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Information on EC 2.4.2.4 - thymidine phosphorylase and Organism(s) Homo sapiens

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.4 thymidine phosphorylase
IUBMB Comments
The enzyme in some tissues also catalyses deoxyribosyltransferase reactions of the type catalysed by EC 2.4.2.6, nucleoside deoxyribosyltransferase.
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This record set is specific for:
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
Synonyms
thymidine phosphorylase, pd-ecgf, dthdpase, platelet-derived endothelial cell growth factor, pynpase, pd-ecgf/tp, pyrimidine nucleoside phosphorylase, pdecgf, platelet-derived endothelial cell growth factor/thymidine phosphorylase, gliostatin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
angiogenic factor platelet-derived endothelial cell growth factor/thymidine phosphorylase
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animal growth regulators, blood platelet-derived endothelial cell growth factors
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blood platelet-derived endothelial cell growth factor
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deoxythymidine phosphorylase
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dthdpase
gliostatin
gliostatins
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PD-ECGF
PD-ECGF/TP
PD-ECGF/TP platelet-derived endothelial cell growth factor
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PDECGF
phosphorylase, thymidine
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platelet derived endothelial cell growth factor
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platelet derived endothelial cell grwoth factor
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platelet derived-endothelial cell growth factor
platelet-derived endothelial cell growth factor
platelet-derived endothelial cell growth factor/thymidine phosphorylase
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platelet-derived endotherial cell growth factor
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pyrimidine deoxynucleoside phosphorylase
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pyrimidine nucleoside phosphorylase
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pyrimidine phosphorylase
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TDRPASE
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ThdPase
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thymidine phosphorylase
thymidine Pi deoxyribosyltransferase
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thymidine-orthophosphate deoxyribosyltransferase
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-
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thymidine:orthophosphate deoxy-D-ribosyltransferase
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-
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-
additional information
the enzyme belongs to the pyrimidine nucleoside phosphorylase family
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
SYSTEMATIC NAME
IUBMB Comments
thymidine:phosphate deoxy-alpha-D-ribosyltransferase
The enzyme in some tissues also catalyses deoxyribosyltransferase reactions of the type catalysed by EC 2.4.2.6, nucleoside deoxyribosyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-23-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(tetrahydro-2-furanyl)-5-fluorouracil + phosphate
?
show the reaction diagram
-
i.e. Tegafur
-
-
?
2'-deoxy-5-nitrouridine + phosphate
5-nitrouracil + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
2'-deoxyuridine + phosphate
uracil + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
r
3-fluorothymidine + phosphate
3-fluorothymine + 2-deoxy-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
5'-deoxy-5'-fluorothymidine + phosphate
thymine + 5-fluoro-2,5-dideoxy-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
5'-deoxy-5-fluorouridine + phosphate
5-fluorouracil + 5-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
r
5'-deoxy-5-fluorouridine + phosphate
5-fluorouracil + 5-deoxy-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
5'-deoxy-5-fluorouridine + phosphate
5-fluorouracil + 5-deoxyribose-1-phosphate
show the reaction diagram
5-fluoro-2'-deoxyuridine + phosphate
5-fluorouracil + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
r
5-fluoro-2'-deoxyuridine + phosphate
5-fluorouracil + 2-deoxy-D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
5-fluoro-2'-deoxyuridine + phosphate
5-fluorouracil + 2-deoxyribose-1-phosphate
show the reaction diagram
5-fluorouracil + 2-deoxy-alpha-D-ribose 1-phosphate
5-fluoro-2'-deoxyuridine + phosphate
show the reaction diagram
5-fluorouridine + phosphate
5-fluorouracil + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
r
5-fluorouridine + phosphate
5-fluorouracil + D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
5-fluorouridine + phosphate
5-fluorouracil + ribose 1-phosphate
show the reaction diagram
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-
-
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?
5-nitro-2'-deoxyuridine + phosphate
5-nitrouracil + 2-deoxy-D-ribose 1-phosphate
show the reaction diagram
bromodeoxyuridine + phosphate
bromouracil + 2-deoxy-D-ribose
show the reaction diagram
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-
-
-
?
deoxythymidine + phosphate
thymine + 2-deoxy-D-ribose 1-phosphate
show the reaction diagram
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-
-
-
?
deoxyuridine + phosphate
uracil + 2-deoxy-D-ribose 1-phosphate
show the reaction diagram
fluorodeoxyuridine + phosphate
fluorouracil + 2-deoxy-D-ribose
show the reaction diagram
-
-
-
-
?
iododeoxyuridine + phosphate
iodouracil + 2-deoxy-D-ribose
show the reaction diagram
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-
-
-
?
thymidine + arsenate
?
show the reaction diagram
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-
-
-
?
thymidine + phosphate
thymine + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
thymidine + phosphate
thymine + 2-deoxy-D-ribose 1-phosphate
show the reaction diagram
thymidine + phosphate
thymine + alpha-D-deoxyribose 1-phosphate
show the reaction diagram
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-
-
r
thymine + 2-deoxy-alpha-D-ribose 1-phosphate
thymidine + phosphate
show the reaction diagram
thymine + 2-deoxy-D-ribose 1-phosphate
thymidine + phosphate
show the reaction diagram
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
show the reaction diagram
-
-
-
r
uridine + phosphate
uracil + D-ribose 1-phosphate
show the reaction diagram
-
-
-
-
?
uridine + phosphate
uracil + ribose 1-phosphate
show the reaction diagram
-
-
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?
additional information
?
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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
5-fluorouracil + 2-deoxy-alpha-D-ribose 1-phosphate
5-fluoro-2'-deoxyuridine + phosphate
show the reaction diagram
-
the enzyme converts 5-fluorouracil to 5-fluoro-2'-deoxyuridine, activating the prodrug, overview. This action can only take place if there is enough co-substrate. 5-Fluorouracil prodrugs and metabolism, detailed overview
5-fluoro-2'-deoxyuridine is further converted by thymidine kinase to 5-fluoro-2'-deoxyuridine 5'-monophosphate
-
?
thymidine + phosphate
thymine + 2-deoxy-alpha-D-ribose 1-phosphate
show the reaction diagram
thymidine + phosphate
thymine + 2-deoxy-D-ribose 1-phosphate
show the reaction diagram
thymine + 2-deoxy-alpha-D-ribose 1-phosphate
thymidine + phosphate
show the reaction diagram
-
-
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r
thymine + 2-deoxy-D-ribose 1-phosphate
thymidine + phosphate
show the reaction diagram
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R,3R,4S,5R)-9-(3,4-dihydroxy-5-trityloxymethyl-tetrahydrofuran-2-yl)-1,9-dihydropurin-6-one
KIN59
(3-benzyl-2,4,5-trioxoimidazolidin-1-yl)acetic acid
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(4xi)-2',3'-O-[(1R)-2-carboxyethylidene]-5-methylcytidine
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(4xi)-5-methyl-2',3'-O-[(1R)-2-phosphonoethylidene]cytidine
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(E)-1-((2-fluorophenyl)(hydroxyimino)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
-
(E)-1-((4-chlorophenyl)(hydroxyimino)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
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(E)-1-((4-ethylphenyl)(hydroxyimino)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
-
(E)-1-((4-fluorophenyl)(hydroxyimino)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
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(E)-1-((hydroxyimino)(3-methoxyphenyl)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
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(E)-1-((hydroxyimino)(4-methoxyphenyl)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
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(E)-1-((hydroxyimino)(p-tolyl)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
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(E)-1-((hydroxyimino)(phenyl)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
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(R)-(1-fluoro-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)propan-2-yloxy)methylphosphonic phosphoric anhydride
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strong inhibitory effect
(R)-1-[3-fluoro-2-(phosphonomethoxy)-propyl]thymine
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at 0.01 mM, 82% inhibition of V79 cell-expressed thymidine phosphorylase, 56% inhibition of thymidine phosphorylase from placenta
(R)-1-[3-fluoro-2-(phosphonomethoxy)propyl]thymine
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efficient inhibitor
(R)-1-[3-hydroxy-2-(phosphonomethoxy)propyl]thymine
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at 0.01 mM, 84% inhibition of V79 cell-expressed thymidine phosphorylase, 84% inhibition of thymidine phosphorylase from placenta
(S)-(1-fluoro-3-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)propan-2-yloxy)methylphosphonic phosphoric anhydride
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strong inhibitory effect
(S)-1-[3-fluoro-2-(phosphonomethoxy)propyl]thymine
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efficient inhibitor
(Z)-1-((2-fluorophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((3,4-dichlorophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((3-fluorophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((4-bromophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((4-chlorophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((4-ethylphenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((4-fluorophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((hydroxyimino)(3-methoxyphenyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((hydroxyimino)(4-methoxyphenyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((hydroxyimino)(m-tolyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((hydroxyimino)(p-tolyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((hydroxyimino)(phenyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-1-((hydroxyimino)(thiophen-2-yl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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(Z)-N'-((4-chloro-2-oxo-4a,8a-dihydro-2H-chromen-3-yl)methylene)-2-oxo-1,2,4a,8a-tetrahydroquinoline-6-carbohydrazide
-
([(1R)-2-fluoro-1-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]ethoxy]methyl)phosphonic acid
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([(1R)-2-fluoro-1-[(5-methyl-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl)methyl]ethoxy]methyl)phosphonic acid
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at 0.01 mM, complete inhibition of V79 cell-expressed thymidine phosphorylase
([(1R)-2-fluoro-1-[(5-methyl-2,6-dioxotetrahydropyrimidin-1(2H)-yl)methyl]ethoxy]methyl)phosphonic acid
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low inhibitory effect
([(1R)-2-hydroxy-1-[(5-methyl-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl)methyl]ethoxy]methyl)phosphonic acid
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at 0.01 mM, 91% inhibition of V79 cell-expressed thymidine phosphorylase, 79% inhibition of thymidine phosphorylase from placenta
([(1S)-2-fluoro-1-[(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]ethoxy]methyl)phosphonic acid
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([(1S)-2-fluoro-1-[(5-methyl-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl)methyl]ethoxy]methyl)phosphonic acid
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at 0.01 mM, complete inhibition of V79 cell-expressed thymidine phosphorylase
([(1S)-2-fluoro-1-[(5-methyl-2,6-dioxotetrahydropyrimidin-1(2H)-yl)methyl]ethoxy]methyl)phosphonic acid
-
low inhibitory effect
([(1S)-2-hydroxy-1-[(5-methyl-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl)methyl]ethoxy]methyl)phosphonic acid
-
at 0.01 mM, complete of V79 cell-expressed thymidine phosphorylase, 95% inhibition of thymidine phosphorylase from placenta
([2,2,2-trifluoro-1-[(5-fluoro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)methyl]ethoxy]methyl)phosphonic acid
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([[(2R,3S,5R)-2-(hydroxymethyl)-5-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuran-3-yl]oxy]methyl)phosphonic acid
-
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1-((methoxyimino)(phenyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
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1-(2-phenylethyl)imidazolidine-2,4,5-trione
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1-(8-phosphonooctyl)-6-amino-5-bromouracil
-
competitive
1-(8-phosphonooctyl)-7-deazaxanthine
-
competitive
