2.7.4.9: dTMP kinase
This is an abbreviated version!
For detailed information about dTMP kinase, go to the full flat file.
Word Map on EC 2.7.4.9
Reaction
Synonyms
ATP: TMP phosphotransferase, Cdc8, deoxythymidine 5'-monophosphate kinase, deoxythymidine monophosphate kinase, dTMP kinase, dTMP kinases, dTMPK, human thymidine monophosphate kinase (hTMPK), kinase, thymidine monophosphate (phosphorylating), kinase, thymidylate (phosphorylating), ORF454, PfTMK, S. aureus thymidylate kinase, thymidine 5'-monophosphate kinase, thymidine kinase, thymidine monophosphate kinase, thymidylate kinase, thymidylate monophosphate kinase, thymidylic acid kinase, thymidylic kinase, TK1, TMK, TMP kinase, TMPK, TMPKmt, TTHA1607, TYMK
ECTree
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Turnover Number on EC 2.7.4.9 - dTMP kinase
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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
