 7.4, temperature not specified in the publication
1.2
levamisole
Wolbachia endosymbiont of Brugia malayi
pH 7.4, temperature not specified in the publication
0.00037
methyl 2-(3-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]-pyridin-6-yl)benzamido)propyl)benzoate
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.104
N,N-dimethyl-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]-pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.068
N-((1H-benzo[d]imidazol-2-yl)methyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.003
N-(2-(1H-benzo[d]imidazol-2-yl)ethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0023
N-(2-(1H-imidazol-5-yl)ethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.00088
N-(2-amino-2-oxoethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0032
N-(2-aminoethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo-[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0026
N-(2-hydroxyethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo-[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0034
N-(3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)phenyl)acetamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.00099
N-(3-(1H-imidazol-4-yl)propyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0002
N-(3-(1H-indol-3-yl)propyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0022
N-(3-(3-(aminomethyl)phenyl)propyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0032
N-(3-(4-(aminomethyl)phenyl)propyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.00012
N-(3-(4-fluorophenyl)propyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.00081
N-(3-cyclopentylpropyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0021
N-(cyanomethyl)-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo-[4,5-b]pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.001
N-benzyl-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]-pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.0022
N-methyl-3-(1-methyl-2-oxo-2,3-dihydro-1H-imidazo[4,5-b]-pyridin-6-yl)benzamide
Pseudomonas aeruginosa
in 40 mM HEPES, pH 8.0, 80 mM KCl, and 1.6 mM MgCl2, at 25°C
0.018
suramin
Wolbachia endosymbiont of Brugia malayi
pH 7.4, temperature not specified in the publication
0.000003
(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0000137
(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000003
(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0000183
(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)propyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.018
(R)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.2
(R)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
IC50 above 0.2 mM, pH and temperature not specified in the publication
0.0051
(R)-1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.2
(R)-1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
IC50 above 0.2 mM, pH and temperature not specified in the publication
0.0004
(S)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0026
(S)-1-(1-(3-(3,4-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0004
(S)-1-(1-(3-(3,5-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0015
(S)-1-(1-(3-(3,5-dichlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0001
(S)-1-(1-(3-(3-bromophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0006
(S)-1-(1-(3-(3-bromophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.001
(S)-1-(1-(3-(3-chloro-4-methylphenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0019
(S)-1-(1-(3-(3-chloro-4-methylphenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0001
(S)-1-(1-(3-(3-chloro-5-fluorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0021
(S)-1-(1-(3-(3-chloro-5-fluorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.00015
(S)-1-(1-(3-(3-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0012
(S)-1-(1-(3-(3-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0004
(S)-1-(1-(3-(3-fluorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0032
(S)-1-(1-(3-(3-fluorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0004
(S)-1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0085
(S)-1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0003
(S)-5-methyl-1-(1-(3-(m-tolyloxy)benzyl)piperidin-3-yl)-pyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0027
(S)-5-methyl-1-(1-(3-(m-tolyloxy)benzyl)piperidin-3-yl)-pyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0013
1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.035
1-(1-(3-(4-chlorophenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.009
1-(1-(3-(4-methoxyphenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.143
1-(1-(3-(4-methoxyphenoxy)benzyl)piperidin-3-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.00095
1-(1-[[4-(3-chlorophenoxy)quinolin-2-yl]methyl]piperidin-4-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.00096
1-(1-[[4-(3-chlorophenoxy)quinolin-2-yl]methyl]piperidin-4-yl)-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.0071
1-[1-[(3,4-dichlorophenyl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.06045
1-[1-[(3,4-dichlorophenyl)methyl]piperidin-4-yl]-5-methylpyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.0000001
2-(3-bromophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
Streptococcus pneumoniae
-
IC50 below 0.1 nM, pH and temperature not specified in the publication
0.0000005
2-(3-bromophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000003
2-(3-bromophenoxy)-4-((R)-3-ethyl-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0000013
2-(3-bromophenoxy)-4-((R)-3-ethyl-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000006
2-(3-bromophenoxy)-4-((S)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0000028
2-(3-bromophenoxy)-4-((S)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000001
2-(3-bromophenoxy)-4-(R)-(2-(1-adamantane)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0000011
2-(3-bromophenoxy)-4-(R)-(2-(1-adamantane)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000001
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)-2-(tetrahydro-2H-pyran-4-yl)ethyl)benzoic acid
Streptococcus pneumoniae
-
IC50 below 0.1 nM, pH and temperature not specified in the publication
0.0000016
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)-2-(tetrahydro-2H-pyran-4-yl)ethyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.000001
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0000025
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000006
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1-(2H)-yl)piperidin-1-yl)butyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0000083
2-(3-chlorophenoxy)-4-((R)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1-(2H)-yl)piperidin-1-yl)butyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000001
2-(3-chlorophenoxy)-4-((R)-2-cyclohexyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
Streptococcus pneumoniae
-
IC50 below 0.1 nM, pH and temperature not specified in the publication
0.0000007
2-(3-chlorophenoxy)-4-((R)-2-cyclohexyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000003
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0000007
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)hexyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000003
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.000001
2-(3-chlorophenoxy)-4-((R)-3,3-dimethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000001
2-(3-chlorophenoxy)-4-((R)-3-ethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.000003
2-(3-chlorophenoxy)-4-((R)-3-ethyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)pentyl)benzoic acid
Staphylococcus aureus
-
IC50 below 3 nM, pH and temperature not specified in the publication
0.0000006
2-(3-chlorophenoxy)-4-((R)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0000012
2-(3-chlorophenoxy)-4-((R)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000002
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
Streptococcus pneumoniae
-
IC50 below 0.2 nM, pH and temperature not specified in the publication
0.000018
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000006
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0000293
2-(3-chlorophenoxy)-4-((S)-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)ethyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000002
2-(3-chlorophenoxy)-4-((S)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0000135
2-(3-chlorophenoxy)-4-((S)-3-methyl-1-((S)-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)piperidin-1-yl)butyl)benzoic acid
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.015
5-methyl-1-(1-(3-(3-(trifluoromethyl)phenoxy)benzyl)piperidin-3-yl)pyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.024
5-methyl-1-(1-(3-(3-(trifluoromethyl)phenoxy)benzyl)piperidin-3-yl)pyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0029
5-methyl-1-[1-(3-phenoxybenzyl)piperidin-3-yl]pyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.0034
5-methyl-1-[1-(3-phenoxybenzyl)piperidin-3-yl]pyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.124
5-methyl-1-[1-(3-phenoxybenzyl)piperidin-3-yl]pyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.156
5-methyl-1-[1-(3-phenoxybenzyl)piperidin-3-yl]pyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0011