1-benzoyl-6-methylpyrimidine-2,4(1H,3H)-dione
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1-benzylimidazolidine-2,4,5-trione
-
1-[(2-methylphenyl)methyl]imidazolidine-2,4,5-trione
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1-[(R)-3-fluoro-2-(phosphonomethoxy)propyl]thymine
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-
1-[2-(phosphonomethoxy)ethyl]thymine
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at 0.01 mM, complete inhibition of V79 cell-expressed thymidine phosphorylase, 85% inhibition of thymidine phosphorylase from placenta
1H-pyrrolo[2,3-d]pyrimidine-2,4(3H,7H)-dione
-
2,7-bis(methylsulfanyl)[1,2,4]triazolo[1,5-a][1,3,5]triazin-5(4H)-one
-
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2-(3,4-dichlorophenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
2-(3,4-dihydroxyphenyl)quinazolin-4(3H)-one
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2-(3-bromophenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
-
2-(3-methylphenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
-
2-(4-bromo-3-methylphenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
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2-(4-bromophenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
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2-(4-methylphenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
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2-(benzylsulfanyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
-
2-(diphenylmethyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
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2-(furan-2-yl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
-
2-(methylsulfanyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
-
2-(methylsulfanyl)-7-sulfanylidene-6,7-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-5(4H)-one
-
-
2-(methylsulfanyl)[1,2,4]triazolo[1,5-a][1,3,5]triazine-5,7(4H,6H)-dione
-
-
2-(pyridin-2-yl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
-
2-benzyl-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
2-deoxy-alpha-D-ribose 1-phosphate
dRib-1-P , a non-competitive product inhibitor of the forward reaction, in the reverse reaction, dRib-1-P enhanced the binding of thymine
2-deoxy-L-ribose
-
-
2-mercapto-7H-pyrrolo[2,3-d]pyrimidin-4(3H)-one
-
2-phenyl-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
2-phenyl-7-sulfanylidene-6,7-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-5(4H)-one
2-phenylquinazolin-4(3H)-one
-
2-phenyl[1,2,4]triazolo[1,5-a][1,3,5]triazine-5,7(4H,6H)-dione
2-[(2-phenylethyl)sulfanyl]-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
-
2-[(3,4-dichlorophenyl)methyl]-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
2-[(3-phenylpropyl)sulfanyl]-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
-
2-[[(5-chloro-2-methylidene-6-oxo-1,2,3,6-tetrahydropyrimidin-4-yl)methyl]sulfanyl]-7-phenyl-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
-
3,3'-(1,3,4-oxadiazole-2,5-diyl)dipyridine
-
3-(((4-chlorophenyl)amino)(phenyl)methyl)-5-(2,6-dimethylphenyl)1,3,4-oxadiazole-2(3H)-thione
-
3-(((4-chlorophenyl)amino)methyl)-5-(2-iodophenyl)-1,3,4-oxadiazole-2(3H)-thione
-
3-((4-benzylpiperazin-1-yl)methyl)-5-(4-chlorophenyl)-1,3,4-oxadiazole-2(3H)-thione
-
3-((5-(4-chlorophenyl)-2-thioxo-1,3,4-oxadiazol-3(2H)-yl)methyl)thiazolidine-2,4-dione
-
3-((benzylamino)methyl)-5-(4-chlorophenyl)-1,3,4-oxadiazole-2(3H)-thione
-
3-(3-(quinoxalin-2-yl)thiazolo[2,3-c][1,2,4]triazol-5-yl)benzene-1,2-diol
-
3-(3-benzyl-2,4,5-trioxoimidazolidin-1-yl)propanamide
-
3-benzoyl-5-chloropyrimidine-2,4(1H,3H)-dione
-
-
3-benzyl-1H-2-benzopyran-1-one
-
3-[(2-methoxy-6-nitroanilino)methyl]-5-(4-methylphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
3-[(2-methylphenyl)methyl]-1H-2-benzopyran-1-one
-
3-[(3,4-dimethylanilino)methyl]-5-phenyl-1,3,4-oxadiazole-2(3H)-thione
-
3-[(E)-[(2,4-dichlorophenyl)imino]methyl]-4H-1-benzopyran-4-one
-
3-[(E)-[(3-methoxy-4-methylphenyl)imino]methyl]-4H-1-benzopyran-4-one
-
3-[2,4,5-trioxo-3-(2-phenylethyl)imidazolidin-1-yl]propanamide
-
3-[3-[(2-methylphenyl)methyl]-2,4,5-trioxoimidazolidin-1-yl]propanamide
-
4,6-dihydroxy-5-nitropyrimidine
-
0.1 mM, competitive
4-(2,5-difluorobenzyl)-N-(4-(trifluoromethyl)phenyl)piperazine-1-carbothioamide
-
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(1-(4-nitrophenyl)ethylidene)benzohydrazide
-
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(2,3,4-trihydroxybenzylidene)benzohydrazide
-
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(2,3,4-trimethoxybenzylidene)benzohydrazide
-
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(2-nitrobenzylidene)benzohydrazide
-
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(3,4,5-trimethoxybenzylidene)benzohydrazide
-
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(4-(phenoxymethyl)benzylidene)benzohydrazide
-
4-oxo-4H-1-benzopyran-3-carbaldehyde
-
4-[(Z)-[(3-hydroxynaphthalen-2-yl)methylidene]amino]-1,5-dimethyl-2-phenylpyrazolidin-3-one
-
5'-O-trityl-inosine
5'-O-tritylinosine
5-(2-chlorophenyl)-3-(((4-chlorophenyl)amino)(phenyl)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(2-chlorophenyl)-3-((thiazol-2-ylamino)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-(((2-nitrophenyl)amino)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-(((3,3-diphenylpropyl)amino)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-(((4-fluorophenyl)amino)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-(((4-hydroxyphenyl)amino)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-((2-methyl-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-((4-(2-methoxyphenyl)piperazin-1-yl)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-((4-cyclohexylpiperazin-1-yl)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-((cyclohexylamino)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-((dicyclohexylamino)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-((naphthalen-1-ylamino)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-((phenylamino)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-chlorophenyl)-3-((thiazol-2-ylamino)methyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(4-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
-
5-(benzylsulfanyl)-2-phenyl-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
5-(methylsulfanyl)-2-phenyl-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
5-amino-6-chlorouracil
-
-
5-benzyl-6-chloropyrimidine-2,4(1H,3H)-dione
-
-
5-benzylacyclouridine
-
-
5-bromo-6-(3'-methylimidazol-1-yl)uracil
IC50: 0.038 mM
5-bromo-6-amino-uracil
-
enzyme inhibition results in a significant increase in basal and oxidative stress-induced apoptosis, the effect is abrogated by supplementation with 2-deoxy-D-ribose-1-phosphate
5-bromo-6-aminouracil
-
-
5-bromo-6-[(2'-nitroimidazol-1'-yl)methyl]uracil
IC50: 0.16 mM
5-bromo-6-[(3-methylimidazol-1-yl)methyl]uracil
IC50: 0.017 mM
5-bromo-6-[(4'-nitroimidazol-1'-yl)methyl]uracil
IC50: 0.181 mM
5-bromo-6-[[(1,3-dihydroxypropan-2-yl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
-
5-bromo-6-[[(2,3-dihydroxypropyl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
-
5-bromo-6-[[(2-hydroxyethyl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
-
5-Bromouracil
-
0.1 mM, competitive
5-butyl-6-chloropyrimidine-2,4(1H,3H)-dione
-
-
5-chloro-6-(2-iminopyrrolidin-1-yl)methyl-2,4(1H,3H)-pyrimidinedione hydrochloride
-
-
5-chloro-6-(2-iminopyrrolidin-1-yl)methyl-2,4-(1H,3H)-pyrimidine
-
-
5-chloro-6-(3'-methylimidazol-1-yl)uracil
IC50: 0.035 mM
5-chloro-6-[(2'-nitroimidazol-1'-yl)methyl]uracil
IC50: 0.115 mM
5-chloro-6-[(3-methylimidazol-1-yl)methyl]uracil
IC50: 0.018 mM
5-chloro-6-[(4'-nitroimidazol-1'-yl)methyl]uracil
IC50: 0.2 mM
5-chloro-6-[([4-oxo-8-[4-(pentafluoro-lambda6-sulfanyl)phenyl]-1,2,3,4-tetrahydropyrazolo[1,5-a][1,3,5]triazin-2-yl]sulfanyl)methyl]pyrimidine-2,4(1H,3H)-dione
-
5-chloro-6-[1-(2-iminopyrrolidinyl) methyl] uracil hydrochloride
-
5-chloro-6-[1-(2-iminopyrrolidinyl)methyl] uracil hydrochloride
5-chloro-6-[1-(2-iminopyrrolidinyl)methyl]uracil
-
-
5-chloro-6-[1-(2-iminopyrrolidinyl)methyl]uracil hydrochloride
-
-
5-chloro-6-[1-(2-iminopyrrolidinyl)methyl]uracilhydrochloride
-
5-chloro-6-[1-(imminopyrrolidinyl)methyl]uracil hydrochloride
5-chloro-6-[[(1,3-dihydroxypropan-2-yl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
-
5-chloro-6-[[(2-hydroxyethyl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
-
5-ethyl-1-[(R)-3-fluoro-2-(phosphonomethoxy)propyl]uracil
-
-
5-ethyl-1-[(R)-3-hydroxy-2-(phosphonomethoxy)propyl]uracil
-
-
5-ethyl-1-[(S)-3-fluoro-2-(phosphonomethoxy)propyl]uracil
-
-
5-fluoro-6-[(2-aminoimidazol-1-yl)methyl]uracil
i.e. AIFU, synthesis, overview, uncompetitive with respect to phosphate, acts as transition state analogs, mimicking the anionic thymine leaving group anchored by their protonated side chains to the enzyme-bound phosphate by electrostatic and H-bonding interactions, modeling of ligand binding at the active site, overview
5-fluorouracil
5-iodo-6-[[(piperidin-1-yl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
-
5-Iodouracil
His116 directly interacts with the inhibitor via its NE2 group, enzyme binding structure, overview
5-methyluridine
-
-
5-Nitrouracil
-
0.1 mM, competitive
5-phenyl-1,3,4-oxadiazole-2(3H)-thione
-
5-phenyl-6-pyrrolidin-1-ylpyrimidine-2,4(1H,3H)-dione
-
-
5-sulfanylidene-2-(thiophen-2-yl)-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
-
5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
-
-
5-[(1E)-but-1-en-1-yl]-6-chloropyrimidine-2,4(1H,3H)-dione
-
-
5-[(E)-[2-(quinoxalin-2-yl)hydrazinylidene]methyl]benzene-1,2,4-triol
-
6-(((1,3-dihydroxypropan-2-yl)amino)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
the inhibitor shows a noncompetitive inhibition mode with both thymidine and inorganic phosphate substrates. Effect of 8g on cell viabilities of different cancer cell lines, overview
6-(2-aminoethyl)amine-5-chlorouracil
-
AEAC
6-(3-methylimidazol-1-yl)uracil
IC50: 0.110 mM
6-(4-phenlybutylamino)uracil
-
PBAU, 50% inhibition at 0.03 mM
6-amino-5-bromopyrimidine-2,4(1H,3H)-dione
-
6-amino-5-bromouracil
6-amino-5-chlorouracil
6-aminothymine
6-aminouracil
-
0.1 mM, competitive
6-benzyl-2-thiouracil
-
0.1 mM, mixed inhibition
6-bromo-5-phenylpyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-(1-methylethenyl)pyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-(2-naphthyl)pyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-(2-thienyl)pyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-(3,5-dimethylphenyl)pyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-(4-fluorophenyl)pyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-cyclohex-1-en-1-ylpyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-cyclopent-1-en-1-yluracil
-
-
6-chloro-5-ethylpyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-heptylpyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-hexylpyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-pentylpyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-phenylpyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-propylpyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-pyridin-3-ylpyrimidine-2,4(1H,3H)-dione hydrochloride
-
-
6-chloro-5-[(1E)-1-ethylprop-1-en-1-yl]pyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-[(1E)-pent-1-en-1-yl]pyrimidine-2,4(1H,3H)-dione
-
-
6-chloro-5-[(1E)-prop-1-en-1-yl]pyrimidine-2,4(1H,3H)-dione
-
-
6-fluoro-5-phenylpyrimidine-2,4(1H,3H)-dione
-
-
6-methyl-5-phenylpyrimidine-2,4(1H,3H)-dione
-
-
6-[(2'-aminoimidazol-1'-yl)methyl]-5-bromouracil
IC50: 0.000019 mM
6-[(2'-aminoimidazol-1'-yl)methyl]-5-chlorouracil
IC50: below 0.000049 mM
6-[(2'-aminoimidazol-1'-yl)methyl]uracil
IC50: 0.0001 mM
6-[(2'-nitroimidazol-1'-yl)methyl]uracil
IC50: 0.2577 mM
6-[(2-aminoethyl)amino]-5-phenylpyrimidine-2,4(1H,3H)-dione
-
-
6-[(3-methylimidazol-1-yl)methyl]thymine
IC50: 0.06 mM
6-[(3-methylimidazol-1-yl)methyl]uracil
IC50: 0.042 mM
6-[(4'-aminoimidazol-1'-yl)methyl]-5-bromouracil
IC50: 0.041 mM
6-[(4'-aminoimidazol-1'-yl)methyl]-5-chlorouracil
IC50: 0.026 mM
6-[(4'-aminoimidazol-1'-yl)methyl]uracil
IC50: 0.143 mM
6-[(4'-nitroimidazol-1'-yl)methyl]uracil
IC50: 0.5 mM
6-[(dimethylamino)methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
-
6-[(dipentylamino)methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
-
6-[(dipropylamino)methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
-
6-[[(2,3-dihydroxypropyl)(methyl)amino]methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
-
6-[[(2-hydroxyethyl)amino]methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
-
6-[[bis(2-ethoxyethyl)amino]methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
-
7-(4-tert-butylphenyl)-2-sulfanylidene-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
-
7-(4-tert-butylphenyl)-2-[[(5-chloro-2-methylidene-6-oxo-1,2,3,6-tetrahydropyrimidin-4-yl)methyl]sulfanyl]-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
-
7-(methylsulfanyl)-2-phenyl-6,7-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-5(4H)-one
-
7-(methylsulfanyl)-2-phenyl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5(4H)-one
-
-
7-deazaxanthine
7-phenyl-2-sulfanylidene-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
-
7-phenylpyrazolo[1,5-a][1,3,5]triazine-2,4(1H,3H)-dione
-
8-phenyl-2-sulfanylidene-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
-
8-[4-(pentafluoro-lambda6-sulfanyl)phenyl]-2-sulfanylidene-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
-
9-[8-phosphonooctyl]-7-deazaxanthine
-
allyloxymethylthymine
-
0.1 mM, uncompetitive
aurothioglucose
-
the expression of tyhmidine phosphorylase mRNA is significantly decreased by stimulation with aurothioglucose
dexamethasone
-
the expression of tyhmidine phosphorylase mRNA is significantly decreased by stimulation with dexamethasone
