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ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine 5'-phosphate
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
ADP + 3'-ethynylcytidine 5'-monophosphate
-
-
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine 5'-phosphate
ATP + 2-thiocytidine
ADP + 2-thiocytidine 5'-monophosphate
ATP + 3'-C-ethynylcytidine
ADP + 3'-C-ethynylcytidine 5'-phosphate
ATP + 3'-C-ethynylcytidine 5'-diphosphate
ADP + 3'-C-ethynylcytidine 5'-triphosphate
ATP + 3'-C-ethynylcytidine 5'-phosphate
ADP + 3'-C-ethynylcytidine 5'-diphosphate
ATP + 3'-C-ethynyluridine
ADP + 3'-C-ethynyluridine 5'-phosphate
ATP + 3'-C-ethynyluridine 5'-diphosphate
ADP + 3'-C-ethynyluridine 5'-triphosphate
ATP + 3'-C-ethynyluridine 5'-phosphate
ADP + 3'-C-ethynyluridine 5'-diphosphate
ATP + 3'-deoxy-3'-ethynylcytidine
ADP + 3'-deoxy-3'-ethynylcytidine 5'-monophosphate
-
recombinant uridine kinase, 20% of activity with uridine
-
?
ATP + 3'-deoxy-3'-ethynyluridine
ADP + 3'-deoxy-3'-ethynyluridine 5'-monophosphate
-
recombinant uridine kinase, 20% of activity with uridine
-
?
ATP + 3'-ethynylcytidine
ADP + 3'-ethynylcytidine 5'-monophosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
-
-
?
ATP + 3'-ethynylcytidine 5'-diphosphate
ADP + 3'-ethynylcytidine 5'-triphosphate
-
-
-
?
ATP + 3'-ethynylcytidine 5'-monophosphate
ADP + 3'-ethynylcytidine 5'-diphosphate
-
-
-
?
ATP + 3'-ethynyluridine
ADP + 3'-ethynyluridine 5'-monophosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
-
-
?
ATP + 3'-ethynyluridine 5'-diphosphate
ADP + 3'-ethynyluridine 5'-triphosphate
-
-
-
?
ATP + 3'-ethynyluridine 5'-monophosphate
ADP + 3'-ethynyluridine 5'-diphosphate
-
-
-
?
ATP + 3,4,5,6-tetrahydrouridine
ADP + 3,4,5,6-tetrahydrouridine 5'-monophosphate
ATP + 3-deazauridine
ADP + 3-deazauridine 5'-monophosphate
ATP + 3-deazauridine
ADP + ?
-
-
-
?
ATP + 3-methyluridine
ADP + 3-methyluridine 5'-monophosphate
recombinant uridine kinase 2, 18% of activity with uridine
-
?
ATP + 4-amino-1-[(1S,4R,5S)-2-fluoro-4,5-dihydroxy-3-(hydroxymethyl)cyclopent-2-en-1-yl]pyrimidin-2(1H)-one
ADP + [(3S,4S,5R)-3-(4-amino-2-oxopyrimidin-1(2H)-yl)-2-fluoro-4,5-dihydroxycyclopent-1-en-1-yl]methyl phosphate
-
-
-
ir
ATP + 4-thiouridine
ADP + 4-thiouridine 5'-monophosphate
ATP + 5-azacytidine
ADP + 5-azacytidine 5'-monophosphate
ATP + 5-azacytidine
ADP + ?
-
-
-
?
ATP + 5-bromouridine
ADP + 5-bromouridine 5'-monophosphate
ATP + 5-fluorocytidine
ADP + 5-fluorocytidine 5'-monophosphate
ATP + 5-fluorocytidine
ADP + ?
-
-
-
?
ATP + 5-fluorouridine
ADP + 5-fluoro-UMP
-
-
-
?
ATP + 5-fluorouridine
ADP + 5-fluoro-uridine monophosphate
-
-
-
?
ATP + 5-fluorouridine
ADP + 5-fluorouridine 5'-monophosphate
ATP + 5-fluorouridine
ADP + ?
-
-
-
?