5-methyl-1-[1-[(4-phenoxyquinolin-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.03251
5-methyl-1-[1-[(4-phenoxyquinolin-2-yl)methyl]piperidin-4-yl]pyrimidine-2,4(1H,3H)-dione
Mycobacterium tuberculosis
pH 7.4, temperature not specified in the publication
0.006
5-methyl-1-[1-[3-(4-methylphenoxy)benzyl]piperidin-3-yl]-pyrimidine-2,4(1H,3H)-dione
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
0.059
5-methyl-1-[1-[3-(4-methylphenoxy)benzyl]piperidin-3-yl]-pyrimidine-2,4(1H,3H)-dione
Staphylococcus aureus
-
pH and temperature not specified in the publication
0.0000002
TK-666
Streptococcus pneumoniae
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.7
-
pH 7.0: about 50% of maximal activity, pH 8.7: about 40% of maximal activity
7 - 9.5
-
pH 7.0: about 40% of maximal activity, pH 9.5: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
upregulation following infection with parasite Gyrodactylus salaris
brenda
-
from HIV-infected patients and healthy noninfected individuals. Enzyme activity is 10fold lower in extracts from infected as compared to uninfected persons
brenda
additional information
-
peripheral blast cell obtained from acute myelocytic leukemia patients
brenda
additional information
A0NAB2
transcription is activated during the G1/S-phase of the cell cycle. The single gene produces a longer isoform targeted to the mitochondria and a shorter cytosolic isoform
brenda
additional information
-
expression in several tissues and erythroblastoma cell lines
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
translocation to chloroplasts depends on a 72-amino-acid N-signal
brenda
-
isoform TMPK2, mitochondrial import sequence at its N-terminus and mitochondrial localization of Green Fluorescent Protein fusion protein
brenda
activity detected in the outer membrane fraction may originate from a novel dTMP kinase, distinct from the canonical TYMK
brenda
-
the enzyme is loosely bound to mitochondrial membrane
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
evolution
malfunction
Zea mays has a single TK1 (ZmTK1) gene and mutant plants are albino and display reduced genome copy number in chloroplasts
physiological function
drug target
molecular dynamics simulation and inhibitory studies show that the enzyme has structural features which suggest using it as a target to develop new anti-plasmodial drugs
drug target
the enzyme is a potential drug target for antifungal drug discovery for a number of reasons. First, it shows several structural differences compared to its human counterpart. These include the Ca-loop, as well as significant shifts in the location of helices and strands. The structural differences can form potential binding sites for allosteric inhibitors. Second, the fact the CaTMPK can utilize dGMP as a substrate suggests that competitive inhibitors that resemble purine nucleosides may preferentially bind to CaTMPK versus the human enzyme
drug target
thymidylate kinase is a key enzyme for the synthesis of DNA, making it an important target for the development of anticancer, antibacterial and antiparasitic drugs
drug target
the enzyme is indispensable for bacterial DNA biosynthesis and has been pursued for the development of new antibacterial agents including against Mycobacterium tuberculosis
drug target
-
the enzyme is indispensable for bacterial DNA biosynthesis and has been pursued for the development of new antibacterial agents including against Mycobacterium tuberculosis
-
drug target
-
thymidylate kinase is a key enzyme for the synthesis of DNA, making it an important target for the development of anticancer, antibacterial and antiparasitic drugs
-
drug target
-
the enzyme is a potential drug target for antifungal drug discovery for a number of reasons. First, it shows several structural differences compared to its human counterpart. These include the Ca-loop, as well as significant shifts in the location of helices and strands. The structural differences can form potential binding sites for allosteric inhibitors. Second, the fact the CaTMPK can utilize dGMP as a substrate suggests that competitive inhibitors that resemble purine nucleosides may preferentially bind to CaTMPK versus the human enzyme
-
evolution
study on influence of sequence evolution and conformational dynamics on its quaternary structure and function. Based on extensive sequence and structure analyses, the study detects several non-conserved residues which are linked by co-evolution and are implicated in the observed variations in flexibility, oligomeric assembly and substrate specificity among the homologs. These lead to differences in the pattern of interactions at the active site in thymidylate kinases of different specificity
evolution
-
study on influence of sequence evolution and conformational dynamics on its quaternary structure and function. Based on extensive sequence and structure analyses, the study detects several non-conserved residues which are linked by co-evolution and are implicated in the observed variations in flexibility, oligomeric assembly and substrate specificity among the homologs. These lead to differences in the pattern of interactions at the active site in thymidylate kinases of different specificity
-
physiological function
-
the enzyme is critical for the synthesis of the thymidine triphosphate precursor necessary for DNA synthesis
physiological function
-
thymidylate kinase is a key enzyme in the control of nucleotide metabolism and synthesis of DNA
physiological function
-
essential enzyme for the growth of the organism because of its critical role in the de novo synthesis of deoxythymidine 5'-diphosphate (TDP), a precursor for TTP that is required for DNA replication and repair
physiological function
critical enzyme in the de novo biosynthesis pathway of pyrimidine nucleotides
physiological function
the enzyme is indispensable for bacterial DNA biosynthesis
physiological function
key enzyme that plays an important role in DNA synthesis
physiological function
-
the enzyme is indispensable for bacterial DNA biosynthesis
-
physiological function
-
key enzyme that plays an important role in DNA synthesis
-
Show AA Sequence and Transmembrane Helices (24253 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23779
-
2 * 23779, electrospray ionization mass spectrometry, wild-type enzyme
23794
-
2 * 23794, electrospray ionization mass spectrometry, G146A mutant enzyme
24000
25000
36500
-
2 * 36500, calculated from the deduced amino acid sequence, crystal structure analysis
52000
additional information
-
thymidylate kinase is the product of the CDC8 gene
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
dimer
-
2 * 36500, calculated from the deduced amino acid sequence, crystal structure analysis
dimer
-
2 * 23779, electrospray ionization mass spectrometry, wild-type enzyme
dimer
-
2 * 23794, electrospray ionization mass spectrometry, G146A mutant enzyme
additional information
the dimeric assembly of thymidylate kinase is an absolute requirement for enzymatic activity and any subtle change in dimeric conformation due to denaturation leads to loss of enzymatic activity
additional information
-
the dimeric assembly of thymidylate kinase is an absolute requirement for enzymatic activity and any subtle change in dimeric conformation due to denaturation leads to loss of enzymatic activity
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method, the structure of thymidylate kinase from Candida albicans, determined by X-ray crystallography, 2.45 A resolution
using 100 mM Bis-Tris propane pH 7.5, 200 mM sodium sulfate, 20% (w/v) PEG 3350
crystallographic structures of the mutant F105Y enzyme in complex with either TMP or 3'-azido-3'-deoxythymidine monophosphate show that the mutation shifts the P-loop to a position that is similar to that found in the complex between Ap5dT and the wild-type enzyme
in complex with phosphorylated N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-thymine and ADP, vapor diffusion method, using 14% (w/v) PEG 3350, 0.1 M HEPES pH 7.5, at 20°C
molecular dynamics simulation of interaction with acyclic nucleoside analogue inhibitors. Key interaction of residue R95 and the distal substituent
-
vapor diffusion method using hanging-drop geometry, crystal structures of the enzyme with dTMP and ADP, dTMP and AppNHp, dTMP with ADP and AlF3, dTDP and ADP, and TP5A
-
cocrystals with 3-azido-3-deoxythymidine 5'-monophosphate and deoxythymidine
in comlplex with inhibitors 4-[3-cyano-6-(3-methoxyphenyl)-2-oxo-1H-pyridin-4-yl]benzoic acid, 4-[3-cyano-2-oxo-7-(1H-pyrazol-4-yl)-5,6-dihydro-1H-benzo[h]quinolin-4-yl]benzoic acid
modeling of enzyme-inhibitor complexes and elaboration of a QSAR model resulting in a set of proposed inhibitors
molecular dynamics simulation of interaction with acyclic nucleoside analogue inhibitors. Key interaction of residue R95 and the distal substituent
TMPK bound to TDP and to brivudin monophosphate, hanging drop vapor diffusion method
hanging drop vapor diffusion method, using 30% (w/v) PEG 4000, 0.2 M MgCl2, and 0.1 M Tris, pH 7.5-8.5, at 22°C
For the His-tagged SaTMK crystals, data is collected on beamline ID 14.1 at the ESRF (Grenoble, France).
