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ATP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-monophosphate
ADP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-diphosphate
-
-
-
?
ATP + 3'-amino-3'-deoxythymidine 5'-monophosphate
ADP + 3'-amino-3'-deoxythymidine 5'-diphosphate
-
-
-
?
ATP + 3'-azido-2',3'-dideoxythymidine monophosphate
ADP + 3'-azido-2',3'-dideoxythymidine diphosphate
-
-
-
?
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
-
-
-
?
ATP + 5-bromo-dUMP
ADP + 5-bromo-dUDP
-
-
-
?
ATP + dUMP
ADP + dUDP
-
-
-
?
ATP + N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-thymine
ADP + ?
-
-
-
?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
ADP + ?
-
-
-
?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-fluorouracil
ADP + ?
-
-
-
?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-thymine
ADP + ?
-
-
-
?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-uracil
ADP + ?
-
-
-
?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-bromouracil
ADP + ?
-
-
-
?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-chlorouracil
ADP + ?
-
-
-
?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-fluorouracil
ADP + ?
-
-
-
?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-thymine
ADP + ?
-
-
-
?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-uracil
ADP + ?
-
-
-
?
ATP + TMP
ADP + TDP
-
-
-
?
CTP + dTMP
CDP + dTDP
-
56% of the activity with ATP
-
-
?
D-dTMP + ATP
D-dTDP + ADP
-
-
-
?
dCTP + dTMP
dCDP + dTDP
-
45% of the activity with ATP
-
-
?
L-dTMP + ATP
L-dTDP + ADP
-
-
-
?
UTP + dTMP
UDP + dTDP
-
60% of the activity with ATP
-
-
?
additional information
?
-
ATP + 3'-azido-3'-deoxythymidine 5'-monophosphate
ADP + 3'-azido-3'-deoxythymidine 5'-diphosphate
-
-
-
?
ATP + 3'-azido-3'-deoxythymidine 5'-monophosphate
ADP + 3'-azido-3'-deoxythymidine 5'-diphosphate
-
i.e. AZT
-
-
?
ATP + 3'-azido-3'-deoxythymidine monophosphate
ADP + 3'-azido-3'-deoxythymidine diphosphate
-
-
-
-
?
ATP + 3'-azido-3'-deoxythymidine monophosphate
ADP + 3'-azido-3'-deoxythymidine diphosphate
-
-
-
?
ATP + dTMP
ADP + dTDP
-
-
-
?
ATP + dTMP
ADP + dTDP
-
-
-
-
?
ATP + dTMP
ADP + dTDP
-
-
-
?
ATP + dTMP
ADP + dTDP
-
-
-
-
?
ATP + dTMP
ADP + dTDP
-
-
-
?
ATP + dTMP
ADP + dTDP
-
involved in dTTP metabolism, essential for cell proliferation
-
-
?
ATP + dTMP
ADP + dTDP
-
involved in TTP metabolism, required for the activation of clinically relevant thymidine analogs such as anti-HIV and anti-cancer prodrugs
-
-
?
dATP + dTMP
dADP + dTDP
-
99% of the activity with ATP
-
?
dATP + dTMP
dADP + dTDP
-
dATP is as active as ATP
-
-
?
dGTP + dTMP
dGDP + dTDP
-
42% of the activity with ATP
-
-
?
dGTP + dTMP
dGDP + dTDP
-
59% of the activity with ATP
-
-
?
GTP + dTMP
GDP + dTDP
-
60% of the activity with ATP
-
-
?
GTP + dTMP
GDP + dTDP
-
38% of maximal activity
-
-
?
additional information
?
-
direct correlation between the rate of phosphorylation of an NMP and its ability to induce a closing of the enzymes phosphate-binding loop
-
-
?
additional information
?
-
-
direct correlation between the rate of phosphorylation of an NMP and its ability to induce a closing of the enzymes phosphate-binding loop
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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(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
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-(3,4-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-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-(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-[(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-[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
3'-(aminomethyl)-3'-deoxythymidine
-
-
3'-(azidomethyl)-3'-deoxy-alpha-D-ribosyl-thymine
-
-
3'-(azidomethyl)-3'-deoxythymidine
-
-
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]butanoic acid
-
comparison with inhibition of Mycobacterium tuberculosis 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]butanoic acid
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
5,5'-dithio-bis(2-nitrobenzoic acid)
-
general thymidylate kinase inhibitor
5-bromo-2'-deoxyuridine
-
-
5-chloro-2'-deoxyuridine
-
-
5-fluoro-2'-deoxyuridine
-
not inhibitory at 4 mM
5-iodo-2'-deoxyuridine
-
-
5-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]pentanoic acid
-
comparison with inhibition of Mycobacterium tuberculosis enzyme
dGDP
-
0.5 mM, 23% inhibition
dUDP
-
0.5 mM, 42% inhibition
N-(3,4-dichlorophenyl)-N'-(5'-deoxy-alpha-D-thymidin-5'-yl)-urea
-
comparison with inhibition of Mycobacterium tuberculosis 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-trifluoromethyl-4-chlorobenzyl)thiourea
-
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 Mycobacterium tuberculosis enzyme
P1-(adenosine 5')-P4-(thymidine 5')-tetraphosphate
-
-
P1-(adenosine 5')-P5-(thymidine 5')-pentaphosphate
-
-
P1-(Adenosine 5')-P6-(thymidine 5')-hexaphosphate
-
-
ADP
-
0.5 mM, 33% inhibition
dADP
-
0.5 mM, 34% inhibition
dTDP
-
0.5 mM, 91% inhibition
thymidine
-
0.77 mM, 27% inhibition
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
-
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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.