ATP + 5-hydroxyuridine
ADP + 5-hydroxyuridine 5'-monophosphate
ATP + 5-methoxyuridine
ADP + 5-methoxyuridine 5'-monophosphate
ATP + 5-methylcytidine
ADP + 5-methylcytidine 5'-monophosphate
ATP + 6-azacytidine
ADP + 6-azacytidine 5'-monophosphate
ATP + 6-azauridine
ADP + 6-azauridine 5'-monophosphate
ATP + 6-azauridine
ADP + ?
-
-
-
?
ATP + cyclopentenyl cytosine
ADP + ?
-
-
-
?
ATP + cyclopentenyl uracil
ADP + ?
-
-
-
?
ATP + cyclopentenyl-cytosine
ADP + cyclopentenylcytosine 5'-monophosphate
-
-
-
?
ATP + cyclopentenylcytosine
ADP + cyclopentenylcytosine 5'-monophosphate
-
recombinant uridine kinase, 12% of activity with uridine
-
?
ATP + fluorocyclopentenylcytosine
?
an orally available cytidine analogue, RX-3117
-
-
?
ATP + N4-acetylcytidine
ADP + N4-acetylcytidine 5'-monophosphate
ATP + N4-aminocytidine
ADP + N4-aminocytidine 5'-monophosphate
recombinant uridine kinase 1, 20% of activity with uridine
-
?
ATP + N4-anisoylcytidine
ADP + N4-anisoylcytidine 5'-monophosphate
ATP + N4-benzoylcytidine
ADP + N4-benzoylcytidine 5'-monophosphate
ATP + ribavirin
ADP + ribavirin monophosphate
-
13% of substrate phosphorylated, within 2 h incubation
-
-
?
dATP + cytidine
dADP + CMP
-
recombinant uridine kinase
-
?
dATP + uridine
dADP + UMP
dCTP + cytidine
dCDP + CMP
-
recombinant uridine kinase
-
?
dCTP + uridine
dCDP + UMP
dGTP + uridine
dGDP + UMP
dTTP + uridine
dTDP + UMP
dUTP + cytidine
dUDP + CMP
-
recombinant uridine kinase
-
?
dUTP + uridine
dUDP + UMP
GTP + 5-fluorocytidine
GDP + 5-fluorocytidine 5'-monophosphate
-
40% of activity with uridine
-
?
GTP + 5-fluorouridine
GDP + 5-fluorouridine 5'-monophosphate
-
60% of activity with uridine
-
?
GTP + 6-azauridine
GDP 6-azauridine 5'-monophosphate
-
31% of activity with uridine
-
?
GTP + cytidine
CMP + GDP
-
-
-
?
GTP + N-acetylcytidine
GDP + N-acetylcytidine 5'-monophosphate
-
57% of activity with uridine
-
?
additional information
?
-
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine 5'-phosphate
-
-
-
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine 5'-phosphate
-
UCK2 enzyme activity required to produce the antitumoral active metabolite
-
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine 5'-phosphate
-
-
-
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine 5'-phosphate
-
UCK2 enzyme activity required to produce the antitumoral active metabolite
-
-
?
ATP + 2-thiocytidine
ADP + 2-thiocytidine 5'-monophosphate
recombinant uridine kinase 2, 86% of activity with uridine
-
?
ATP + 2-thiocytidine
ADP + 2-thiocytidine 5'-monophosphate
recombinant uridine kinase 1, 20% of activity with uridine
-
?
ATP + 3'-C-ethynylcytidine
ADP + 3'-C-ethynylcytidine 5'-phosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
-
-
ir
ATP + 3'-C-ethynylcytidine
ADP + 3'-C-ethynylcytidine 5'-phosphate
-
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
-
-
ir
ATP + 3'-C-ethynylcytidine 5'-diphosphate
ADP + 3'-C-ethynylcytidine 5'-triphosphate
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-diphosphate
ADP + 3'-C-ethynylcytidine 5'-triphosphate
-
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-phosphate
ADP + 3'-C-ethynylcytidine 5'-diphosphate
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-phosphate
ADP + 3'-C-ethynylcytidine 5'-diphosphate
-
-
-
-
?