-
The data for the untagged SaTMK crystals is collected using Cu Ka radiation from a Rigaku MicroMax 007 generator equipped with aMAR345 image plate.
-
hanging drop method, three-dimensional structure of the enzyme in its apo and ADP-bound forms
high-resolution X-ray crystal structures of thymidylate kinase in apo and ligand-bound states, structures of binary and ternary complexes of thymidylate kinase with its natural substrates ATP and ATP-TMP, respectively
to 1.83 A resolution, orthorhombic space group P212121, with unit-cell parameters a = 39.50, b = 80.29, c = 122.55 A
molecular docking studies using inhibitors (4E)-1-(4-hydroxy-3-methoxyphenyl)dec-4-en-3-one, 1-(1-(4-hydroxy-3-methoxyphenyl)-3-oxodecan-5-yl)-5-methylpyrimidine-2,4-(1H,3H)-dione, 5-bromo-1-(1-(4-hydroxy-3-methoxyphenyl)-3-oxodecan-5-yl)-pyrimidine-2,4-(1H,3H)-dione
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G146A
-
mutation is accompanied by a small but significant enhancement of the thermodynamic stability, midpoint denaturation temperature is 3°C higher than that of the wild-type enzyme, midpoint transition is 3.3 M urea, compared to 3.0 M for the wild-type enzyme
F105Y
S108A
-
mutant enzyme exhibits significantly higher Km and lower kcat for dGMP, but does not affect the overall enzyme kinetics toward TMP
S108T
-
mutation shows minimal effect on overall kinetics toward TMP but results in significantly higher Km and lower kcat toward dGMP
Y153F
-
mutant affects TMP binding. The OH of Y153F forms a direct hydrogen bond to N2 of guanine or via a bridging water molecule to O2 of thymidine
R93A
D90L
high similarity to the wild-type. Less than 10% of wild-type activity
K16M
high similarity to the wild-type. Less than 10% of wild-type activity
T18V
equivalent activity to wild-type enzyme, crystal structure of the mutant enzyme is very high similarity to the wild-type structure. Increase in thermal stability by 3.4°C
V158T
equivalent activity to wild-type enzyme, crystal structure of the mutant enzyme is very high similarity to the wild-type structure, thermal stability similar to that of wild-type enzyme
Y162F
Y92H
equivalent activity to wild-type enzyme, crystal structure of the mutant enzyme is very high similarity to the wild-type structure, significant decrease in thermal stability of 8.8 °C as compared with wild-type enzyme
Y99F
high similarity to the wild-type, activity is about 60% of the wild-type activity
D90L
-
high similarity to the wild-type. Less than 10% of wild-type activity
-
T18V
-
equivalent activity to wild-type enzyme, crystal structure of the mutant enzyme is very high similarity to the wild-type structure. Increase in thermal stability by 3.4°C
-
Y162F
-
significant decrease in thermal stability of 10 °C as compared with wild-type enzyme
-
Y92H
-
equivalent activity to wild-type enzyme, crystal structure of the mutant enzyme is very high similarity to the wild-type structure, significant decrease in thermal stability of 8.8 °C as compared with wild-type enzyme
-
Y99F
-
high similarity to the wild-type, activity is about 60% of the wild-type activity
-
additional information
F105Y
-
increase in activity and preferential specificity towards 3'-azido-3'-deoxythymidine 5'-monophosphate
F105Y
stabilization of active site dynamics leads to increased activity with 3-azido-3-deoxythymidine monophosphate for the mutant enzyme
Y162F
significant decrease in thermal stability of 10 °C as compared with wild-type enzyme
Y162F
equivalent activity to wild-type enzyme, crystal structure of the mutant enzyme is very high similarity to the wild-type structure
additional information
A0NAB2
T-DNA insertion line zeus1 contains a sporophytic zygote-lethal mutation in thymidylate kinase. In plants with targeted gene disruption, the reporter gene is preferentially expressed in cells undergoing division, but is not detected during the male and female gametophytic mitoses. Reporter gene expression is observed in mature embryo sacs prior to fertilization
additional information
-
introduction of an engineered, highly active dTMP kinase into T cells for more efficient conversion of the 3'-azido-3'-deoxythymidine prodrug to its diphosphorylated form and blocking replication of formerly 3'-azido-3'-deoxythymidine resistant HIV. Substitution of the LID domain in human enzyme by the Escherichia coli LID sequence and mutation of the P-loop Arg residue to Gly results in 100fold higher rate of 3'-azido-3'-deoxythymidine monophosphate phosphorylation than the native form. Link of mutant enzymes to the protein transduction domain of Tat for direct cell delivery
additional information
-
introduction of an engineered, highly active dTMP kinase into T cells for more efficient conversion of the 3'-azido-3'-deoxythymidine prodrug to its diphosphorylated form and blocking replication of formerly 3'-azido-3'-deoxythymidine resistant HIV. Substitution of the LID domain in human enzyme by the Escherichia coli LID sequence and mutation of the P-loop Arg residue to Gly results in 100fold higher rate of 3'-azido-3'-deoxythymidine monophosphate phosphorylation than the native form. Link of mutant enzymes to the protein transduction domain of Tat for direct cell delivery
additional information
-
engineering of enzyme/prodrug combinations for selectively inducing apoptosis in lentiviral vector-transduced cells, based on designed variants of human thymidylate kinase that effectively phosphorylate 3'-azido-3'-deoxythymidine. Recombinant lentiviral vector constructs contain either mutant F105Y of human thymidylate kinase or mutant R16G that additionally displays an exchange of 11 amino acids residues of wild-type with 13 residues from the Escherichia coli orthologue. In addition, they contain human CD19 lacking its cytoplasmic tail
additional information
-
silencing of expression in p53-/- and in p53+/+ colon cancer cells by lentiviral-based small hairpin RNA results in decrease of the dTTP pool without affecting p53 expression and generating cytotoxicity. Thymidylate kinase knock-down increases doxorubicin sensitivity dramatically in p53-proficient, p53-null HCT-116,and LoVo colon cancer cells. The decrease in the dTTP pool augments the DNA damage response and enhances apoptotic induction after exposure to low-dose doxorubicin, leading to cell death
additional information
-
expression as fusion protein with Green Fluorescent Protein in HeLa cell, mitochondrial localization. Over-expression of TMPK2 increases the steady-state level of cellular dTTP and promotes the conversion of radioactive labeled-thymidine and -dTMP to dTDP and dTTP in mitochondria
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