Colonic Neoplasms
Thymidylate kinase: an old topic brings new perspectives.
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.
Leukemia
Metabolism of 5-fluorouracil in sensitive and resistant tumor cells.
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
DNA synthesis in tumor-bearing rats.
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
Sensitizing cancer cells: is it really all about U?
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.
Sarcoma, Yoshida
DNA synthesis in tumor-bearing rats.
Sarcoma, Yoshida
Metabolism of 5-fluorouracil in sensitive and resistant tumor cells.
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
LEA3D: a computer-aided ligand design for structure-based drug design.
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 analogues as novel antimalarials.
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
Substrate specificity of vaccinia virus thymidylate kinase.
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.
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0.012
2',3'-didehydro-2',3'-dideoxythymidine 5'-monophosphate
pH 7.5, 25°C
0.012
3'-azido-3'-deoxythymidine 5'-monophosphate
pH 7.5, 25°C
0.0038 - 0.012
3'-azido-3'-deoxythymidine monophosphate
0.008
3'-fluoro-3'-deoxythymidine 5'-monophosphate
pH 7.5, 25°C
0.01
5-bromo-dUMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.17
dUMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
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
0.02 - 0.13
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
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
0.0038
3'-azido-3'-deoxythymidine monophosphate
pH and temperature not specified in the publication, mutant enzyme F105Y
0.012
3'-azido-3'-deoxythymidine monophosphate
-
pH 7.4
0.012
3'-azido-3'-deoxythymidine monophosphate
pH and temperature not specified in the publication, wild-type enzyme
0.0051
ATP
pH 7.6, temperature not specified in the publication
0.006
ATP
pH 7.5, 25°C, reaction with dTMP
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
0.069
ATP
pH 7.5, 25°C, reaction with 3'-azido-3'-deoxythymidine 5'-monophosphate
0.62
ATP
-
ATP in form of MgATP2-
0.0045
dTMP
-
-
0.0049
dTMP
-
pH 7.4, 37°C
0.005
dTMP
-
pH 7.4, 30°C
0.02
dTMP
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
0.0063
TMP
pH and temperature not specified in the publication, wild-type enzyme
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0.09
2',3'-didehydro-2',3'-dideoxythymidine 5'-monophosphate
pH 7.5, 25°C
0.14
3'-amino-3'-deoxythymidine 5'-monophosphate
pH 7.5, 25°C
0.003 - 1.7
3'-azido-3'-deoxythymidine 5'-monophosphate
0.012 - 0.25
3'-azido-3'-deoxythymidine monophosphate
0.03
3'-fluoro-3'-deoxythymidine 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
4.8
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
0.5 - 0.9
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
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
0.01
3'-azido-3'-deoxythymidine 5'-monophosphate
pH 7.5, 25°C
0.012
3'-azido-3'-deoxythymidine 5'-monophosphate
-
wild-type
0.17
3'-azido-3'-deoxythymidine 5'-monophosphate
-
mutant F105Y fused to the protein transduction domain of Tat
0.27
3'-azido-3'-deoxythymidine 5'-monophosphate
-
mutant F105Y
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
0.14
dTMP
-
mutant F105Y fused to the protein transduction domain of Tat
0.76
dTMP
-
wild-type enzyme fused to the protein transduction domain of Tat
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
120
5-bromo-dUMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
150
dTMP
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
4.1 - 45
N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
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
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.
0.252
(3E)-4-[4-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]but-3-enoic acid
-
-
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
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
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
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
-
-
0.7
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
-
-
0.362
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
0.22
3'-(aminomethyl)-3'-deoxythymidine
-
-
1.04
3'-(azidomethyl)-3'-deoxythymidine
-
-
0.293
4-[4-[(5-bromo-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
-
-
0.214
5-bromo-2'-deoxyuridine
-
pH 7.4, 30°C
0.375
5-chloro-2'-deoxyuridine
-
pH 7.4, 30°C
0.35
5-iodo-2'-deoxyuridine
-
pH 7.4, 30°C
0.122
5-[4-[(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]phenyl]pentanoic acid
-
-
0.18
deoxythymidine
-
pH 7.4, 30°C
0.0116
N-(3,4-dichlorophenyl)-N'-(5'-deoxy-alpha-D-thymidin-5'-yl)-urea
-
pH 7.4
0.079
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(3,4-dichlorophenylethyl)thiourea
-
pH 7.4
0.05
N-(5'-deoxy-alpha-D-thymidin-5'-yl)-N'-(3-trifluoromethyl-4-chlorobenzyl)thiourea
-
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 - 0.0209
P1-(adenosine 5')-P4-(thymidine 5')-tetraphosphate
0.00047 - 0.0006
P1-(adenosine 5')-P5-(thymidine 5')-pentaphosphate
0.00018 - 0.0002
P1-(Adenosine 5')-P6-(thymidine 5')-hexaphosphate
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
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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
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
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
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
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
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
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
Homo sapiens, 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
Homo sapiens, Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis
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
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
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
Homo sapiens, Mycobacterium tuberculosis (P9WKE1), Mycobacterium tuberculosis
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
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
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
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
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
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
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
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