diethyl ((2-[(3,4-dihydro-5-methyl-2,4-dioxopyrimidin-1(2H)-yl)methyl]cyclopent-1-en-1-yl)(difluoro)methyl)phosphonate
-
-
diethyl ((2-[(3,4-dihydro-5-methyl-2,4-dioxopyrimidin-1(2H)-yl)methyl]cyclopent-1-en-1-yl)methyl)phosphonate
-
-
diethyl ((2-[(5-chloro-3,4-dihydro-2,4-dioxopyrimidin-1(2H)-yl)methyl]cyclopent-1-en-1-yl)methyl)phosphonate
-
-
diethyl (2-[(5-chloro-3,4-dihydro-2,4-dioxopyrimidin-1(2H)-yl)methyl]benzyl)phosphonate
-
-
diethyl ([2-(hydroxymethyl)cyclopent-1-en-1-yl]methyl)phosphonate
-
-
diethyl [(Z)-4-(5-chloro-3,4-dihydro-2,4-dioxopyrimidin-1(2H)-yl)but-2-en-1-yl]phosphonate
-
-
diethyl [(Z)-4-hydroxybut-2-en-1-yl]phosphonate
-
-
diethyl [2-(hydroxymethyl)benzyl]phosphonate
-
-
disodium ((2-[(3,4-dihydro-5-methyl-2,4-dioxopyrimidin-1(2H)-yl)methyl]cyclopent-1-en-1-yl)(difluoro)methyl)phosphonate
-
-
disodium ((2-[(3,4-dihydro-5-methyl-2,4-dioxopyrimidin-1(2H)-yl)methyl]cyclopent-1-en-1-yl)methyl)phosphonate
-
-
disodium ((2-[(5-chloro-3,4-dihydro-2,4-dioxopyrimidin-1(2H)-yl)methyl]cyclopent-1-en-1-yl)methyl)phosphonate
-
-
disodium (2-[(5-chloro-3,4-dihydro-2,4-dioxopyrimidin-1(2H)-yl)methyl]benzyl)phosphonate
-
-
disodium [(Z)-4-(5-chloro-3,4-dihydro-2,4-dioxopyrimidin-1(2H)-yl)but-2-en-1-yl]phosphonate
-
-
ethyl (3-benzyl-2,4,5-trioxoimidazolidin-1-yl)acetate
-
ethyl [2,4,5-trioxo-3-(2-phenylethyl)imidazolidin-1-yl]acetate
-
ethyl [3-[(2-methylphenyl)methyl]-2,4,5-trioxoimidazolidin-1-yl]acetate
-
hydrogen [[(1R,2S,4S)-2-(hydroxymethyl)-4-(5-methyl-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl)pyrrolidinium-1-yl]methyl]phosphonate
-
-
KIN56
-
IC50: 0.351 mM
KIN59
i.e. 5'-O-tritylinosine, noncompetitive inhibition
N'-(2,4-dichlorobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(2-cyanobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(2-hydroxy-3-methoxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(3,5-dichloro-2-hydroxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(3-aminobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(3-cyanobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(3-hydroxy-4-methoxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(4-(dimethylamino)benzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(4-chlorobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(4-cyanobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(4-hydroxy-3,5-dimethoxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(4-hydroxy-3-methoxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(5-bromo-2-methoxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N'-(anthracen-9-ylmethylene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
-
N-((5-(4-chlorophenyl)-2-thioxo-1,3,4-oxadiazole-3(2H)-yl)methyl)3(trifluoromethyl) benzamide
-
N-(4-oxo-2-sulfanylidene-8-[[4-(trifluoromethyl)phenyl]methyl]-1,2,3,4-tetrahydropyrazolo[1,5-a][1,3,5]triazin-7-yl)thiourea
-
N-(8-benzyl-4-oxo-2-sulfanylidene-1,2,3,4-tetrahydropyrazolo[1,5-a][1,3,5]triazin-7-yl)thiourea
-
NSC 65043
-
IC50: 0.077 mM
p-chloromercuribenzoate
-
above 0.01 mM
prostaglandin E2
-
-
symplocomoside
-
symponoside
-
TAS-102
is a combination of trifluridine (FTD, a fluorinated thymidine analogue) and tipiracil hydrochloride (TPI, a TP inhibitor) at a 1:0.5 molar ratio. The FTD monophosphate metabolite trifluoromethyl deoxyuridine 5'-monophosphate inhibits TS by binding to its active site, but the inhibition is rapidly reversible. Phosphorylation of trifluoromethyl deoxyuridine 5'-monophosphate results in the formation of trifluoromethyl deoxyuridine 5'-triphosphate that is misincorporated into DNA. Importantly, the concentration of FTD incorporated into DNA is approximately 300fold higher than that of 5FU. FTD is rapidly degraded by TP to its inactive metabolite (5-trifluoromethyl-2,4(1H,3H)-pyrimidinedione). Thus, the main mechanism of action of TAS-102 is its misincorporation into DNA. Tipiracil inhibits the main catabolic pathway of the drug, thus enhancing its half-life and cytotoxicity
TFT
designated TAS-102
thymidine
thymidine phosphorylase inhibitor
-
-
-
thymine
tipiracil hydrochloride
TPI
trifluridine
FTD, is rapidly degraded by TP to its inactive metabolite, 5-trifluoromethyl-2,4(1H,3H)-pyrimidinedione
Uracil
-
inhibits activity in turmor tissue, but not in normal tissue
Urea
-
inhibition at high concentration, 4 M, stimulation at low concentration
uridine
-
-
[(2S,3aR,4R,6R,6aR)-4-(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-6-(hydroxymethyl)tetrahydrofuro[3,4-d][1,3]dioxol-2-yl]phosphonic acid
-
-
[(2S,4R,5S)-5-(2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxy-1,3-oxazolidin-2-yl]phosphonic acid
-
-
[(3aR,4R,6R,6aR)-4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-6-(hydroxymethyl)tetrahydrofuro[3,4-d][1,3]dioxol-2-yl]phosphonic acid
-
-
[(3aR,4R,6R,6aR)-4-(hydroxymethyl)-6-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuro[3,4-d][1,3]dioxol-2-yl]phosphonic acid
-
-
[2,4,5-trioxo-3-(2-phenylethyl)imidazolidin-1-yl]acetic acid
-
[3-[(2-methylphenyl)methyl]-2,4,5-trioxoimidazolidin-1-yl]acetic acid
-
[8-(2,4-dioxo-2,3,4,6-tetrahydro-1H-pyrrolo[3,4-d]pyrimidin-1-yl)octyl]phosphonic acid
-
no antitumor activity found with CCRF-CEM T-lymphoblastoid cells, human promyelocytic leukemia HL-60 cells, human cervix carcinoma HeLa S3 cells
[8-(2,4-dioxo-2,3,4,7-tetrahydro-1H-pyrrolo[2,3-d]pyrimidin-1-yl)octyl]phosphonic acid
-
no antitumor activity found with CCRF-CEM T-lymphoblastoid cells, human promyelocytic leukemia HL-60 cells, human cervix carcinoma HeLa S3 cells
[[(1R)-2-(5-ethyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-1-(fluoromethyl)ethoxy]methyl]phosphonic acid
-
-
[[(2R,3aR,6aR)-6-(4-amino-5-methyl-2-oxopyrimidin-1(2H)-yl)-4-(hydroxymethyl)hexahydrofuro[3,4-b]furan-2-yl]methyl]phosphonic acid
-
[[(2S,3aR,6aR)-6-(4-amino-5-methyl-2-oxopyrimidin-1(2H)-yl)-4-(hydroxymethyl)hexahydrofuro[3,4-b]furan-2-yl]methyl]phosphonic acid
-
[[(2S,3aR,6aS)-4-(4-amino-5-methyl-2-oxopyrimidin-1(2H)-yl)-6-(hydroxymethyl)hexahydrofuro[3,4-b]furan-2-yl]methyl]phosphonic acid
-
[[(3S,4R)-3-hydroxy-4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pyrrolidin-1-yl]carbonyl]phosphonic acid
-
-
[[2-(5-fluoro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)ethoxy]methyl]phosphonic acid
-
-
[[2-(5-methyl-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl)ethoxy]methyl]phosphonic acid
-
at 0.01 mM, complete inhibition of V79 cell-expressed thymidine phosphorylase, 82% inhibition of thymidine phosphorylase from placenta
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-deoxy-alpha-D-ribose 1-phosphate
dRib-1-P , a noncompetitive product inhibitor of the forward reaction, in the reverse reaction, dRib-1-P enhanced the binding of thymine
cyclophosphamide
docetaxel
-
induces thymidine phosphorylase expression
doxorubicin
thymidine phosphorylase expression is upregulated after treatment with 60 mg/m2 doxorubicin
epirubicin
thymidine phosphorylase expression is upregulated after treatment with 75 mg/m2 epirubicin
interferon alpha
-
interferon alpha2b
-
induces thymidine phosphorylase mRNA and protein expression in a dose-dependent manner
-
interferon beta
-
causes a rapid and transient increase of thymidine phosphorylase expression
-
interferon gamma
-
causes a rapid and transient increase of thymidine phosphorylase expression
-
interleukin-1beta
-
the expression of tyhmidine phosphorylase mRNA is significantly increased by stimulation with interleukin-1beta
-
mitomycin C
-
induces thymidine phosphorylase expression
paclitaxel
thymine
thymine is a product activator, but becomes a substrate inhibitor at concentrations eight times higher than its Km. Competitive substrate inhibition at high concentration for the human liver TP
Tumor necrosis factor alpha
-
Urea
-
stimulates at low concentration, inhibits at high concentration, 4 M
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.3
1-(Tetrahydro-2-furanyl)-5-fluorouracil
-
-
0.735
2'-deoxyuridine
pH 8.0, 37°C
0.09
2-deoxy-alpha-D-ribose 1-phosphate
pH 7.5, 37°C
0.2 - 1.72
5'-deoxy-5-fluorouridine
0.325
5-fluoro-2'-deoxyuridine
pH 8.0, 37°C
1.3
5-fluorouridine
pH 8.0, 37°C
0.16
5-nitro-2'-deoxyuridine
0.00064 - 0.107
phosphate
0.043 - 9.3
thymidine
0.244 - 9.828
thymine
0.275 - 47.6
uridine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.88
5-nitro-2'-deoxyuridine
pH 7.4, 25°C
0.157 - 8.2
thymidine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
67
phosphate
at pH 7.5 at 37°C
109
thymidine
at pH 7.5 at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0435
(4xi)-2',3'-O-[(1R)-2-carboxyethylidene]-5-methylcytidine
-
0.000236
(4xi)-5-methyl-2',3'-O-[(1R)-2-phosphonoethylidene]cytidine
-
0.021 - 0.211
4,6-dihydroxy-5-nitropyrimidine
0.0002 - 0.00455
5-benzyl-6-chloropyrimidine-2,4(1H,3H)-dione
0.0011 - 0.006
5-Bromouracil
0.00103 - 0.00165
5-butyl-6-chloropyrimidine-2,4(1H,3H)-dione
0.017
5-chloro-6-(2-iminopyrrolidin-1-yl)methyl-2,4(1H,3H)-pyrimidinedione hydrochloride
-
in 50 mM Tris, 1 mM EDTA, pH 7.4, at 37°C
0.0000013 - 0.0000021
5-chloro-6-(2-iminopyrrolidin-1-yl)methyl-2,4-(1H,3H)-pyrimidine
0.000002 - 0.00002
5-chloro-6-[1-(2-iminopyrrolidinyl)methyl] uracil hydrochloride
0.00002
5-chloro-6-[1-(imminopyrrolidinyl)methyl]uracil hydrochloride
-
-
0.000017
5-fluoro-6-[(2-aminoimidazol-1-yl)methyl]uracil
-
0.043 - 0.0728
5-fluorouracil
0.48
5-Iodouracil
-
0.017
5-methyluridine
-
pH 6.0, recombinant enzyme
0.0051 - 0.0253
5-Nitrouracil
0.02
5-phenyl-6-pyrrolidin-1-ylpyrimidine-2,4(1H,3H)-dione
0.00063 - 0.00092
5-[(1E)-but-1-en-1-yl]-6-chloropyrimidine-2,4(1H,3H)-dione
0.000165
6-(2-aminoethyl)amine-5-chlorouracil
-
-
0.0034
6-amino-5-chlorouracil
-
-
0.088 - 0.13
6-aminouracil
0.075 - 0.137
6-benzyl-2-thiouracil
0.00121
6-bromo-5-phenylpyrimidine-2,4(1H,3H)-dione
0.00334 - 0.0051
6-chloro-5-(1-methylethenyl)pyrimidine-2,4(1H,3H)-dione
0.00394 - 0.00459
6-chloro-5-(2-naphthyl)pyrimidine-2,4(1H,3H)-dione
0.00028 - 0.00054
6-chloro-5-(2-thienyl)pyrimidine-2,4(1H,3H)-dione
0.00127 - 0.00174
6-chloro-5-(3,5-dimethylphenyl)pyrimidine-2,4(1H,3H)-dione
0.00071 - 0.00097
6-chloro-5-(4-fluorophenyl)pyrimidine-2,4(1H,3H)-dione
0.00042 - 0.00075
6-chloro-5-cyclohex-1-en-1-ylpyrimidine-2,4(1H,3H)-dione
0.0002 - 0.00029
6-chloro-5-cyclopent-1-en-1-yluracil
0.02
6-chloro-5-ethylpyrimidine-2,4(1H,3H)-dione
0.0016 - 0.00465
6-chloro-5-heptylpyrimidine-2,4(1H,3H)-dione
0.00106 - 0.00179
6-chloro-5-hexylpyrimidine-2,4(1H,3H)-dione
0.00309 - 0.00367
6-chloro-5-pentylpyrimidine-2,4(1H,3H)-dione
0.0004 - 0.00043
6-chloro-5-phenylpyrimidine-2,4(1H,3H)-dione
0.00402 - 0.00581
6-chloro-5-propylpyrimidine-2,4(1H,3H)-dione
0.00301 - 0.00399
6-chloro-5-pyridin-3-ylpyrimidine-2,4(1H,3H)-dione hydrochloride
0.00049 - 0.00091
6-chloro-5-[(1E)-1-ethylprop-1-en-1-yl]pyrimidine-2,4(1H,3H)-dione
0.00041 - 0.00091
6-chloro-5-[(1E)-pent-1-en-1-yl]pyrimidine-2,4(1H,3H)-dione
0.00117 - 0.00121
6-chloro-5-[(1E)-prop-1-en-1-yl]pyrimidine-2,4(1H,3H)-dione
0.00047 - 0.0005
6-fluoro-5-phenylpyrimidine-2,4(1H,3H)-dione
0.02
6-methyl-5-phenylpyrimidine-2,4(1H,3H)-dione
0.02
6-[(2-aminoethyl)amino]-5-phenylpyrimidine-2,4(1H,3H)-dione
0.127 - 0.1286
allyloxymethylthymine
0.005
hydrogen [[(1R,2S,4S)-2-(hydroxymethyl)-4-(5-methyl-2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl)pyrrolidinium-1-yl]methyl]phosphonate
-
-
2 - 5
NSC 65043
-
-
0.00002
thymidine phosphorylase inhibitor
-
-
-
0.158
Uracil
-
tumor tissue
0.013
uridine
-
pH 6.0, recombinant enzyme
0.00077
[(2S,3aR,4R,6R,6aR)-4-(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-6-(hydroxymethyl)tetrahydrofuro[3,4-d][1,3]dioxol-2-yl]phosphonic acid
-
-
0.004
[(2S,4R,5S)-5-(2,6-dioxo-3,6-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxy-1,3-oxazolidin-2-yl]phosphonic acid
-
-
0.005
[(3aR,4R,6R,6aR)-4-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-6-(hydroxymethyl)tetrahydrofuro[3,4-d][1,3]dioxol-2-yl]phosphonic acid
-
-
0.01
[(3aR,4R,6R,6aR)-4-(hydroxymethyl)-6-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)tetrahydrofuro[3,4-d][1,3]dioxol-2-yl]phosphonic acid
-
-
0.0334
[[(2R,3aR,6aR)-6-(4-amino-5-methyl-2-oxopyrimidin-1(2H)-yl)-4-(hydroxymethyl)hexahydrofuro[3,4-b]furan-2-yl]methyl]phosphonic acid
-
0.00105
[[(2S,3aR,6aR)-6-(4-amino-5-methyl-2-oxopyrimidin-1(2H)-yl)-4-(hydroxymethyl)hexahydrofuro[3,4-b]furan-2-yl]methyl]phosphonic acid
-
0.00803
[[(2S,3aR,6aS)-4-(4-amino-5-methyl-2-oxopyrimidin-1(2H)-yl)-6-(hydroxymethyl)hexahydrofuro[3,4-b]furan-2-yl]methyl]phosphonic acid
-
0.01
[[(3S,4R)-3-hydroxy-4-(5-methyl-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)pyrrolidin-1-yl]carbonyl]phosphonic acid
-
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.044
(2R,3R,4S,5R)-9-(3,4-dihydroxy-5-trityloxymethyl-tetrahydrofuran-2-yl)-1,9-dihydropurin-6-one
Homo sapiens
pH and temperature not specified in the publication
0.264
(3-benzyl-2,4,5-trioxoimidazolidin-1-yl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.0537
(E)-1-((2-fluorophenyl)(hydroxyimino)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0156
(E)-1-((4-chlorophenyl)(hydroxyimino)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0107
(E)-1-((4-ethylphenyl)(hydroxyimino)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0413
(E)-1-((4-fluorophenyl)(hydroxyimino)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0334
(E)-1-((hydroxyimino)(3-methoxyphenyl)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0252
(E)-1-((hydroxyimino)(4-methoxyphenyl)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0225
(E)-1-((hydroxyimino)(p-tolyl)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0373
(E)-1-((hydroxyimino)(phenyl)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0493
(Z)-1-((2-fluorophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.00012
(Z)-1-((3,4-dichlorophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0412
(Z)-1-((3-fluorophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0027