10 min, in absence of substrate activity decreases to 32% of the initial activity, completely stable in presence of 10 mM dTMP
57
60
65
additional information
-
the denaturation temperature of the enzyme increase by 2.9°C in the presence of 5 mM ATP and by 8°C in the presence of 5 mM dTMP
60
-
10 min, in absence of substrate activity decreases to 1% of the initial activity, partial protection in presence of 10 mM dTMP
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dissociation of the native dimeric species of the enzyme occurs at an urea concentration of around 4 M, leading to the accumulation of partially folded monomers that unfold totally at urea concentrations above 5.5 M
-
midpoint transition is 3.0 M urea for the wild-type enzyme and 3.3 M for the G146A mutant enzyme
-
the canonical enzyme is stable and its activity is not affected by the presence of NaCl
the enzyme from outer mitochondrial membrane is unstable and loses activity rapidly, it also loses activity in the presence of a high concentration of NaCl
the enzyme is very labile and can be stabilized for long periods of time by its substrate thymidine 5'-monophosphate in the presence of 2-mercaptoethanol
-
the enzyme is very unstable and may be stabilized in the presence of 2-mercaptoethanol with dTMP, dTDP, or ADP but not with ATP, MgATP2- or mercaptoethanol alone
-
the stability of the enzyme is maintained during purification by the constant presence of dTMP and 2-mercaptoethanol and by the elimination of substrate-destoying phosphatase activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose column chromatography and Mono Q column chromatography
-
nickel HisTrap column chromatography and Superdex 75 gel filtration
partial
the stability of the enzyme is maintained during purification by the constant presence of dTMP and 2-mercaptoethanol and by the elimination of substrate-destoying phosphatase activity
-
truncated recombinant enzyme, full length enzyme could not be crystallized
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression of wild-type enzyme and G146A variant in Escherichia coli BL21(DE3)/pDIA17
-
full length and truncated enzyme lacking the first 22 amino acids expressed in Escherichia coli BL21 C41 (DE3)
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
guanidine hydrochloride and urea-induced unfolding of thymidylate kinase is noncooperative and influences the functional properties of the enzyme much less than their Cm values. Thymidylate kinase is more prone to ionic perturbation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
additional information
-
Mycobacterium tuberculosis thymidine monophosphate kinase (TMPKmt) recently emerged as a potentially attractive target for the design of a novel class of antituberculosis agents.
drug development
potential target for the development of new antituberculosis drugs due to the low sequence similarity with the human enzyme
drug development
potential target for the development of antituberculosis drugs
drug development
potential target for antituberculosis drugs
drug development
-
potential target for the development of new antituberculosis drugs due to the low sequence similarity with the human enzyme
drug development
-
potential targets for the development of antiviral and cancer therapies
medicine
the enzyme is a promising target for developing drugs against tuberculosis because the configuration of its active site is unique in the TMPK family
medicine
-
introduction of an engineered, highly active dTMP kinase into T cells for more efficient conversion of the 3'-azido-3'-deoxythymidine prodrug to its diphosphorylated form and blocking replication of formerly 3'-azido-3'-deoxythymidine resistant HIV. Combined treatment of HIV-infected T-cells with 3'-azido-3'-deoxythymidine and the engineered thymidylate kinases restores 3'-azido-3'-deoxythymidine-induced repression of viral production
medicine
-
enzyme/prodrug combination for selectively inducing apoptosis in lentiviral vector-transduced cells, based on designed variants of human thymidylate kinase that effectively phosphorylate 3'-azido-3'-deoxythymidine. Mechanism involves apoptosis induction via disruption of the inner membrane potential and activation of caspase-3. Low-dose 3'-azido-3'-deoxythymidine administration to non-obese diabetic/severe combined immunodeficiency mice injected with the engineered cells suppresses tumor growth
medicine
-
introduction of an engineered, highly active dTMP kinase into T cells for more efficient conversion of the 3'-azido-3'-deoxythymidine prodrug to its diphosphorylated form and blocking replication of formerly 3'-azido-3'-deoxythymidine resistant HIV. Combined treatment of HIV-infected T-cells with 3'-azido-3'-deoxythymidine and the engineered thymidylate kinases restores 3'-azido-3'-deoxythymidine-induced repression of viral production
medicine
-
silencing of expression in p53-/- and in p53+/+ colon cancer cells by lentiviral-based small hairpin RNA results in decrease of the dTTP pool without affecting p53 expression and generating cytotoxicity. Thymidylate kinase knock-down increases doxorubicin sensitivity dramatically in p53-proficient, p53-null HCT-116,and LoVo colon cancer cells. The decrease in the dTTP pool augments the DNA damage response and enhances apoptotic induction after exposure to low-dose doxorubicin, leading to cell death
medicine
-
bystander cell killing contributes to tumor regression in a xenograft model relying on the delivery of expression of the thymidylate kinase suicide gene into tumors via direct intratumoral injection of recombinant therapeutic lentivirus. The thymidylate kinase/azidothymidine enzyme-prodrug axis can be effectively utilized in suicide gene therapy of solid tumors
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bone, R.; Cheng, Y.C.; Wolfenden, R.
Inhibition of adenosine and thymidylate kinases by bisubstrate analogs
J. Biol. Chem.
261
16410-16413
1986
Homo sapiens
brenda
Kielley, R.K.
Purification and properties of thymidine monophosphate kinase from mouse hepatoma
J. Biol. Chem.
245
4204-4212
1970
Mus musculus
brenda
Tamiya, N.; Yusa, T.; Yamaguchi, Y.; Tsukifuji, R.; Kuroiwa, N.; Moriyama, Y.; Fujimura, S.
Co-purification of thymidylate kinase and cytosolic thymidine kinase from human term placenta by affinity chromatography
Biochim. Biophys. Acta
995
28-35
1989
Homo sapiens
brenda
Jong, A.Y.S.; Campbell, J.L.
Characterization of Saccharomyces cerevisiae thymidylate kinase, the CDC8 gene product. General properties, kinetic analysis, and subcellular localization
J. Biol. Chem.
259
14394-14398
1984
Saccharomyces cerevisiae
brenda
Chen, M.C.; Walker, J.; Prusoff, W.H.
