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Information on EC 2.7.4.9 - dTMP kinase and Organism(s) Homo sapiens

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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
tmpk, dtmp kinase, tmpkmt, thymidine monophosphate kinase, tmp kinase, pftmk, dtmpk, thymidylate monophosphate kinase, s. aureus thymidylate kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxythymidine 5'-monophosphate kinase
-
-
-
-
dTMP kinase
-
-
-
-
dTMP kinases
-
dTMPK
-
-
-
-
human thymidine monophosphate kinase (hTMPK)
-
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
Phosphorylation
of L-dTMP
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:dTMP phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9014-43-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-monophosphate
ADP + 2',3'-didehydro-2',3'-dideoxythymidine 5'-diphosphate
show the reaction diagram
-
-
-
?
ATP + 3'-amino-3'-deoxythymidine 5'-monophosphate
ADP + 3'-amino-3'-deoxythymidine 5'-diphosphate
show the reaction diagram
-
-
-
?
ATP + 3'-azido-2',3'-dideoxythymidine monophosphate
ADP + 3'-azido-2',3'-dideoxythymidine diphosphate
show the reaction diagram
-
-
-
?
ATP + 3'-azido-3'-deoxythymidine 5'-monophosphate
ADP + 3'-azido-3'-deoxythymidine 5'-diphosphate
show the reaction diagram
ATP + 3'-azido-3'-deoxythymidine monophosphate
ADP + 3'-azido-3'-deoxythymidine diphosphate
show the reaction diagram
ATP + 3'-fluoro-3'-deoxythymidine 5'-monophosphate
ADP + 3'-fluoro-3'-deoxythymidine 5'-diphosphate
show the reaction diagram
-
-
-
?
ATP + 5-bromo-dUMP
ADP + 5-bromo-dUDP
show the reaction diagram
-
-
-
?
ATP + ddTMP
?
show the reaction diagram
-
-
-
?
ATP + dTMP
ADP + dTDP
show the reaction diagram
ATP + dUMP
ADP + dUDP
show the reaction diagram
-
-
-
?
ATP + N1-[(E)-3-dihydroxyphosphonyl-prop-2-enyl]-thymine
ADP + ?
show the reaction diagram
-
-
-
?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-chlorouracil
ADP + ?
show the reaction diagram
-
-
-
?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-5-fluorouracil
ADP + ?
show the reaction diagram
-
-
-
?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-thymine
ADP + ?
show the reaction diagram
-
-
-
?
ATP + N1-[(E)-4-dihydroxyphosphonyl-but-2-enyl]-uracil
ADP + ?
show the reaction diagram
-
-
-
?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-bromouracil
ADP + ?
show the reaction diagram
-
-
-
?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-chlorouracil
ADP + ?
show the reaction diagram
-
-
-
?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-5-fluorouracil
ADP + ?
show the reaction diagram
-
-
-
?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-thymine
ADP + ?
show the reaction diagram
-
-
-
?
ATP + N1-[(E)-5-dihydroxyphosphonyl-pent-2-enyl]-uracil
ADP + ?
show the reaction diagram
-
-
-
?
ATP + TMP
ADP + TDP
show the reaction diagram
-
-
-
?
CTP + dTMP
CDP + dTDP
show the reaction diagram
-
56% of the activity with ATP
-
-
?
D-dTMP + ATP
D-dTDP + ADP
show the reaction diagram
-
-
-
?
dATP + dTMP
dADP + dTDP
show the reaction diagram
dCTP + dTMP
dCDP + dTDP
show the reaction diagram
-
45% of the activity with ATP
-
-
?
dGTP + dTMP
dGDP + dTDP
show the reaction diagram
GTP + dTMP
GDP + dTDP
show the reaction diagram
L-dTMP + ATP
L-dTDP + ADP
show the reaction diagram
-
-
-
?
UTP + dTMP
UDP + dTDP
show the reaction diagram
-
60% of the activity with ATP
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + dTMP
ADP + dTDP
show the reaction diagram
L-dTMP + ATP
L-dTDP + ADP
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
deoxythymidine
-
-
dGDP
-
0.5 mM, 23% inhibition
dTMP
-
-
dTTP
-
-
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
-
-
thymidine
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.0051 - 0.62
ATP
0.02
D-dTMP
-
0.13
dATP
-
pH 7.2, 37°C
0.45
dGTP
-
pH 7.2, 37°C
0.0045 - 0.02
dTMP
0.17
dUMP
at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2
0.33
GTP
-
pH 7.2, 37°C
0.38
L-dTMP
-
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
0.0042 - 0.0063
TMP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.03
ddTMP
pH 7.5, 25°C
0.14 - 3
dTMP
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
0.17 - 0.73
TMP
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.005
dTMP
-
-
0.75
dTTP
-
-
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
0.18
thymidine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.809
-
-
0.833
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
upregulation in monocyte/macrophage differentiating cells
Manually annotated by BRENDA team
-
from HIV-infected patients and healthy noninfected individuals. Enzyme activity is 10fold lower in extracts from infected as compared to uninfected persons
Manually annotated by BRENDA team
-
term placenta
Manually annotated by BRENDA team
additional information
-
expression in several tissues and erythroblastoma cell lines
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
high levels of canonical TMPK protein
Manually annotated by BRENDA team
low levels of canonical TMPK protein
Manually annotated by BRENDA team
low levels of canonical TMPK protein
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KTHY_HUMAN
212
0
23819
Swiss-Prot
Mitochondrion (Reliability: 5)
H7BZ20_HUMAN
192
0
21767
TrEMBL
other Location (Reliability: 3)
Q53F55_HUMAN
212
0
23761
TrEMBL
Mitochondrion (Reliability: 3)
Q6FGU2_HUMAN
212
0
23819
TrEMBL
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
2 * 24000, SDS-PAGE
50000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 24000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F105Y
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione beads chromatography
-
recombinant protein using His-tag
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli
-
expressed in Escherichia coli JM109 cells
-
expressed in Mus musculus heart
-
expression as fusion protein with Green Fluorescent Protein in HeLa cell
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
-
potential targets for the development of antiviral and cancer therapies
medicine
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team