(Z)-1-((4-bromophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0014
(Z)-1-((4-chlorophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0034
(Z)-1-((4-ethylphenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0441
(Z)-1-((4-fluorophenyl)(hydroxyimino)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0251
(Z)-1-((hydroxyimino)(3-methoxyphenyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0165
(Z)-1-((hydroxyimino)(4-methoxyphenyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0159
(Z)-1-((hydroxyimino)(m-tolyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0072
(Z)-1-((hydroxyimino)(p-tolyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0214
(Z)-1-((hydroxyimino)(phenyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0399
(Z)-1-((hydroxyimino)(thiophen-2-yl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.0856
1-((methoxyimino)(phenyl)methyl)-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.103
1-(2-phenylethyl)imidazolidine-2,4,5-trione
Homo sapiens
pH and temperature not specified in the publication
0.0924
1-benzoyl-6-methylpyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH 8.4, 30°C
0.115
1-benzylimidazolidine-2,4,5-trione
Homo sapiens
pH and temperature not specified in the publication
0.128
1-[(2-methylphenyl)methyl]imidazolidine-2,4,5-trione
Homo sapiens
pH and temperature not specified in the publication
0.04
1H-pyrrolo[2,3-d]pyrimidine-2,4(3H,7H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
2,7-bis(methylsulfanyl)[1,2,4]triazolo[1,5-a][1,3,5]triazin-5(4H)-one
Homo sapiens
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.01084
2-(3,4-dichlorophenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0429
2-(3,4-dihydroxyphenyl)quinazolin-4(3H)-one
Homo sapiens
pH and temperature not specified in the publication
0.03178
2-(3-bromophenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.03442
2-(3-methylphenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.01309
2-(4-bromo-3-methylphenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.02206
2-(4-bromophenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.03158
2-(4-methylphenyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.05538
2-(benzylsulfanyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.03637
2-(diphenylmethyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
pH and temperature not specified in the publication
0.03154
2-(furan-2-yl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.05167
2-(methylsulfanyl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.1
2-(methylsulfanyl)-7-sulfanylidene-6,7-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-5(4H)-one
Homo sapiens
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.1
2-(methylsulfanyl)[1,2,4]triazolo[1,5-a][1,3,5]triazine-5,7(4H,6H)-dione
Homo sapiens
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.02453
2-(pyridin-2-yl)-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.013 - 0.04332
2-benzyl-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
0.03956
2-phenyl-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
0.1
2-phenyl-7-sulfanylidene-6,7-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-5(4H)-one
Homo sapiens
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.0462
2-phenylquinazolin-4(3H)-one
Homo sapiens
pH and temperature not specified in the publication
0.1
2-phenyl[1,2,4]triazolo[1,5-a][1,3,5]triazine-5,7(4H,6H)-dione
Homo sapiens
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.05988
2-[(2-phenylethyl)sulfanyl]-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.013
2-[(3,4-dichlorophenyl)methyl]-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
pH and temperature not specified in the publication
0.05925
2-[(3-phenylpropyl)sulfanyl]-5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.013
2-[[(5-chloro-2-methylidene-6-oxo-1,2,3,6-tetrahydropyrimidin-4-yl)methyl]sulfanyl]-7-phenyl-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
Homo sapiens
pH and temperature not specified in the publication
0.037
3,3'-(1,3,4-oxadiazole-2,5-diyl)dipyridine
Homo sapiens
pH and temperature not specified in the publication
0.0446
3-(((4-chlorophenyl)amino)methyl)-5-(2-iodophenyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.1833
3-((4-benzylpiperazin-1-yl)methyl)-5-(4-chlorophenyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.0547
3-((5-(4-chlorophenyl)-2-thioxo-1,3,4-oxadiazol-3(2H)-yl)methyl)thiazolidine-2,4-dione
Homo sapiens
pH 7.4, 25°C
0.0303
3-((benzylamino)methyl)-5-(4-chlorophenyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.106
3-(3-benzyl-2,4,5-trioxoimidazolidin-1-yl)propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0144
3-[(2-methoxy-6-nitroanilino)methyl]-5-(4-methylphenyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH and temperature not specified in the publication
0.061
3-[(2-methylphenyl)methyl]-1H-2-benzopyran-1-one
Homo sapiens
pH and temperature not specified in the publication
0.04061
3-[(3,4-dimethylanilino)methyl]-5-phenyl-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH and temperature not specified in the publication
0.04029
3-[(E)-[(2,4-dichlorophenyl)imino]methyl]-4H-1-benzopyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.01977
3-[(E)-[(3-methoxy-4-methylphenyl)imino]methyl]-4H-1-benzopyran-4-one
Homo sapiens
pH and temperature not specified in the publication
0.04
3-[2,4,5-trioxo-3-(2-phenylethyl)imidazolidin-1-yl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.088
3-[3-[(2-methylphenyl)methyl]-2,4,5-trioxoimidazolidin-1-yl]propanamide
Homo sapiens
pH and temperature not specified in the publication
0.0146
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(1-(4-nitrophenyl)ethylidene)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0011
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(2,3,4-trihydroxybenzylidene)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0546
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(2,3,4-trimethoxybenzylidene)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0063
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(2-nitrobenzylidene)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0473
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(3,4,5-trimethoxybenzylidene)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0283
4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)-N'-(4-(phenoxymethyl)benzylidene)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.022
4-[(Z)-[(3-hydroxynaphthalen-2-yl)methylidene]amino]-1,5-dimethyl-2-phenylpyrazolidin-3-one
Homo sapiens
pH and temperature not specified in the publication
0.067
5'-O-trityl-inosine
0.0872
5-(2-chlorophenyl)-3-(((4-chlorophenyl)amino)(phenyl)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.0464
5-(2-chlorophenyl)-3-((thiazol-2-ylamino)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.0384
5-(4-chlorophenyl)-3-(((2-nitrophenyl)amino)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.0693
5-(4-chlorophenyl)-3-(((3,3-diphenylpropyl)amino)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.0237
5-(4-chlorophenyl)-3-(((4-hydroxyphenyl)amino)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.0297
5-(4-chlorophenyl)-3-((2-methyl-1H-imidazol-1-yl)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.0582
5-(4-chlorophenyl)-3-((4-(2-methoxyphenyl)piperazin-1-yl)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.0832
5-(4-chlorophenyl)-3-((4-cyclohexylpiperazin-1-yl)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.0506
5-(4-chlorophenyl)-3-((cyclohexylamino)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.0228
5-(4-chlorophenyl)-3-((dicyclohexylamino)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.1171
5-(4-chlorophenyl)-3-((naphthalen-1-ylamino)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.1505
5-(4-chlorophenyl)-3-((thiazol-2-ylamino)methyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH 7.4, 25°C
0.03824
5-(4-hydroxyphenyl)-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH and temperature not specified in the publication
0.1112
5-(benzylsulfanyl)-2-phenyl-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
pH and temperature not specified in the publication
0.09505
5-(methylsulfanyl)-2-phenyl-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
pH and temperature not specified in the publication
0.038
5-bromo-6-(3'-methylimidazol-1-yl)uracil
Homo sapiens
IC50: 0.038 mM
0.16
5-bromo-6-[(2'-nitroimidazol-1'-yl)methyl]uracil
Homo sapiens
IC50: 0.16 mM
0.017
5-bromo-6-[(3-methylimidazol-1-yl)methyl]uracil
Homo sapiens
IC50: 0.017 mM
0.181
5-bromo-6-[(4'-nitroimidazol-1'-yl)methyl]uracil
Homo sapiens
IC50: 0.181 mM
0.0056
5-bromo-6-[[(1,3-dihydroxypropan-2-yl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.04 - 0.1
5-bromo-6-[[(2,3-dihydroxypropyl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
0.024
5-bromo-6-[[(2-hydroxyethyl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.035
5-chloro-6-(3'-methylimidazol-1-yl)uracil
Homo sapiens
IC50: 0.035 mM
0.115
5-chloro-6-[(2'-nitroimidazol-1'-yl)methyl]uracil
Homo sapiens
IC50: 0.115 mM
0.018
5-chloro-6-[(3-methylimidazol-1-yl)methyl]uracil
Homo sapiens
IC50: 0.018 mM
0.2
5-chloro-6-[(4'-nitroimidazol-1'-yl)methyl]uracil
Homo sapiens
IC50: 0.2 mM
0.00036
5-chloro-6-[([4-oxo-8-[4-(pentafluoro-lambda6-sulfanyl)phenyl]-1,2,3,4-tetrahydropyrazolo[1,5-a][1,3,5]triazin-2-yl]sulfanyl)methyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.000035
5-chloro-6-[1-(2-iminopyrrolidinyl)methyl] uracil hydrochloride
Homo sapiens
pH and temperature not specified in the publication
0.000035
5-chloro-6-[1-(2-iminopyrrolidinyl)methyl]uracil
Homo sapiens
-
-
0.000023
5-chloro-6-[1-(2-iminopyrrolidinyl)methyl]uracilhydrochloride
Homo sapiens
in 0.1 M potassium phosphate buffer (pH 7.4), at 25°C
0.001
5-chloro-6-[[(1,3-dihydroxypropan-2-yl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.039
5-chloro-6-[[(2-hydroxyethyl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.034
5-iodo-6-[[(piperidin-1-yl)amino]methyl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.05
5-phenyl-1,3,4-oxadiazole-2(3H)-thione
Homo sapiens
pH and temperature not specified in the publication
0.03095
5-sulfanylidene-2-(thiophen-2-yl)-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.05813
5-sulfanylidene-5,6-dihydro[1,2,4]triazolo[1,5-a][1,3,5]triazin-7(4H)-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0032
5-[(E)-[2-(quinoxalin-2-yl)hydrazinylidene]methyl]benzene-1,2,4-triol
Homo sapiens
pH and temperature not specified in the publication
0.00012
6-(((1,3-dihydroxypropan-2-yl)amino)methyl)-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.11
6-(3-methylimidazol-1-yl)uracil
Homo sapiens
IC50: 0.110 mM
0.017
6-amino-5-bromopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.0068 - 0.017
6-amino-5-bromouracil
0.07
6-aminothymine
Homo sapiens
pH and temperature not specified in the publication
0.000019
6-[(2'-aminoimidazol-1'-yl)methyl]-5-bromouracil
Homo sapiens
IC50: 0.000019 mM
0.000049
6-[(2'-aminoimidazol-1'-yl)methyl]-5-chlorouracil
Homo sapiens
IC50: below 0.000049 mM
0.0001
6-[(2'-aminoimidazol-1'-yl)methyl]uracil
Homo sapiens
IC50: 0.0001 mM
0.2577
6-[(2'-nitroimidazol-1'-yl)methyl]uracil
Homo sapiens
IC50: 0.2577 mM
0.06
6-[(3-methylimidazol-1-yl)methyl]thymine
Homo sapiens
IC50: 0.06 mM
0.042
6-[(3-methylimidazol-1-yl)methyl]uracil
Homo sapiens
IC50: 0.042 mM
0.041
6-[(4'-aminoimidazol-1'-yl)methyl]-5-bromouracil
Homo sapiens
IC50: 0.041 mM
0.026
6-[(4'-aminoimidazol-1'-yl)methyl]-5-chlorouracil
Homo sapiens
IC50: 0.026 mM
0.143
6-[(4'-aminoimidazol-1'-yl)methyl]uracil
Homo sapiens
IC50: 0.143 mM
0.5
6-[(4'-nitroimidazol-1'-yl)methyl]uracil
Homo sapiens
IC50: 0.5 mM
0.0084
6-[(dimethylamino)methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.028
6-[(dipentylamino)methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.1
6-[(dipropylamino)methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
above, pH and temperature not specified in the publication
0.036
6-[[(2,3-dihydroxypropyl)(methyl)amino]methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.012
6-[[(2-hydroxyethyl)amino]methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.087
6-[[bis(2-ethoxyethyl)amino]methyl]-5-iodopyrimidine-2,4(1H,3H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.0066
7-(4-tert-butylphenyl)-2-sulfanylidene-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0015 - 0.0097
7-(4-tert-butylphenyl)-2-[[(5-chloro-2-methylidene-6-oxo-1,2,3,6-tetrahydropyrimidin-4-yl)methyl]sulfanyl]-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
0.1
7-(methylsulfanyl)-2-phenyl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5(4H)-one
Homo sapiens
-
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.03868 - 0.045
7-deazaxanthine
0.0462
7-phenyl-2-sulfanylidene-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0263
8-phenyl-2-sulfanylidene-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
Homo sapiens
pH and temperature not specified in the publication
0.00004
8-[4-(pentafluoro-lambda6-sulfanyl)phenyl]-2-sulfanylidene-2,3-dihydropyrazolo[1,5-a][1,3,5]triazin-4(1H)-one
Homo sapiens
pH and temperature not specified in the publication
0.342
ethyl (3-benzyl-2,4,5-trioxoimidazolidin-1-yl)acetate
Homo sapiens
pH and temperature not specified in the publication
0.357
ethyl [2,4,5-trioxo-3-(2-phenylethyl)imidazolidin-1-yl]acetate
Homo sapiens
pH and temperature not specified in the publication
0.303
ethyl [3-[(2-methylphenyl)methyl]-2,4,5-trioxoimidazolidin-1-yl]acetate
Homo sapiens
pH and temperature not specified in the publication
0.351
KIN56
Homo sapiens
-
IC50: 0.351 mM
0.0033
N'-(2,4-dichlorobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0185
N'-(2-cyanobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0073
N'-(2-hydroxy-3-methoxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0024