Kinetic studies of herpes simplex virus type 1-encoded thymidine and thymidylate kinase, a multifunctional enzyme
J. Biol. Chem.
254
10747-10753
1979
Human alphaherpesvirus 1
brenda
Lee, L.S.; Cheng, Y.C.
Human thymidylate kinase. Purification, characterization, and kinetic behavior of the thymidylate kinase derived from chronic myelocytic leukemia
J. Biol. Chem.
252
5686-5691
1977
Homo sapiens
brenda
Smith, L.K.; Eakin, R.E.
Partial purification and characterization of thymidylate kinase from embryonic chick liver
Arch. Biochem. Biophys.
167
61-71
1975
Gallus gallus
brenda
Rossi, M.; Woodward, D.O.
Enzymes of deoxythymidine triphosphate biosynthesis in Neurospora crassa mitochondria
J. Bacteriol.
121
640-647
1975
Neurospora crassa
brenda
Cheng, Y.C.; Prusoff, W.H.
Mouse ascites sarcoma 180 thymidylate kinase. General properties, kinetic analysis, and inhibition studies
Biochemistry
12
2612-2619
1973
Mus musculus
brenda
de Groot, E.J.; Schweiger, H.G.
Thymidylate kinase from Acetabularia. I. Properties of the enzyme
J. Cell Sci.
64
13-25
1983
Acetabularia acetabulum
brenda
Nelson, D.J.; Carter, C.E.
Purification and characterization of Thymidine 5-monophosphate kinase from Escherichia coli B
J. Biol. Chem.
244
5254-5262
1969
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Jong, A.Y.S.; Kuo, C.l.; Campbell, J.L.
The CDC8 gene of yeast encodes thymidylate kinase
J. Biol. Chem.
259
11052-11059
1984
Saccharomyces cerevisiae
brenda
Ostermann, N.; Segura-Pena, D.; Meier, C.; Veit, T.; Monnerjahn, C.; Konrad, M.; Lavie, A.
Structures of human thymidylate kinase in complex with prodrugs: implications for the structure-based design of novel compounds
Biochemistry
42
2568-2577
2003
Homo sapiens (P23919), Homo sapiens
brenda
Chenal-FRancisque, V.; Tourneux, L.; carniel, E.; Christova, P.; de la Sierra, I.; Barzu, O.; Gilles, A.M.
The highly similar TMP kinase of Yersinia pestis and Escherichia coli differ markedly in their ATTMP phosphorylating activity
Eur. J. Biochem.
265
112-119
1999
Escherichia coli, Yersinia pestis
brenda
Tourneux, L.; Bucurenci, N.; Lascu, I.; sakamoto, H.; Briand, G.; Gilles, A.M.
Substitution of an alanine residue for glycine 146 in TMP kinase from Escherichia coli is responsible for bacterial hypersensitivity to bromodeoxyuridine
J. Bacteriol.
180
4291-4293
1998
Escherichia coli
brenda
Petit, C.M.; Koretke, K.K.
Characterization of Streptococcus pneumoniae thymidylate kinase: steady-state kinetics of the forward reaction and isothermal titration calorimetry
Biochem. J.
363
825-831
2002
Streptococcus pneumoniae
brenda
Fioravanti, E.; Haouz, A.; Ursby, T.; Munier-Lehmann, H.; Delarue, M.; Bourgeois, D.
Mycobacterium tuberculosis thymidylate kinase: structural studies of intermediates along the reaction pathway
J. Mol. Biol.
327
1077-1092
2003
Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis
brenda
terentyev, L.L.; Terentyeva, N.A.; Rasskazov, V.A.
Purification and some properties of thymidylate kinase from sea urchin
Biochemistry
64
80-85
1999
Strongylocentrotus intermedius
brenda
Jacobsson, B.; Britton, S.; Trnevik, Y.; Eriksson, S.
Decreas in thymidylate kinase activity in peripheral blood mononuclear cells from HIV-infected individuals
Biochem. Pharmacol.
56
389-395
1998
Homo sapiens
brenda
Munier-lehmann, H.; Chaffotte, A.; Pochet, S.; Labesse, G.
Thymidylate kinase of Mycobacterium tuberculosis: a chimera sharing properties common to eukaryotic and bacterial enzymes
Protein Sci.
10
1195-1205
2001
Mycobacterium tuberculosis
brenda
Ostermann, N.; Schlichting, I.; Brundiers, R.; Konrad, M.; Reinstein, J.; Veit, T.; Goody, R.S.; Lavie, A.
Insights into the phosphoryltransfer mechanism of human thymidylate kinase gained from crystal structures of enzyme complexes along the reaction coordinate
Structure
8
629-642
2000
Homo sapiens
brenda
Fioravanti, E.; Adam, V.; Munier-Lehmann, H.; Bourgeois, D.
The crystal structure of Mycobacterium tuberculosis thymidylate kinase in complex with 3'-azidodeoxythymidine monophosphate suggests a mechanism for competitive inhibition
Biochemistry
44
130-137
2005
Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis
brenda
Pochet, S.; Dugue, L.; Labesse, G.; Delepierre, M.; Munier-Lehmann, H.
Comparative study of purine and pyrimidine nucleoside analogues acting on the thymidylate kinases of Mycobacterium tuberculosis and of humans
ChemBioChem
4
742-747
2003
Mycobacterium tuberculosis, Homo sapiens
brenda
Haouz, A.; Vanheusden, V.; Munier-Lehmann, H.; Froeyen, M.; Herdewijn, P.; Van Calenbergh, S.; Delarue, M.
Enzymatic and structural analysis of inhibitors designed against Mycobacterium tuberculosis thymidylate kinase. New insights into the phosphoryl transfer mechanism
J. Biol. Chem.
278
4963-4971
2003
Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis
brenda
Vanheusden, V.; Munier-Lehmann, H.; Froeyen, M.; Busson, R.; Rozenski, J.; Herdewijn, P.; Van Calenbergh, S.
Discovery of bicyclic thymidine analogues as selective and high-affinity inhibitors of Mycobacterium tuberculosis thymidine monophosphate kinase
J. Med. Chem.
47
6187-6194
2004
Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis, Homo sapiens
brenda
Lavie, A.; Konrad, M.
Structural requirements for efficient phosphorylation of nucleotide analogs by human thymidylate kinase
Mini Rev. Med. Chem.
4
351-359
2004
Homo sapiens
brenda
Munier-Lehmann, H.; Pochet, S.; Dugue, L.; Dutruel, O.; Labesse, G.; Douget, D.
Design of Mycobacterium tuberculosis thymidine monophosphate kinase inhibitors
Nucleosides Nucleotides Nucleic Acids
22
801-804
2003
Mycobacterium tuberculosis
brenda
Gardberg, A.; Shuvalova, L.; Monnerjahn, C.; Konrad, M.; Lavie, A.
Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases
Structure
11
1265-1277
2003
Equid alphaherpesvirus 4, Herpes simplex virus
brenda
Van Daele, I.; Munier-Lehmann, H.; Hendrickx, P.M.; Marchal, G.; Chavarot, P.; Froeyen, M.; Qing, L.; Martins, J.C.; Van Calenbergh, S.
Synthesis and biological evaluation of bicyclic nucleosides as inhibitors of M. tuberculosis thymidylate kinase
ChemMedChem
1
1081-1090
2006
Mycobacterium tuberculosis, Mycobacterium tuberculosis variant bovis
brenda
Alexandre, J.A.; Roy, B.; Topalis, D.; Pochet, S.; Perigaud, C.; Deville-Bonne, D.
Enantioselectivity of human AMP, dTMP and UMP-CMP kinases
Nucleic Acids Res.
35
4895-4904
2007
Homo sapiens (P23919)
brenda
Kotaka, M.; Dhaliwal, B.; Ren, J.; Nichols, C.E.; Angell, R.; Lockyer, M.; Hawkins, A.R.; Stammers, D.K.
Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding
Protein Sci.
15
774-784
2006
Staphylococcus aureus
brenda
Gasse, C.; Douguet, D.; Huteau, V.; Marchal, G.; Munier-Lehmann, H.; Pochet, S.
Substituted benzyl-pyrimidines targeting thymidine monophosphate kinase of Mycobacterium tuberculosis: synthesis and in vitro anti-mycobacterial activity
Bioorg. Med. Chem.
16
6075-6085
2008
Homo sapiens, Mycobacterium tuberculosis
brenda
Hu, C.M.; Chang, Z.F.
Synthetic lethality by lentiviral short hairpin RNA silencing of thymidylate kinase and doxorubicin in colon cancer cells regardless of the p53 status
Cancer Res.
68
2831-2840
2008
Homo sapiens
brenda
Familiar, O.; Munier-Lehmann, H.; Negri, A.; Gago, F.; Douguet, D.; Rigouts, L.; Hernandez, A.I.; Camarasa, M.J.; Perez-Perez, M.J.
Exploring acyclic nucleoside analogues as inhibitors of Mycobacterium tuberculosis thymidylate kinase
ChemMedChem
3
1083-1093
2008
Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis, Homo sapiens
brenda
Collins, C.M.; Olstad, K.; Sterud, E.; Jones, C.S.; Noble, L.R.; Mo, T.A.; Cunningham, C.O.
Isolation of a novel fish thymidylate kinase gene, upregulated in Atlantic salmon (Salmo salar L.) following infection with the monogenean parasite Gyrodactylus salaris
Fish Shellfish Immunol.
23
793-807
2007
Salmo salar
brenda
Chen, Y.L.; Lin, D.W.; Chang, Z.F.
Identification of a putative human mitochondrial thymidine monophosphate kinase associated with monocytic/macrophage terminal differentiation
Genes Cells
13
679-689
2008
Homo sapiens
brenda
Kandeel, M.; Kitade, Y.
Molecular characterization, heterologous expression and kinetic analysis of recombinant Plasmodium falciparum thymidylate kinase
J. Biochem.
144
245-250
2008
Plasmodium falciparum
brenda
Lavie, A.; Su, Y.; Ghassemi, M.; Novak, R.M.; Caffrey, M.; Sekulic, N.; Monnerjahn, C.; Konrad, M.; Cook, J.L.
Restoration of the antiviral activity of 3'-azido-3'-deoxythymidine (AZT) against AZT-resistant human immunodeficiency virus by delivery of engineered thymidylate kinase to T cells
J. Gen. Virol.
89
1672-1679
2008
Escherichia coli, Homo sapiens
brenda
Van Daele, I.; Munier-Lehmann, H.; Froeyen, M.; Balzarini, J.; Van Calenbergh, S.
Rational design of 5-thiourea-substituted alpha-thymidine analogues as thymidine monophosphate kinase inhibitors capable of inhibiting mycobacterial growth
J. Med. Chem.
50
5281-5292
2007
Homo sapiens, Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis
brenda
Sato, T.; Neschadim, A.; Konrad, M.; Fowler, D.H.; Lavie, A.; Medin, J.A.
Engineered human tmpk/AZT as a novel enzyme/prodrug axis for suicide gene therapy
Mol. Ther.
15
962-970
2007
Homo sapiens
brenda
Byun, Y.; Vogel, S.R.; Phipps, A.J.; Carnrot, C.; Eriksson, S.; Tiwari, R.; Tjarks, W.
Synthesis and Biological Evaluation of Inhibitors of Thymidine Monophosphate Kinase from Bacillus anthracis
Nucleosides Nucleotides Nucleic Acids
27
244-260
2008
Bacillus anthracis
brenda
Ronceret, A.; Gadea-Vacas, J.; Guilleminot, J.; Lincker, F.; Delorme, V.; Lahmy, S.; Pelletier, G.; Chaboute, M.E.; Devic, M.
The first zygotic division in Arabidopsis requires de novo transcription of thymidylate kinase
Plant J.
53
776-789
2008
Arabidopsis thaliana (A0NAB2)
brenda
Carnrot, C.; Wang, L.; Topalis, D.; Eriksson, S.
Mechanisms of substrate selectivity for Bacillus anthracis thymidylate kinase
Protein Sci.
17
1486-1493
2008
Bacillus anthracis (Q81W11), Bacillus anthracis
brenda
Hu, C.M.; Chang, Z.F.
A bioluminescent method for measuring thymidylate kinase activity suitable for high-throughput screening of inhibitor
Anal. Biochem.
398
269-271
2010
Homo sapiens
brenda
Chien, C.Y.; Chen, B.R.; Chou, C.K.; Sclafani, R.A.; Su, J.Y.
The yeast Cdc8 exhibits both deoxythymidine monophosphate and diphosphate kinase activities
FEBS Lett.
583
2281-2286
2009
Saccharomyces cerevisiae
brenda
Andrade, C.H.; Pasqualoto, K.F.; Ferreira, E.I.; Hopfinger, A.J.
Rational design and 3D-pharmacophore mapping of 5'-thiourea-substituted alpha-thymidine analogues as mycobacterial TMPK inhibitors
J. Chem. Inf. Model.
49
1070-1078
2009
Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis
brenda
Kohler, J.J.; Hosseini, S.H.; Cucoranu, I.; Zhelyabovska, O.; Green, E.; Ivey, K.; Abuin, A.; Fields, E.; Hoying, A.; Russ, R.; Santoianni, R.; Raper, C.M.; Yang, Q.; Lavie, A.; Lewis, W.
Transgenic cardiac-targeted overexpression of human thymidylate kinase
Lab. Invest.
90
383-390
2010
Homo sapiens
brenda
Kandeel, M.; Kato, A.; Kitamura, Y.; Kitade, Y.
Thymidylate kinase: the lost chemotherapeutic target
Nucleic Acids Symp. Ser.
53
283-284
2009
Plasmodium falciparum, Anaplasma marginale
brenda
Meyer, P.; Caillat, C.; Topalis, D.; Balzarini, J.; Deville-Bonne, D.