N'-(3,5-dichloro-2-hydroxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0011
N'-(3-aminobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0274
N'-(3-cyanobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0046
N'-(3-hydroxy-4-methoxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0188
N'-(4-(dimethylamino)benzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0164
N'-(4-chlorobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0221
N'-(4-cyanobenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0053
N'-(4-hydroxy-3,5-dimethoxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.006
N'-(4-hydroxy-3-methoxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0367
N'-(5-bromo-2-methoxybenzylidene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0394
N'-(anthracen-9-ylmethylene)-4-(5-(isoquinolin-3-yl)-1,3,4-oxadiazol-2-yl)benzohydrazide
Homo sapiens
pH 7.4, 25°C
0.0256
N-((5-(4-chlorophenyl)-2-thioxo-1,3,4-oxadiazole-3(2H)-yl)methyl)3(trifluoromethyl) benzamide
Homo sapiens
pH 7.4, 25°C
0.00382
N-(4-oxo-2-sulfanylidene-8-[[4-(trifluoromethyl)phenyl]methyl]-1,2,3,4-tetrahydropyrazolo[1,5-a][1,3,5]triazin-7-yl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.02992
N-(8-benzyl-4-oxo-2-sulfanylidene-1,2,3,4-tetrahydropyrazolo[1,5-a][1,3,5]triazin-7-yl)thiourea
Homo sapiens
pH and temperature not specified in the publication
0.077
NSC 65043
Homo sapiens
-
IC50: 0.077 mM
0.06545
symplocomoside
Homo sapiens
pH and temperature not specified in the publication
0.22567
symponoside
Homo sapiens
pH and temperature not specified in the publication
0.00003 - 0.035
TPI
0.085
[2,4,5-trioxo-3-(2-phenylethyl)imidazolidin-1-yl]acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.236
[3-[(2-methylphenyl)methyl]-2,4,5-trioxoimidazolidin-1-yl]acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.0017 - 0.027
[8-(2,4-dioxo-2,3,4,6-tetrahydro-1H-pyrrolo[3,4-d]pyrimidin-1-yl)octyl]phosphonic acid
0.0073 - 0.0151
[8-(2,4-dioxo-2,3,4,7-tetrahydro-1H-pyrrolo[2,3-d]pyrimidin-1-yl)octyl]phosphonic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00386
-
in normal uterine cervix tissue
0.00527
-
mean thymidine phosphorylase activity in population
0.01
-
mitochondrial neurogastrointestinal encephalomyopathy syndrome patient, leukocytes
0.04176
-
in cancerous uterine cervix tissue
0.114
purified native enzyme, pH 8.0, 37°C, substrate uridine
0.2 - 0.32
-
leukocytes of heterozygous individuals in enzyme mutation and mitochondrial neurogastrointestinal encephalomyopathy syndrome
0.24
crude extract, at pH 7.5 at 37°C
0.36 - 0.8
-
wild-type activity in leukocytes
1.5
purified native enzyme, pH 8.0, 37°C, substrate 5-fluorouridine or 5'-deoxy-5-fluorouridine
1100
-
-
18480
purified native enzyme, pH 8.0, 37°C
4.3
after 17.9fold purification, at pH 7.5 at 37°C
5.55
purified native enzyme, pH 8.0, 37°C, substrate thymidine
8.1
purified native enzyme, pH 8.0, 37°C, substrate 5-fluoro-2'-deoxyuridine
8.91
purified native enzyme, pH 8.0, 37°C, substrate 2'-deoxyuridine
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
assay at, pH 10 is used because 2-deoxy-D-ribose 1-phosphate is heat labile at pH 7.4
5 - 8.5
thymidine phosphorolysis
5.5
thymine production, assay at
7.6
assay at
7.8
-
assay at
8.4
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
activity range of phosphorolysis of thymidine, profile overview
5 - 9
activity range of synthesis of thymidine, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 37
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
thymidine phosphorylase mRNA levels are low and statistically not different in whole basal cell carcinoma cells and normal skin and are strongly downregulated in laser capture microdissected-basal cell carcinoma cells as compared with laser capture microdissected-normal epidermis
Manually annotated by BRENDA team
higher PyNpase levels in tumor tissue than in normal tissue or tissue adjacent to the tumor, PyNpase levels independent of age, gender, history of recurrence, multiplicity, tumor size, tumor shape, pathological stage (Ta, T1-4), PyNpase levels differ between histological stages being highest in G3, and between papillary versus non-papillary growth pattern, higher PyPnase levels in high-risk group (G3 or Tis or T2) than in low-risk group (primary, single, G1 and Ta)
Manually annotated by BRENDA team
-
presurgery serum from 47 patients with ovarian cancer, and control serum from women with normal ovaries, treated surgically due to nononcological reasons. Significant higher enzyme activity in malignant serum specimen from ovarian cancer patients when compared to the control
Manually annotated by BRENDA team
-
thymidine phosphorylase shows a characteristic pattern of distribution dependent on the phase of the menstrual cycle: enzyme expression moves from stroma to epithelium as the cycle progresses34 and is inversely correlated with estradiol concentrations
Manually annotated by BRENDA team
patients with PD-ECGF/TP-positive tumors have a poorer prognosis than those with negative tumors
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
epidermoid
Manually annotated by BRENDA team
-
cholangiocarcinoma-derived cell line, which has a naturally high level of endogenous thymidine phosphorylase
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
from peripheral blood
Manually annotated by BRENDA team
-
the cytoplasmic level of heterogeneous nuclear ribonucleoprotein K is significantly correlated with the elevated expression of thymidine phosphorylase, and high levels of both proteins are predictive of a poor prognosis in nasopharyngeal carcinoma
Manually annotated by BRENDA team
-
the enzyme is strongly induced in the serum-deprived nasopharyngeal carcinoma cells, the serum deprivation-triggered upregulation of the enzyme is due to mRNA stabilization, not protein stabilization or transcriptional activation requiring the mRNA CU-rich element sequence and heterogeneous nuclear ribonucleoprotein K, overview
Manually annotated by BRENDA team
-
the enzyme is strongly induced in the serum-deprived nasopharyngeal carcinoma cells, the serum deprivation-triggered upregulation of the enzyme is due to mRNA stabilization, not protein stabilization or transcriptional activation requiring the mRNA CU-rich element sequence and heterogeneous nuclear ribonucleoprotein K, overview
Manually annotated by BRENDA team
-
malignant tissue
Manually annotated by BRENDA team
-
tissue from 47 patiens with ovarian cancer after surgery. Significant higher enzyme activity in malignant tissue from ovarian cancer patients when compared to the control
Manually annotated by BRENDA team
-
tissue from 47 patiens with ovarian cancer after surgery. Significant higher enzyme activity in malignant tissue from ovarian cancer patients when compared to the control
Manually annotated by BRENDA team
-
shows significantly greater activity in cancer tissues than in normal tissues
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
neutrophil in gastric cancer tissue
Manually annotated by BRENDA team
additional information
-
the mechanism behind the secretion of thymidine phosphorylase is possibly a posttranslational process whereby serine residues of the enzyme are covalently linked to phosphate groups of nucleotides, leading to the formation of a nucleotidylated protein that can be secreted
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TYPH_HUMAN
482
0
49955
Swiss-Prot
other Location (Reliability: 2)
E5KRG5_HUMAN
482
0
49955
TrEMBL
other Location (Reliability: 2)
B2RBL3_HUMAN
482
0
49923
TrEMBL
other Location (Reliability: 2)
B3KQ24_HUMAN
174
0
17286
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
gel filtration
110000
120000
-
gel filtration
121000
gel filtration
45000
48855
2 * 48855, mass spectrometry
49024
2 * 49024, calculated from amino acid sequence
50000
2 * 50000, SDS-PAGE
52000
-
recombinant enzyme lacking 10 amino acid residues, SDS-PAGE
55000
58000
-
2 * 58000, SDS-PAGE, enzyme is capable of being converted to a less active form larger in MW and possibly trimeric or tetrameric in structure
60000
-
2 * 60000, SDS-PAGE
90000
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
two alternative enzyme forms, a 27 kDa splice variant and another form containing five additional amino acids on the N-terminus, the second form is processed at Thr6 instead of Ala11
additional information
-
the mechanism behind the secretion of thymidine phosphorylase is possibly a posttranslational process whereby serine residues of the enzyme are covalently linked to phosphate groups of nucleotides, leading to the formation of a nucleotidylated protein that can be secreted
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of crystal structure of recombinant human TP in complex with 5-iodouracil (5IUR) at 3.0 A and 2.5 A resolutions, respectively
enzyme complexed with TPI
-
purified recombinant thymidine phosphorylase, free and in complex with 5-iodouracil, X-ray diffraction structure determination and analysis at 3.0 A and 2.5 A resolutions, respectively
structure of enzyme from crystals grown in the presence of thymidine
structure of HTP bound to the small molecule inhibitor 5-chloro-6-[1-(2-iminopyrrolidinyl)methyl]uracil hydrochloride, glutathione S-transferase fused to thymidine phosphorylase residues 12–482 (based on Swissprot accession number P19971) via a thrombin-cleavable linker, crystallizationd at 15°C using the hanging-drop vapor method
X-ray diffraction structure determination and analysis of the free enzyme at 3.5 A resolution, and of the in complex with the small and potent inhibitor 5-chloro-6-[1-(2-iminopyrrolidinyl)methyl] uracil at 2.1 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D203A
H116F
site-directed mutagenesis, inactive mutant
H116K
site-directed mutagenesis, inactive mutant
I214A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K115A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K115E
L148R
R202E
site-directed mutagenesis, inactive mutant
R202S
S217G
site-directed mutagenesis, inactive mutant
Y199A
site-directed mutagenesis, inactive mutant
Y199F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y199L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
30 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to repeated freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, phosphate buffer containing 2% mannitol, stable for over 1 year, human enzyme
-
4°C, storage results in a decrease of the 120 kDA component, an increase of the high molecular weight component, and a loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
98% purity
-
ammonium sulfate fractionation
-
chromatography
-
homogeneity
-
native enzyme 5130fold from liver cytosol to apparent homogeneity by anion exchange and hydrophobic interaction chromatography, and dialysis, followed by hydroxyapatite chromatography
Ni+-chelation-affinity chromatography
-
Q-Sepharose column chromatography and phenyl Sepharose column chromatography
recombinant enzyme from Escherichia coli strain BL21(DE3) by calmodulin affinity chromatography, cleavage of the calmodulin binding protein tag by enterokinase, removal by chromatography on soybean trypsin inhibitor-sepharose
-
recombinant wild-type and mutan enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
separation of uridine phosphorylase and thymidine phosphorylase activities
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Chinese hamster V-79 cells
-
expressed in CHO cells
-
expressed in Colo-320TP1 and C26A cells
-
expressed in Escherichia coli
-
expressed in Escherichia coli Rosetta (DE3) cells
expressed in Jurkat cells
-
expressed in V-79 hamster cells
-
expressed in V79 Chinese hamster cells
-
expression in KB cells
expression in rat vascular smooth muscle cell
-
expression of the calmodulin binding protein-tagged enzyme in Escherichia coli strain BL21(DE3) cells transformed with the pCal-n-EK/TP and pGroESL vectors
-
expression of wild-type and mutan enzymes in Escherichia coli strain BL21(DE3)
recombinant enzyme lacks 10 amino acids at amino-terminus
-
transfected into colon cancer cell line Colo320
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
capecitabine does not affect enzyme activity and expression
-
chorionic gonadotropin36 and a combination of progesterone and transforming growth factor b1 upregulate the enzyme expression. The enzyme is also upregulated in several diseases, detailed overview
-
EGF receptor inhibition may lead to TP overexpression, and tissue hypoxia secondary to low hemoglobin levels may induce TP overexpression
the enzyme expression is is inversely correlated with estradiol concentrations in the endometrium
-
the enzyme is highly upregulated in a variety of solid tumours
the enzyme is strongly induced in the serum-deprived nasopharyngeal carcinoma cell lines TW-01, TW-02, and TW-04, the serum deprivation-triggered upregulation of the enzyme is due to mRNA stabilization, not protein stabilization or transcriptional activation requiring the mRNA CU-rich element sequence and heterogeneous nuclear ribonucleoprotein K, mechanism and kinetics, overview
-
treatment with 0.005-0.04 mM tamoxifen decreases mRNA and protein levels through AKT inactivation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
methods to measure thymidine and deoxyuridine concentrations and thymidine phosphorylase activity in biological samples. Thymidine phosphorylase activity can be measured by an endpoint determination of the thymine formed after 1 h incubation of the buffy coat homogenate in the presence of a large excess of its substrate thymidine, either spectrophotometrically or by HPLC-UV. The protocols allow the detection of thymidine phosphorylase dysfunction in patients with mitochondrial neurogastrointestinal encephalomyopathy, MNGIE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zimmerman, M.; Seidenberg, J.