Structural basis for the specificity of thymidylate kinases from human pathogens: implications for nucleotide analogues activation
Nucleic Acids Symp. Ser.
53
41
2009
unidentified poxvirus
brenda
Caillat, C.; Topalis, D.; Agrofoglio, L.A.; Pochet, S.; Balzarini, J.; Deville-Bonne, D.; Meyer, P.
Crystal structure of poxvirus thymidylate kinase: an unexpected dimerization has implications for antiviral therapy
Proc. Natl. Acad. Sci. USA
105
16900-16905
2008
Orthopoxvirus vaccinia (P68693)
brenda
Wayengera, M.
Theoretical basis for reducing time-lines to the determination of positive Mycobacterium tuberculosis cultures using thymidylate kinase (TMK) assays
Theor. Biol. Med. Model.
6
4-4
2009
Mycobacterium tuberculosis
brenda
Leibly, D.J.; Abendroth, J.; Bryan, C.M.; Sankaran, B.; Kelley, A.; Barrett, L.K.; Stewart, L.; Van Voorhis, W.C.
Structure of thymidylate kinase from Ehrlichia chaffeensis
Acta Crystallogr. Sect. F
67
1090-1094
2011
Ehrlichia chaffeensis (Q2GHN3)
brenda
Kandeel, M.; Kitade, Y.
The substrate binding preferences of Plasmodium thymidylate kinase
Biol. Pharm. Bull.
34
173-176
2011
Plasmodium falciparum
brenda
Van Poecke, S.; Munier-Lehmann, H.; Helynck, O.; Froeyen, M.; Van Calenbergh, S.
Synthesis and inhibitory activity of thymidine analogues targeting Mycobacterium tuberculosis thymidine monophosphate kinase
Bioorg. Med. Chem.
19
7603-7611
2011
Mycobacterium tuberculosis
brenda
Toti, K.S.; Verbeke, F.; Risseeuw, M.D.; Frecer, V.; Munier-Lehmann, H.; Van Calenbergh, S.
Synthesis and evaluation of 5-modified thymidines and 5-hydroxymethyl-2-deoxyuridines as Mycobacterium tuberculosis thymidylate kinase inhibitors
Bioorg. Med. Chem.
21
257-268
2013
Mycobacterium tuberculosis
brenda
Familiar, O.; Munier-Lehmann, H.; Ainsa, J.A.; Camarasa, M.J.; Perez-Perez, M.J.
Design, synthesis and inhibitory activity against Mycobacterium tuberculosis thymidine monophosphate kinase of acyclic nucleoside analogues with a distal imidazoquinolinone
Eur. J. Med. Chem.
45
5910-5918
2010
Mycobacterium tuberculosis
brenda
Topalis, D.; Pradere, U.; Roy, V.; Caillat, C.; Azzouzi, A.; Broggi, J.; Snoeck, R.; Andrei, G.; Lin, J.; Eriksson, S.; Alexandre, J.A.; El-Amri, C.; Deville-Bonne, D.; Meyer, P.; Balzarini, J.; Agrofoglio, L.A.
Novel antiviral C5-substituted pyrimidine acyclic nucleoside phosphonates selected as human thymidylate kinase substrates
J. Med. Chem.
54
222-232
2011
Homo sapiens (P23919), Homo sapiens
brenda
Martinez-Botella, G.; Breen, J.N.; Duffy, J.E.; Dumas, J.; Geng, B.; Gowers, I.K.; Green, O.M.; Guler, S.; Hentemann, M.F.; Hernandez-Juan, F.A.; Joseph-McCarthy, D.; Kawatkar, S.; Larsen, N.A.; Lazari, O.; Loch, J.T.; Macritchie, J.A.; McKenzie, A.R.; Newman, J.V.; Olivier, N.B.; Otterson, L.G.; Owens, A.P.
Discovery of selective and potent inhibitors of gram-positive bacterial thymidylate kinase (TMK)
J. Med. Chem.
55
10010-10021
2012
Staphylococcus aureus, Streptococcus pneumoniae
brenda
Choi, J.Y.; Plummer, M.S.; Starr, J.; Desbonnet, C.R.; Soutter, H.; Chang, J.; Miller, J.R.; Dillman, K.; Miller, A.A.; Roush, W.R.
Structure guided development of novel thymidine mimetics targeting Pseudomonas aeruginosa thymidylate kinase: from hit to lead generation
J. Med. Chem.
55
852-870
2012
Pseudomonas aeruginosa (Q9HZN8)
brenda
Kumar, M.; Sharma, S.; Srinivasan, A.; Singh, T.P.; Kaur, P.
Structure-based in-silico rational design of a selective peptide inhibitor for thymidine monophosphate kinase of Mycobacterium tuberculosis
J. Mol. Model.
17
1173-1182
2011
Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis
brenda
Kato, A.; Yasuda, Y.; Kitamura, Y.; Kandeel, M.; Kitade, Y.
Carbocyclic thymidine derivatives efficiently inhibit Plasmodium falciparum thymidylate kinase (PfTMK)
Parasitol. Int.
61
501-503
2012
Plasmodium falciparum
brenda
Guevara-Hernandez, E.; Garcia-Orozco, K.D.; Sotelo-Mundo, R.R.
Biochemical characterization of thymidine monophosphate kinase from white spot syndrome virus: a functional domain from the viral ORF454
Protein Pept. Lett.
19
1220-1224
2012
white spot syndrome virus
brenda
Chaudhary, S.K.; Jeyakanthan, J.; Sekar, K.
Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of thymidylate kinase (TTHA1607) from Thermus thermophilus HB8
Acta Crystallogr. Sect. F
69
118-121
2013
Thermus thermophilus (Q5SHX3), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SHX3)
brenda
Doharey, P.K.; Suthar, M.K.; Verma, A.; Kumar, V.; Yadav, S.; Balaramnavar, V.M.; Rathaur, S.; Saxena, A.K.; Siddiqi, M.I.; Saxena, J.K.
Molecular cloning and characterization of Brugia malayi thymidylate kinase
Acta Trop.
133
83-92
2014
Wolbachia endosymbiont of Brugia malayi (Q5GTD5), Wolbachia endosymbiont of Brugia malayi TRS (Q5GTD5)
brenda
Singh, V.K.; Doharey, P.K.; Kumar, V.; Saxena, J.K.; Siddiqi, M.I.; Rathaur, S.; Narender, T.
Synthesis, molecular docking and Brugia malayi thymidylate kinase (BmTMK) enzyme inhibition study of novel derivatives of [6]-shogaol
Eur. J. Med. Chem.
93
74-82
2015
Wolbachia endosymbiont of Brugia malayi (Q5GTD5), Wolbachia endosymbiont of Brugia malayi TRS (Q5GTD5)
brenda
Doharey, P.K.; Singh, S.K.; Verma, P.; Verma, A.; Rathaur, S.; Saxena, J.K.
Insights into the structure-function relationship of Brugia malayi thymidylate kinase (BmTMK)
Int. J. Biol. Macromol.