Deoxyribosyl transfer. I. Thymidine phosphorylase and nucleoside deoxyribosyltransferase in normal and malignant tissues
J. Biol. Chem.
239
2618-2621
1964
Cavia porcellus, Homo sapiens, Mesocricetus auratus, Rattus norvegicus
Manually annotated by BRENDA team
Sugata, S.; Kono, A.; Hara, Y.; Karube, Y.; Matsushima, Y.
Partial purification of a thymidine phosphorylase from human gastric cancer
Chem. Pharm. Bull.
34
1219-1222
1986
Homo sapiens
Manually annotated by BRENDA team
Zimmerman, M.
Deoxyribosyl transfer. II. Nucleoside:pyrimidine deoxyribosyltransferase activity of three partially purified thymidine phosphorylases
J. Biol. Chem.
239
2622-2627
1964
Escherichia coli, Escherichia coli B / ATCC 11303, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Desgranges, C.; Razaka, G.; Rabaud, M.; Bricaud, H.
Catabolism of thymidine in human blood platelets: purification and properties of thymidine phosphorylase
Biochim. Biophys. Acta
654
211-218
1981
Homo sapiens
Manually annotated by BRENDA team
Kubilus, J.; Lee, L.D.; Baden, H.P.
Purification of thymidine phosphorylase from human amniochorion
Biochim. Biophys. Acta
527
221-228
1978
Homo sapiens
Manually annotated by BRENDA team
el Kouni, M.H.; el Kouni, M.M.; Naguib, F.N.
Differences in activities and substrate specificity of human and murine pyrimidine nucleoside phosphorylases: implications for chemotherapy with 5-fluoropyrimidines
Cancer Res.
53
3687-3693
1993
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Pizzorno, G.; Cao, D.; Leffert, J.J.; Russell, R.L.; Zhang, D.; Handschumacher, R.E.
Homeostatic control of uridine and the role of uridine phosphorylase: a biological and clinical update
Biochim. Biophys. Acta
1587
133-144
2002
Homo sapiens
Manually annotated by BRENDA team
de Bruin, M.; Smid, K.; Laan, A.C.; Noordhuis, P.; Fukushima, M.; Hoekman, K.; Pinedo, H.M.; Peters, G.J.
Rapid disappearance of deoxyribose-1-phosphate in platelet derived endothelial cell growth factor/thymidine phosphorylase overexpressing cells
Biochem. Biophys. Res. Commun.
301
675-679
2003
Homo sapiens
Manually annotated by BRENDA team
Finnis, C.; Dodsworth, N.; Pollitt, C.E.; Carr, G.; Sleep, D.
Thymidine phosphorylase activity of platelet-derived endothelial cell growth factor is responsible for endothelial cell mitogenicity
Eur. J. Biochem.
212
201-210
1993
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Liu, M.; Cao, D.; Russell, R.; Handschumacher, R.E.; Pizzorno, G.
Expression, characterization, and detection of human uridine phosphorylase and identification of variant uridine phosphorolytic activity in selected human tumors
Cancer Res.
58
5418-5424
1998
Homo sapiens
Manually annotated by BRENDA team
Miszczak-Zaborska, E.; Wozniak, K.
The activity of thymidine phosphorylase obtained from human uterine leiomyomas and studied in the presence of pyrimidine derivatives
Z. Naturforsch. c
52
670-675
1997
Homo sapiens
Manually annotated by BRENDA team
Miyadera, K.; Dohmae, N.; Takio, K.; Sumizawa, T.; Haraguchi, M.; Furukawa, T.; Yamada, Y.; Akiyama, S.
Structural characterization of thymidine phosphorylase purified from human placenta
Biochem. Biophys. Res. Commun.
212
1040-1045
1995
Homo sapiens
Manually annotated by BRENDA team
Miyadera, K.; Sumizawa, T.; Haraguchi, M.; Yoshida, H.; Konstanty, W.; Yamada, Y.; Akiyama, S.
Role of thymidine phosphorylase activity in the angiogenic effect of platelet derived endothelial cell growth factor/thymidine phosphorylase
Cancer Res.
55
1687-1690
1995
Homo sapiens
Manually annotated by BRENDA team
Sumizawa, T.; Furukawa, T.; Haraguchi, M.; Yoshimura, A.; Takeyasu, A.; Ishizawa, M.; Yamada, Y.; Akiyama, S.
Thymidine phosphorylase activity associated with platelet-derived endothelial cell growth factor
J. Biochem.
114
9-14
1993
Homo sapiens
Manually annotated by BRENDA team
Klein, R.S.; Lenzi, M.; Lim, T.H.; Hotchkiss, K.A.; Wilson, P.; Schwartz, E.L.
Novel 6-substituted uracil analogs as inhibitors of the angiogenic actions of thymidine phosphorylase
Biochem. Pharmacol.
62
1257-1263
2001
Homo sapiens
Manually annotated by BRENDA team
Focher, F.; Spadari, S.
Thymidine phosphorylase: a two-face janus in anticancer chemotherapy
Curr. Cancer Drug Targets
1
141-153
2001
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Yang, Q.; Yoshimura, G.; Mori, I.; Sakurai, T.; Kakudo, K.
Thymidine phosphorylase and breast carcinoma
Anticancer Res.
22
2355-2360
2002
Homo sapiens
Manually annotated by BRENDA team
McNally, V.A.; Gbaj, A.; Douglas, K.T.; Stratford, I.J.; Jaffar, M.; Freeman, S.; Bryce, R.A.
Identification of a novel class of inhibitor of human and Escherichia coli thymidine phosphorylase by in silico screening
Bioorg. Med. Chem. Lett.
13
3705-3709
2003
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Akiyama, S.; Furukawa, T.; Sumizawa, T.; Takebayashi, Y.; Nakajima, Y.; Shimaoka, S.; Haraguchi, M.
The role of thymidine phosphorylase, an angiogenic enzyme, in tumor progression
Cancer Sci.
95
851-857
2004
Homo sapiens
Manually annotated by BRENDA team
De Bruin, M.; Van Capel, T.; Smid, K.; Fukushima, M.; Hoekman, K.; Pinedo, H.M.; Peters, G.J.
The effect of fluoropyrimidines with or without thymidine phosphorylase inhibitor on the expression of thymidine phosphorylase
Eur. J. Pharmacol.
491
93-99
2004
Homo sapiens
Manually annotated by BRENDA team
Miszczak-Zaborska, E.; Wojcik-Krowiranda, K.; Kubiak, R.; Bienkiewicz, A.; Bartkowiak, J.
The activity of thymidine phosphorylase as a new ovarian tumor marker
Gynecol. Oncol.
94
86-92
2004
Homo sapiens
Manually annotated by BRENDA team
Liekens, S.; Hernandez, A.I.; Ribatti, D.; De Clercq, E.; Camarasa, M.J.; Perez-Perez, M.J.; Balzarini, J.
The nucleoside derivative 5'-O-trityl-inosine (KIN59)suppresses thymidine phosphorylase-triggered angiogenesis via a noncompetitive mechanism of action
J. Biol. Chem.
279
29598-29605
2004
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Reigan, P.; Edwards, P.N.; Gbaj, A.; Cole, C.; Barry, S.T.; Page, K.M.; Ashton, S.E.; Luke, R.W.; Douglas, K.T.; Stratford, I.J.; Jaffar, M.; Bryce, R.A.; Freeman, S.
Aminoimidazolylmethyluracil analogues as potent inhibitors of thymidine phosphorylase and their bioreductive nitroimidazolyl prodrugs
J. Med. Chem.
48
392-402
2005
Escherichia coli, Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Kobayashi, M.; Okamoto, K.; Akimori, T.; Tochika, N.; Yoshimoto, T.; Okabayashi, T.; Sugimoto, T.; Araki, K.
Localization of thymidine phosphorylase in advanced gastric and colorectal cancer
J. Mol. Histol.
35
69-74
2004
Homo sapiens
Manually annotated by BRENDA team
Norman, R.A.; Barry, S.T.; Bate, M.; Breed, J.; Colls, J.G.; Ernill, R.J.; Luke, R.W.; Minshull, C.A.; McAlister, M.S.; McCall, E.J.; McMiken, H.H.; Paterson, D.S.; Timms, D.; Tucker, J.A.; Pauptit, R.A.
Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor
Structure
12
75-84
2004
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Ma, T.; Zhu, Z.G.; Ji, Y.B.; Zhang, Y.; Yu, Y.Y.; Liu, B.Y.; Yin, H.R.; Lin, Y.Z.
Correlation of thymidylate synthase, thymidine phosphorylase and dihydropyrimidine dehydrogenase with sensitivity of gastrointestinal cancer cells to 5-fluorouracil and 5-fluoro-2'-deoxyuridine
World J. Gastroenterol.
10
172-176
2004
Homo sapiens
Manually annotated by BRENDA team
Zhang, J.M.; Mizoi, T.; Shiiba, K.; Sasaki, I.; Matsuno, S.
Expression of thymidine phosphorylase by macrophages in colorectal cancer tissues
World J. Gastroenterol.
10
545-549
2004
Homo sapiens
Manually annotated by BRENDA team
Liakakos, T.; Troupis, T.; Ghiconti, I.; Triantafyllidis, S.; Macheras, A.; Karatzas, G.; Pavlakis, K.
Immunohistochemical localization of thymidine phosphorylase in gastric cancer: is there a role of the differential expression in tumor cells and associated stromal cells?
Anticancer Res.
26
3899-3904
2006
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
El Omari, K.; Bronckaers, A.; Liekens, S.; Perez-Perez, M.J.; Balzarini, J.; Stammers, D.K.
Structural basis for non-competitive product inhibition in human thymidine phosphorylase: implications for drug design
Biochem. J.
399
199-204
2006
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Jeung, H.C.; Che, X.F.; Haraguchi, M.; Zhao, H.Y.; Furukawa, T.; Gotanda, T.; Zheng, C.L.; Tsuneyoshi, K.; Sumizawa, T.; Roh, J.K.; Akiyama, S.
Protection against DNA damage-induced apoptosis by the angiogenic factor thymidine phosphorylase
FEBS Lett.
580
1294-1302
2006
Homo sapiens (P19971)
Manually annotated by BRENDA team
Hirano, M.; Lagier-Tourenne, C.; Valentino, M.L.; Marti, R.; Nishigaki, Y.
Thymidine phosphorylase mutations cause instability of mitochondrial DNA
Gene
354
152-156
2005
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Passantino, L.; Patruno, R.; Valerio, P.; Penna, A.; Mazzone, F.; Zito, A.F.; Catalano, V.; Pellecchia, A.; Jirillo, E.; Ranieri, G.
Thymidine phosphorylase profiles in nonmalignant and malignant pancreatic tissue. Potential therapeutic role of capecitabine on tumoral and endothelial cells and tumor-infiltrating macrophages
Immunopharmacol. Immunotoxicol.
27
95-107
2005
Homo sapiens
Manually annotated by BRENDA team
Temmink, O.H.; de Bruin, M.; Laan, A.C.; Turksma, A.W.; Cricca, S.; Masterson, A.J.; Noordhuis, P.; Peters, G.J.
The role of thymidine phosphorylase and uridine phosphorylase in (fluoro)pyrimidine metabolism in peripheral blood mononuclear cells
Int. J. Biochem. Cell Biol.
38
1759-1765
2006
Homo sapiens (P19971)
Manually annotated by BRENDA team
Temmink, O.H.; de Bruin, M.; Turksma, A.W.; Cricca, S.; Laan, A.C.; Peters, G.J.
Activity and substrate specificity of pyrimidine phosphorylases and their role in fluoropyrimidine sensitivity in colon cancer cell lines
Int. J. Biochem. Cell Biol.
39
565-575
2007
Homo sapiens
Manually annotated by BRENDA team
Ezaki, T.; Ikegami, T.; Maeda, T.; Yamada, T.; Ishida, T.; Hashizume, M.; Maehara, Y.
Prognostic value of thymidine phosphorylase activity in liver tissue adjacent to hepatocellular carcinoma
Int. J. Clin. Oncol.
10
171-176
2005
Homo sapiens
Manually annotated by BRENDA team
van Kuilenburg, A.B.; Zoetekouw, L.
Determination of thymidine phosphorylase activity by a non-radiochemical assay using reversed-phase high-performance liquid chromatography
J. Chromatogr. B
820
271-275
2005
Homo sapiens
Manually annotated by BRENDA team
Meropol, N.J.; Gold, P.J.; Diasio, R.B.; Andria, M.; Dhami, M.; Godfrey, T.; Kovatich, A.J.; Lund, K.A.; Mitchell, E.; Schwarting, R.
Thymidine phosphorylase expression is associated with response to capecitabine plus irinotecan in patients with metastatic colorectal cancer
J. Clin. Oncol.
24
4069-4077
2006
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Edwards, P.N.
A kinetic, modeling and mechanistic re-analysis of thymidine phosphorylase and some related enzymes
J. Enzyme Inhib. Med. Chem.
21
483-499
2006
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Allan, A.L.; Gladstone, P.L.; Price, M.L.; Hopkins, S.A.; Juarez, J.C.; Donate, F.; Ternansky, R.J.; Shaw, D.E.; Ganem, B.; Li, Y.; Wang, W.; Ealick, S.
Synthesis and evaluation of multisubstrate bicyclic pyrimidine nucleoside inhibitors of human thymidine phosphorylase
J. Med. Chem.
49
7807-7815
2006
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
McNally, V.A.; Rajabi, M.; Gbaj, A.; Stratford, I.J.; Edwards, P.N.; Douglas, K.T.; Bryce, R.A.; Jaffar, M.; Freeman, S.
Design, synthesis and enzymatic evaluation of 6-bridged imidazolyluracil derivatives as inhibitors of human thymidine phosphorylase
J. Pharm. Pharmacol.
59
537-547
2007
Homo sapiens, Homo sapiens (P19971)
Manually annotated by BRENDA team
Liekens, S.; Balzarini, J.; Hernandez, A.I.; De Clercq, E.; Priego, E.M.; Camarasa, M.J.; Perez-Perez, M.J.
Thymidine phosphorylase is noncompetitively inhibited by 5-O-trityl-inosine (KIN59) and related compounds
Nucleosides Nucleotides Nucleic Acids
25
975-980
2006
Escherichia coli, Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Chujo, M.; Miura, T.; Kawano, Y.; Miyawaki, M.; Imakiire, T.; Hayashita, Y.; Kawahara, K.
Thymidine phosphorylase levels and dihydropyrimidine dehydrogenase levels in non-small cell lung cancer tissues
Oncol. Rep.
16
777-780
2006
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Oberemm, A.; Meckert, C.; Brandenburger, L.; Herzig, A.; Lindner, Y.; Kalenberg, K.; Krause, E.; Ittrich, C.; Kopp-Schneider, A.; Stahlmann, R.; Richter-Reichhelm, H.; Gundert-Remy, U.
Differential signatures of protein expression in marmoset liver and thymus induced by single-dose TCDD treatment
Toxicology
206
33-48
2005
Homo sapiens (P19971)
Manually annotated by BRENDA team
Ogiuchi, Y.; Maruoka, Y.; Ando, T.; Kobayashi, M.; Ogiuchi, H.
Thymidylate synthase, thymidine phosphorylase and orotate phosphoribosyl transferase levels as predictive factors of chemotherapy in oral squamous cell carcinoma
Acta Histochem. Cytochem.
41
39-46
2008
Homo sapiens
Manually annotated by BRENDA team
Jensen, S.A.; Vainer, B.; Witton, C.J.; Jorgensen, J.T.; Sorensen, J.B.
Prognostic significance of numeric aberrations of genes for thymidylate synthase, thymidine phosphorylase and dihydrofolate reductase in colorectal cancer
Acta Oncol.
47
1054-1061
2008
Homo sapiens
Manually annotated by BRENDA team
Ijuin, T.; Nibu, K.; Doi, K.; Inoue, H.; Saitoh, M.; Ohtsuki, N.; Makino, K.; Amatsu, M.
Thymidine phosphorylase mRNA level predicts survival of patients with advanced oropharyngeal cancer
Acta Otolaryngol.
127
305-311
2007
Homo sapiens
Manually annotated by BRENDA team
Puglisi, F.; Cardellino, G.G.; Crivellari, D.; Di Loreto, C.; Magri, M.D.; Minisini, A.M.; Mansutti, M.; Andreetta, C.; Russo, S.; Lombardi, D.; Perin, T.; Damante, G.; Veronesi, A.
Thymidine phosphorylase expression is associated with time to progression in patients receiving low-dose, docetaxel-modulated capecitabine for metastatic breast cancer
Ann. Oncol.
19
1541-1546
2008
Homo sapiens
Manually annotated by BRENDA team
Soong, R.; Shah, N.; Salto-Tellez, M.; Tai, B.C.; Soo, R.A.; Han, H.C.; Ng, S.S.; Tan, W.L.; Zeps, N.; Joseph, D.; Diasio, R.B.; Iacopetta, B.
Prognostic significance of thymidylate synthase, dihydropyrimidine dehydrogenase and thymidine phosphorylase protein expression in colorectal cancer patients treated with or without 5-fluorouracil-based chemotherapy
Ann. Oncol.
19
915-919
2008
Homo sapiens
Manually annotated by BRENDA team
Andreetta, C.; Puppin, C.; Minisini, A.; Valent, F.; Pegolo, E.; Damante, G.; Di Loreto, C.; Pizzolitto, S.; Pandolfi, M.; Fasola, G.; Piga, A.; Puglisi, F.
Thymidine phosphorylase expression and benefit from capecitabine in patients with advanced breast cancer
Ann. Oncol.
20
265-271
2008
Homo sapiens
Manually annotated by BRENDA team
Puglisi, F.; Andreetta, C.; Valent, F.; Minisini, A.M.; Rijavec, E.; Russo, S.; Mansutti, M.; Cardellino, G.; Pizzolitto, S.; Di Loreto, C.
Anthracyclines and taxanes induce the upregulation of thymidine phosphorylase in breast cancer cells
Anticancer Drugs
18
883-888
2007
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Koizumi, W.; Okayasu, I.; Hyodo, I.; Sakamoto, J.; Kojima, H.; Kojima, H.
Prediction of the effect of capecitabine in gastric cancer by immunohistochemical staining of thymidine phosphorylase and dihydropyrimidine dehydrogenase
Anticancer Drugs
19
819-824
2008
Homo sapiens
Manually annotated by BRENDA team
Ogata, Y.; Sasatomi, T.; Mori, S.; Matono, K.; Ishibashi, N.; Akagi, Y.; Fukushima, T.; Murakami, H.; Ushijima, M.; Shirouzu, K.
Significance of thymidine phosphorylase in metronomic chemotherapy using CPT-11 and doxifluridine for advanced colorectal carcinoma
Anticancer Res.
27
2605-2611
2007
Homo sapiens
Manually annotated by BRENDA team
Sakurai, Y.; Yoshida, I.; Kamoshida, S.; Inaba, K.; Isogaki, J.; Komori, Y.; Uyama, I.; Tsutsumi, Y.
Changes of gene expression of thymidine phosphorylase, thymidylate synthase, dihydropyrimidine dehydrogenase after the administration of 5-deoxy-5-fluorouridine, paclitaxel and its combination in human gastric cancer xenografts
Anticancer Res.
28
1593-1602
2008
Homo sapiens, Mus musculus (Q99N42), Mus musculus
Manually annotated by BRENDA team
Ikeda, R.; Tajitsu, Y.; Iwashita, K.; Che, X.F.; Yoshida, K.; Ushiyama, M.; Furukawa, T.; Komatsu, M.; Yamaguchi, T.; Shibayama, Y.; Yamamoto, M.; Zhao, H.Y.; Arima, J.; Takeda, Y.; Akiyama, S.; Yamada, K.
Thymidine phosphorylase inhibits the expression of proapoptotic protein BNIP3
Biochem. Biophys. Res. Commun.
370
220-224
2008
Homo sapiens
Manually annotated by BRENDA team
Liekens, S.; Bronckaers, A.; Perez-Perez, M.J.; Balzarini, J.
Targeting platelet-derived endothelial cell growth factor/thymidine phosphorylase for cancer therapy
Biochem. Pharmacol.
74
1555-1567
2007
Homo sapiens
Manually annotated by BRENDA team
Pomeisl, K.; Holy, A.; Votruba, I.; Pohl, R.
Syntheses of N3-substituted thymine acyclic nucleoside phosphonates and a comparison of their inhibitory effect towards thymidine phosphorylase
Bioorg. Med. Chem. Lett.
18
1364-1367
2008
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Bartsch, R.; Steger, G.G.; Forstner, B.; Wenzel, C.; Pluschnig, U.; Rizovski, B.; Altorjai, G.; Zielinski, C.C.; Mader, R.M.
Expression of thymidine phosphorylase in peripheral blood cells of breast cancer patients is not increased by paclitaxel
BMC Clin. Pharmacol.
7
7-7
2007
Homo sapiens
Manually annotated by BRENDA team
Graham-Cole, C.L.; Thomas, H.D.; Taylor, G.A.; Newell, D.R.; Melton, R.G.; Hesp, R.; Boddy, A.V.
An evaluation of thymidine phosphorylase as a means of preventing thymidine rescue from the thymidylate synthase inhibitor raltitrexed
Cancer Chemother. Pharmacol.
59
197-206
2007
Homo sapiens
Manually annotated by BRENDA team
Guarcello, V.; Blanquicett, C.; Naguib, F.N.; El Kouni, M.H.
Suppression of thymidine phosphorylase expression by promoter methylation in human cancer cells lacking enzyme activity
Cancer Chemother. Pharmacol.
62
85-96
2008
Homo sapiens
Manually annotated by BRENDA team
Saif, M.W.; Black, G.; Roy, S.; Bell, D.; Russo, S.; Eloubeidi, M.A.; Steg, A.; Johnson, M.R.; Zelterman, D.; Diasio, R.B.
Phase II study of capecitabine with concomitant radiotherapy for patients with locally advanced pancreatic cancer: up-regulation of thymidine phosphorylase
Cancer J.
13
247-256
2007
Homo sapiens
Manually annotated by BRENDA team
Layman, R.M.; Thomas, D.G.; Griffith, K.A.; Smerage, J.B.; Helvie, M.A.; Roubidoux, M.A.; Diehl, K.M.; Newman, L.A.; Sabel, M.S.; Hayman, J.A.; Pierce, L.J.; Hayes, D.F.; Schott, A.F.
Neoadjuvant docetaxel and capecitabine and the use of thymidine phosphorylase as a predictive biomarker in breast cancer
Clin. Cancer Res.
13
4092-4097
2007
Homo sapiens
Manually annotated by BRENDA team
Chen, L.C.; Hsueh, C.; Tsang, N.M.; Liang, Y.; Chang, K.P.; Hao, S.P.; Yu, J.S.; Chang, Y.S.
Heterogeneous ribonucleoprotein K and thymidine phosphorylase are independent prognostic and therapeutic markers for nasopharyngeal carcinoma
Clin. Cancer Res.
14
3807-3813
2008
Homo sapiens
Manually annotated by BRENDA team
Reigan, P.; Gbaj, A.; Stratford, I.J.; Bryce, R.A.; Freeman, S.
Xanthine oxidase-activated prodrugs of thymidine phosphorylase inhibitors
Eur. J. Med. Chem.
43
1248-1260
2008
Escherichia coli, Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Stoebner, P.E.; Le Gallic, L.; Berthe, M.L.; Boulle, N.; Lallemant, B.; Marque, M.; Gaspard, C.; Delfour, C.; Lavabre-Bertrand, T.; Martinez, J.; Meunier, L.
Decreased expression of thymidine phosphorylase/platelet-derived endothelial cell growth factor in basal cell carcinomas
Exp. Dermatol.
17
908-915
2008
Homo sapiens
Manually annotated by BRENDA team
Jinfeng, M.; Kimura, W.; Sakurai, F.; Moriya, T.; Mizutani, M.; Hirai, I.
Prognostic role of angiogenesis and its correlations with thymidine phosphorylase and p53 expression in ductal adenocarcinoma of the pancreas
Hepatogastroenterology
54
1635-1640
2007
Homo sapiens
Manually annotated by BRENDA team
Hayashi, T.; Kawahara, H.; Kobayashi, S.; Kashiwagi, H.; Hirai, K.; Yanaga, K.
Importance of thymidine phosphorylase, dihydropyrimidine dehydrogenase and thymidylate synthase expression at the invasive front of T3 rectal cancer as prognostic factors
Hepatogastroenterology
55
403-406
2008
Homo sapiens
Manually annotated by BRENDA team
Haraguchi, M.; Komuta, K.; Ueda, T.; Akashi, A.; Minami, S.; Furui, J.; Kanematsu, T.
Prognostic significance of the serum thymidine phosphorylase levels in venous blood drainage specimens in patients with colorectal cancer
Hepatogastroenterology
55
418-421
2008
Homo sapiens
Manually annotated by BRENDA team
Kobayashi, Y.; Wada, Y.; Ohara, T.; Okuda, Y.; Suzuki, N.; Hasegawa, K.; Kiguchi, K.; Ishizuka, B.
Enzymatic activities of uridine and thymidine phosphorylase in normal and cancerous uterine cervical tissues
Hum. Cell
20
107-110
2007
Homo sapiens
Manually annotated by BRENDA team
Miyake, K.; Imura, S.; Yoshizumi, T.; Ikemoto, T.; Morine, Y.; Shimada, M.
Role of thymidine phosphorylase and orotate phosphoribosyltransferase mRNA expression and its ratio to dihydropyrimidine dehydrogenase in the prognosis and clinicopathological features of patients with pancreatic cancer
Int. J. Clin. Oncol.
12
111-119
2007
Homo sapiens
Manually annotated by BRENDA team
Ranieri, G.; Grammatica, L.; Patruno, R.; Zito, A.F.; Valerio, P.; Iacobellis, S.; Gadaleta, C.; Gasparini, G.; Ribatti, D.
A possible role of thymidine phosphorylase expression and 5-fluorouracil increased sensitivity in oropharyngeal cancer patients
J. Cell. Mol. Med.
11
362-368
2007
Homo sapiens
Manually annotated by BRENDA team
Jang, J.S.; Lee, W.S.; Lee, J.S.; Kim, H.W.; Ko, G.H.; Ha, W.S.
The expression of thymidine phosphorylase in cancer-infiltrating inflammatory cells in stomach cancer
J. Korean Med. Sci.
22
S109-S114
2007
Homo sapiens
Manually annotated by BRENDA team
Nencka, R.; Votruba, I.; Hrebabecky, H.; Jansa, P.; Tloustova, E.; Horska, K.; Masojidkova, M.; Holy, A.
Discovery of 5-substituted-6-chlorouracils as efficient inhibitors of human thymidine phosphorylase
J. Med. Chem.
50
6016-6023
2007
Homo sapiens
Manually annotated by BRENDA team
Honda, J.; Sasa, M.; Moriya, T.; Bando, Y.; Hirose, T.; Takahashi, M.; Nagao, T.; Tangoku, A.
Thymidine phosphorylase and dihydropyrimidine dehydrogenase are predictive factors of therapeutic efficacy of capecitabine monotherapy for breast cancer-preliminary results
J. Med. Invest.
55
54-60
2008
Homo sapiens
Manually annotated by BRENDA team
Gunningham, S.P.; Currie, M.J.; Morrin, H.R.; Tan, E.Y.; Turley, H.; Dachs, G.U.; Watson, A.I.; Frampton, C.; Robinson, B.A.; Fox, S.B.
The angiogenic factor thymidine phosphorylase up-regulates the cell adhesion molecule P-selectin in human vascular endothelial cells and is associated with P-selectin expression in breast cancers
J. Pathol.
212
335-344
2007
Homo sapiens
Manually annotated by BRENDA team
Kocakova, I.; Svoboda, M.; Kubosova, K.; Chrenko, V.; Roubalova, E.; Krejci, E.; Sefr, R.; Slampa, P.; Frgala, T.; Zaloudik, J.