88
565-571
2016
Wolbachia endosymbiont of Brugia malayi (Q5GTD5), Wolbachia endosymbiont of Brugia malayi TRS (Q5GTD5)
brenda
Guevara-Hernandez, E.; Arvizu-Flores, A.A.; Lugo-Sanchez, M.E.; Velazquez-Contreras, E.F.; Castillo-Yanez, F.J.; Brieba, L.G.; Sotelo-Mundo, R.R.
A novel viral thymidylate kinase with dual kinase activity
J. Bioenerg. Biomembr.
47
431-440
2015
white spot syndrome virus
brenda
Kawatkar, S.P.; Keating, T.A.; Olivier, N.B.; Breen, J.N.; Green, O.M.; Guler, S.Y.; Hentemann, M.F.; Loch, J.T.; McKenzie, A.R.; Newman, J.V.; Otterson, L.G.; Martinez-Botella, G.
Antibacterial inhibitors of Gram-positive thymidylate kinase: structure-activity relationships and chiral preference of a new hydrophobic binding region
J. Med. Chem.
57
4584-4597
2014
Staphylococcus aureus
brenda
Naik, M.; Raichurkar, A.; Bandodkar, B.S.; Varun, B.V.; Bhat, S.; Kalkhambkar, R.; Murugan, K.; Menon, R.; Bhat, J.; Paul, B.; Iyer, H.; Hussein, S.; Tucker, J.A.; Vogtherr, M.; Embrey, K.J.; McMiken, H.; Prasad, S.; Gill, A.; Ugarkar, B.G.; Venkatraman, J.; Read, J.; Panda, M.
Structure guided lead generation for M. tuberculosis thymidylate kinase (Mtb TMK): discovery of 3-cyanopyridone and 1,6-naphthyridin-2-one as potent inhibitors
J. Med. Chem.
58
753-766
2015
Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis H37Rv (P9WKE1)
brenda
Noguchi, Y.; Yasuda, Y.; Tashiro, M.; Kataoka, T.; Kitamura, Y.; Kandeel, M.; Kitade, Y.
Synthesis of carbocyclic pyrimidine nucleosides and their inhibitory activities against Plasmodium falciparum thymidylate kinase
Parasitol. Int.
62
368-371
2013
Plasmodium falciparum
brenda
Sato, T.; Neschadim, A.; Lavie, A.; Yanagisawa, T.; Medin, J.A.
The engineered thymidylate kinase (TMPK)/AZT enzyme-prodrug axis offers efficient bystander cell killing for suicide gene therapy of cancer
PLoS ONE
8
e78711
2013
Homo sapiens
brenda
Keita, M.; Kumar, A.; Dali, B.; Megnassan, E.; Siddiqi, M.; Frecer, V.; Miertus, S.
Quantitative structure-activity relationships and design of thymine-like inhibitors of thymidine monophosphate kinase of Mycobacterium tuberculosis with favourable pharmacokinetic profiles
RSC Adv.
4
55853-55866
2014
Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis H37Rv (P9WKE1)
-
brenda
Fucci, I.J.; Sinha, K.; Rule, G.S.
Stabilization of active site dynamics leads to increased activity with 3-azido-3-deoxythymidine monophosphate for F105Y mutant human thymidylate kinase
ACS Omega
5
2355-2367
2020
Homo sapiens (P23919)
brenda
Chaudhary, S.K.; Jeyakanthan, J.; Sekar, K.
Structural and functional roles of dynamically correlated residues in thymidylate kinase
Acta Crystallogr. Sect. D
74
341-354
2018
Thermus thermophilus (Q5SHX3), Thermus thermophilus ATCC 27634 (Q5SHX3)
brenda
Sinha, K.; Rule, G.S.
The structure of thymidylate kinase from Candida albicans reveals a unique structural element
Biochemistry
56
4360-4370
2017
Candida albicans (Q59TV7), Candida albicans ATCC MYA-2876 (Q59TV7)
brenda
Chen, M.D.; Sinha, K.; Rule, G.S.; Ly, D.H.
Interaction of alpha-thymidine inhibitors with thymidylate kinase from Plasmodium falciparum
Biochemistry
57
2868-2875
2018
Plasmodium falciparum (Q8I4S1), Plasmodium falciparum
brenda
Chen, M.D.; Fucci, I.J.; Sinha, K.; Rule, G.S.
dGMP binding to thymidylate kinase from Plasmodium falciparum shows half-site binding and induces protein dynamics at the dimer interface
Biochemistry
59
694-703
2020
Plasmodium falciparum
brenda
Biswas, A.; Jasti, S.; Jeyakanthan, J.; Sekar, K.
Role of sequence evolution and conformational dynamics in the substrate specificity and oligomerization mode of thymidylate kinases
J. Biomol. Struct. Dyn.
35
2136-2154
2017
Sulfurisphaera tokodaii (Q970Q8), Sulfurisphaera tokodaii DSM 16993 (Q970Q8)
brenda
Song, L.; Merceron, R.; Gracia, B.; Quintana, A.L.; Risseeuw, M.D.P.; Hulpia, F.; Cos, P.; Ainsa, J.A.; Munier-Lehmann, H.; Savvides, S.N.; Van Calenbergh, S.
Structure guided lead generation toward nonchiral M. tuberculosis thymidylate kinase inhibitors
J. Med. Chem.
61
2753-2775
2018
Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis (A5U7S1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WKE1)
brenda
Biswas, A.; Shukla, A.; Vijayan, R.S.K.; Jeyakanthan, J.; Sekar, K.
Crystal structures of an archaeal thymidylate kinase from Sulfolobus tokodaii provide insights into the role of a conserved active site arginine residue
J. Struct. Biol.
197
236-249
2017
Sulfurisphaera tokodaii (Q970Q8), Sulfurisphaera tokodaii DSM 16993 (Q970Q8)
brenda
Frisk, J.H.; Eriksson, S.; Pejler, G.; Wang, L.
Identification of a novel thymidylate kinase activity
Nucleosides Nucleotides Nucleic Acids
39
1359-1368
2020
Homo sapiens, Homo sapiens (P23919)
brenda
Najera-Martinez, M.; Pedroza-Garcia, J.; Suzuri-Hernandez, L.; Mazubert, C.; Drouin-Wahbi, J.; Vazquez-Ramos, J.; Raynaud, C.; Plasencia, J.
Maize thymidine kinase activity is present throughout plant development and its heterologous expression confers tolerance to an organellar DNA-damaging agent
Plants (Basel)
9
1-14
2020
Zea mays (B0R217)
brenda
Kandeel, M.; Kitade, Y.; Al-Taher, A.; Al-Nazawi, M.
The structural basis of unique substrate recognition by Plasmodium thymidylate kinase Molecular dynamics simulation and inhibitory studies
PLoS ONE
14
e0212065
2019
Plasmodium falciparum (Q8I4S1), Plasmodium falciparum
brenda
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