Preoperative radiotherapy and concomitant capecitabine treatment induce thymidylate synthase and thymidine phosphorylase mRNAs in rectal carcinoma
Neoplasma
54
447-453
2007
Homo sapiens
Manually annotated by BRENDA team
Mazurek, A.; Kuc, P.; Mazurek-Wadolkowska, E.; Laudanski, T.
A role of thymidine phosphorylase and P53 tissue protein expression in biology of endometrial cancer
Neoplasma
55
261-265
2008
Homo sapiens
Manually annotated by BRENDA team
Grierson, J.R.; Brockenbrough, J.S.; Rasey, J.S.; Wiens, L.W.; Schwartz, J.L.; Jordan, R.; Vesselle, H.
Evaluation of 5-deoxy-5-[F-18]fluorothymidine as a tracer of intracellular thymidine phosphorylase activity
Nucl. Med. Biol.
34
471-478
2007
Homo sapiens
Manually annotated by BRENDA team
Pomeisl, K.; Holy, A.; Votruba, I.
Pyrimidine acyclic nucleoside phosphonates and phosphorylated analogs. Part 2. Syntheses and investigation of their inhibitory effects towards human thymidine phosphorylase
Nucleic Acids Symp. Ser.
52
657-658
2008
Homo sapiens
Manually annotated by BRENDA team
Panova, N.; Kosiova, I.; Petrova, M.; Vanek, V.; Liboska, R.; Kovackova, S.; Kocalka, P.; Kralikova, S.; Tocik, Z.; Pav, O.; Paces, O.; Rejman, D.; Rosenberg, I.
Nucleoside phosphonic acids in thymidine phosphorylase inhibition: structure-activity relationship
Nucleic Acids Symp. Ser.
52
665-666
2008
Homo sapiens
Manually annotated by BRENDA team
Pomeisl, K.; Votruba, I.; Holy, A.; Pohl, R.
Syntheses of pyrimidine acyclic nucleoside phosphonates as potent inhibitors of thymidine phosphorylase (PD-ECGF) from SD-lymphoma
Nucleosides Nucleotides Nucleic Acids
26
1025-1028
2007
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Bijnsdorp, I.V.; de Bruin, M.; Laan, A.C.; Fukushima, M.; Peters, G.J.
The role of platelet-derived endothelial cell growth factor/thymidine phosphorylase in tumor behavior
Nucleosides Nucleotides Nucleic Acids
27
681-691
2008
Homo sapiens
Manually annotated by BRENDA team
Han, H.S.; Hwang, T.S.
Angiogenesis in gastric cancer: importance of the thymidine phosphorylase expression of cancer cells as an angiogenic factor
Oncol. Rep.
17
61-65
2007
Homo sapiens
Manually annotated by BRENDA team
Tanikawa, T.; Waguri-Nagaya, Y.; Kusabe, T.; Aoyama, M.; Asai, K.; Otsuka, T.
Gliostatin/thymidine phosphorylase-regulated vascular endothelial growth-factor production in human fibroblast-like synoviocytes
Rheumatol. Int.
27
553-559
2007
Homo sapiens
Manually annotated by BRENDA team
Saif, M.W.; Juneja, V.; Black, G.; Thronton, J.; Johnson, M.R.; Diasio, R.B.
Palmar-plantar erythrodysesthesia in patients receiving capecitabine and intratumor thymidine phosphorylase and dihydropyrimidine dehydrogenase: is there a pharmacologic explanation?
Support. Cancer Ther.
4
211-218
2007
Homo sapiens
Manually annotated by BRENDA team
Hua, D.; Huang, Z.H.; Mao, Y.; Deng, J.Z.
Thymidylate synthase and thymidine phosphorylase gene expression as predictive parameters for the efficacy of 5-fluorouracil-based adjuvant chemotherapy for gastric cancer
World J. Gastroenterol.
13
5030-5034
2007
Homo sapiens
Manually annotated by BRENDA team
Fujimoto, K.; Matsumura, Y.; Tani, Y.; Ozono, S.; Hirao, Y.; Okajima, E.
Tissue levels of pyrimidine nucleoside phosphorylase activity in human and rodent bladder cancer and normal bladder tissue
Int. J. Urol.
14
754-759
2007
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Nakajima, Y.; Madhyastha, R.; Maruyama, M.
2-Deoxy-D-ribose, a downstream mediator of thymidine phosphorylase, regulates tumor angiogenesis and progression
Anticancer Agents Med. Chem.
9
239-245
2009
Homo sapiens
Manually annotated by BRENDA team
Loo, W.T.; Chow, L.W.; Suzuki, T.; Ono, K.; Ishida, T.; Hirakawa, H.; Ohuchi, N.; Sasano, H.
Expression of thymidine phosphorylase and dihydropyrimidine dehydrogenase in human breast carcinoma cells and tissues
Anticancer Res.
29
2525-2530
2009
Homo sapiens
Manually annotated by BRENDA team
Mitsiki, E.; Papageorgiou, A.C.; Iyer, S.; Thiyagarajan, N.; Prior, S.H.; Sleep, D.; Finnis, C.; Acharya, K.R.
Structures of native human thymidine phosphorylase and in complex with 5-iodouracil
Biochem. Biophys. Res. Commun.
386
666-670
2009
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Bronckaers, A.; Aguado, L.; Negri, A.; Camarasa, M.J.; Balzarini, J.; Perez-Perez, M.J.; Gago, F.; Liekens, S.
Identification of aspartic acid-203 in human thymidine phosphorylase as an important residue for both catalysis and non-competitive inhibition by the small molecule crystallization chaperone 5'-O-tritylinosine (KIN59)
Biochem. Pharmacol.
78
231-240
2009
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Jain, H.V.; Rasheed, R.; Kalman, T.I.
The role of phosphate in the action of thymidine phosphorylase inhibitors: implications for the catalytic mechanism
Bioorg. Med. Chem. Lett.
20
1648-1651
2010
Escherichia coli, Homo sapiens (P19971)
Manually annotated by BRENDA team
Pula, G.; Mayr, U.; Evans, C.; Prokopi, M.; Vara, D.S.; Yin, X.; Astroulakis, Z.; Xiao, Q.; Hill, J.; Xu, Q.; Mayr, M.
Proteomics identifies thymidine phosphorylase as a key regulator of the angiogenic potential of colony-forming units and endothelial progenitor cell cultures
Circ. Res.
104
32-40
2009
Homo sapiens
Manually annotated by BRENDA team
Birck, M.; Clinch, K.; Gainsford, G.; Schramm, V.; Tyler, P.
Syntheses of 5-chlorouracils/thymines with 1-[phosphono(methyl/difluoromethyl)]-1,2-unsaturated-moiety-substituted methyl groups at N(1) and human thymidine phosphorylase inhibitory activity
Helv. Chim. Acta
92
823-838
2009
Homo sapiens
-
Manually annotated by BRENDA team
Miszczak-Zaborska, E.; Kubiak, R.; Bienkiewicz, A.; Bartkowiak, J.
The cytosol activity of thymidine phosphorylase in endometrial cancer
J. Exp. Clin. Cancer Res.
27
64
2008
Homo sapiens
Manually annotated by BRENDA team
Brockenbrough, J.S.; Morihara, J.K.; Hawes, S.E.; Stern, J.E.; Rasey, J.S.; Wiens, L.W.; Feng, Q.; Vesselle, H.
Thymidine kinase 1 and thymidine phosphorylase expression in non-small-cell lung carcinoma in relation to angiogenesis and proliferation
J. Histochem. Cytochem.
57
1087-1097
2009
Homo sapiens
Manually annotated by BRENDA team
Bakker, J.A.; Schlesser, P.; Smeets, H.J.; Francois, B.; Bierau, J.
Biochemical abnormalities in a patient with thymidine phosphorylase deficiency with fatal outcome
J. Inherit. Metab. Dis.
33
S139-143
2010
Homo sapiens
Manually annotated by BRENDA team
Bronckaers, A.; Gago, F.; Balzarini, J.; Liekens, S.
The dual role of thymidine phosphorylase in cancer development and chemotherapy
Med. Res. Rev.
29
903-953
2009
Geobacillus stearothermophilus, Escherichia coli, Homo sapiens, Mus musculus, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Chen, L.C.; Liu, H.P.; Li, H.P.; Hsueh, C.; Yu, J.S.; Liang, C.L.; Chang, Y.S.
Thymidine phosphorylase mRNA stability and protein levels are increased through ERK-mediated cytoplasmic accumulation of hnRNP K in nasopharyngeal carcinoma cells
Oncogene
28
1904-1915
2009
Homo sapiens
Manually annotated by BRENDA team
Yue, H.; Tanaka, K.; Furukawa, T.; Karnik, S.S.; Li, W.
Thymidine phosphorylase inhibits vascular smooth muscle cell proliferation via upregulation of STAT3
Biochim. Biophys. Acta
1823
1316-1323
2012
Homo sapiens
Manually annotated by BRENDA team
Marak, D.; Otmar, M.; Votruba, I.; Dracinsky, M.; Krecmerova, M.
8-Aza-7,9-dideazaxanthine acyclic nucleoside phosphonate inhibitors of thymidine phosphorylase
Bioorg. Med. Chem. Lett.
21
652-654
2011
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Marti, R.; Lopez, L.C.; Hirano, M.
Assessment of thymidine phosphorylase function: measurement of plasma thymidine (and deoxyuridine) and thymidine phosphorylase activity
Methods Mol. Biol.
837
121-133
2012
Homo sapiens
Manually annotated by BRENDA team
Thanasai, J.; Limpaiboon, T.; Jearanaikoon, P.; Sripa, B.; Pairojkul, C.; Tantimavanich, S.; Miwa, M.
Effects of thymidine phosphorylase on tumor aggressiveness and 5-fluorouracil sensitivity in cholangiocarcinoma
World J. Gastroenterol.
16
1631-1638
2010
Homo sapiens
Manually annotated by BRENDA team
Ko, J.C.; Chiu, H.C.; Syu, J.J.; Jian, Y.J.; Chen, C.Y.; Jian, Y.T.; Huang, Y.J.; Wo, T.Y.; Lin, Y.W.
Tamoxifen enhances erlotinib-induced cytotoxicity through down-regulating AKT-mediated thymidine phosphorylase expression in human non-small-cell lung cancer cells
Biochem. Pharmacol.
88
119-127
2014
Homo sapiens
Manually annotated by BRENDA team
Bera, H.; Dolzhenko, A.V.; Sun, L.; Dutta Gupta, S.; Chui, W.K.
Synthesis and in vitro evaluation of 1,2,4-triazolo[1,5-a][1,3,5]triazine derivatives as thymidine phosphorylase inhibitors
Chem. Biol. Drug Des.
82
351-360
2013
Homo sapiens
Manually annotated by BRENDA team
Deves, C.; Rostirolla, D.C.; Martinelli, L.K.; Bizarro, C.V.; Santos, D.S.; Basso, L.A.
The kinetic mechanism of human thymidine phosphorylase - a molecular target for cancer drug development
Mol. Biosyst.
10
592-604
2014
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Tozer, T.; Heale, K.; Manto Chagas, C.; de Barros, A.L.B.; Alisaraie, L.
Interdomain twists of human thymidine phosphorylase and its active-inactive conformations binding of 5-FU and its analogues to human thymidine phosphorylase versus dihydropyrimidine dehydrogenase
Chem. Biol. Drug Des.
94
1956-1972
2019
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Bajaj, S.; Roy, P.P.; Singh, J.
Synthesis, thymidine phosphorylase inhibitory and computational study of novel 1,3,4-oxadiazole-2-thione derivatives as potential anticancer agents
Comput. Biol. Chem.
76
151-160
2018
Homo sapiens (P19971)
Manually annotated by BRENDA team
Bera, H.; Chigurupati, S.
Recent discovery of non-nucleobase thymidine phosphorylase inhibitors targeting cancer
Eur. J. Med. Chem.
124
992-1003
2016
Escherichia coli (P0C037), Homo sapiens (P19971)
Manually annotated by BRENDA team
Zhao, S.; Li, K.; Jin, Y.; Lin, J.
Synthesis and biological evaluation of novel 1-(aryl-aldehyde-oxime)uracil derivatives as a new class of thymidine phosphorylase inhibitors
Eur. J. Med. Chem.
144
41-51
2018
Homo sapiens (P19971)
Manually annotated by BRENDA team
Tampellini, M.; Bironzo, P.; Di Maio, M.; Scagliotti, G.V.
Thymidine phosphorylase the unforeseen driver in colorectal cancer treatment?
Future Oncol.
14
1223-1231
2018
Homo sapiens (P19971)
Manually annotated by BRENDA team
Oh, T.; El Kouni, M.H.
Kinetics mechanism and regulation of native human hepatic thymidine phosphorylase
Int. J. Biochem. Cell Biol.
110
122-129
2019
Homo sapiens (P19971), Homo sapiens, Mus musculus (Q99N42)
Manually annotated by BRENDA team
de Moura Sperotto, N.D.; Deves Roth, C.; Rodrigues-Junior, V.S.; Ev Neves, C.; Reisdorfer Paula, F.; da Silva Dadda, A.; Bergo, P.; Freitas de Freitas, T.; Souza Macchi, F.; Moura, S.; Duarte de Souza, A.P.; Campos, M.M.; Valim Bizarro, C.; Santos, D.S.; Basso, L.A.; Machado, P.
Design of novel inhibitors of human thymidine phosphorylase synthesis, enzyme inhibition, in vitro toxicity, and impact on human glioblastoma cancer
J. Med. Chem.
62
1231-1245
2019
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Oh, T.; El Kouni, M.H.
Distinct substrate specificity and physicochemical characterization of native human hepatic thymidine phosphorylase
PLoS ONE
13
e0202826
2018
Homo sapiens (P19971), Homo sapiens
Manually annotated by BRENDA team
Zaman, K.; Rahim, F.; Taha, M.; Wadood, A.; Shah, S.A.A.; Ahmed, Q.U.; Zakaria, Z.A.
Synthesis of new isoquinoline-base-oxadiazole derivatives as potent inhibitors of thymidine phosphorylase and molecular docking study
Sci. Rep.
9
16015
2019
Homo sapiens (P19971)
Manually annotated by BRENDA team