ATP + 3'-C-ethynyluridine
ADP + 3'-C-ethynyluridine 5'-phosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
-
-
?
ATP + 3'-C-ethynyluridine
ADP + 3'-C-ethynyluridine 5'-phosphate
-
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
-
-
?
ATP + 3'-C-ethynyluridine 5'-diphosphate
ADP + 3'-C-ethynyluridine 5'-triphosphate
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-diphosphate
ADP + 3'-C-ethynyluridine 5'-triphosphate
-
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-phosphate
ADP + 3'-C-ethynyluridine 5'-diphosphate
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-phosphate
ADP + 3'-C-ethynyluridine 5'-diphosphate
-
-
-
-
?
ATP + 3,4,5,6-tetrahydrouridine
ADP + 3,4,5,6-tetrahydrouridine 5'-monophosphate
recombinant uridine kinase 1, 13% of activity with uridine
-
?
ATP + 3,4,5,6-tetrahydrouridine
ADP + 3,4,5,6-tetrahydrouridine 5'-monophosphate
recombinant uridine kinase 2, 81% of activity with uridine
-
?
ATP + 3-deazauridine
ADP + 3-deazauridine 5'-monophosphate
recombinant uridine kinase 2, 49% of activity with uridine
-
?
ATP + 3-deazauridine
ADP + 3-deazauridine 5'-monophosphate
-
-
-
?
ATP + 4-thiouridine
ADP + 4-thiouridine 5'-monophosphate
recombinant uridine kinase 1, 122% of activity with uridine
-
?
ATP + 4-thiouridine
ADP + 4-thiouridine 5'-monophosphate
recombinant uridine kinase 2, 125% of activity with uridine
-
?
ATP + 5-azacytidine
ADP + 5-azacytidine 5'-monophosphate
-
-
-
?
ATP + 5-azacytidine
ADP + 5-azacytidine 5'-monophosphate
-
-
-
?
ATP + 5-azacytidine
ADP + 5-azacytidine 5'-monophosphate
-
39.1% of the activity with uridine
-
?
ATP + 5-bromouridine
ADP + 5-bromouridine 5'-monophosphate
recombinant uridine kinase 1, 50% of activity with uridine
-
?
ATP + 5-bromouridine
ADP + 5-bromouridine 5'-monophosphate
recombinant uridine kinase 2,6% of activity with uridine
-
?
ATP + 5-fluorocytidine
ADP + 5-fluorocytidine 5'-monophosphate
recombinant uridine kinase 1, 37% of activity with uridine
-
?
ATP + 5-fluorocytidine
ADP + 5-fluorocytidine 5'-monophosphate
recombinant uridine kinase 2, 184% of activity with uridine
-
?
ATP + 5-fluorocytidine
ADP + 5-fluorocytidine 5'-monophosphate
-
-
-
?
ATP + 5-fluorouridine
ADP + 5-fluorouridine 5'-monophosphate
-
-
-
?
ATP + 5-fluorouridine
ADP + 5-fluorouridine 5'-monophosphate
-
recombinant uridine kinase
-
?
ATP + 5-fluorouridine
ADP + 5-fluorouridine 5'-monophosphate
recombinant uridine kinase 2, 89% of activity with uridine
-
?
ATP + 5-fluorouridine
ADP + 5-fluorouridine 5'-monophosphate
-
-
-
?
ATP + 5-fluorouridine
ADP + 5-fluorouridine 5'-monophosphate
-
-
-
?
ATP + 5-fluorouridine
ADP + 5-fluorouridine 5'-monophosphate
-
-
-
?
ATP + 5-fluorouridine
ADP + 5-fluorouridine 5'-monophosphate
-
-
-
?
ATP + 5-fluorouridine
ADP + 5-fluorouridine 5'-monophosphate
-
66.9% of the activity with uridine
-
?
ATP + 5-hydroxyuridine
ADP + 5-hydroxyuridine 5'-monophosphate
recombinant uridine kinase 1, 14% of activity with uridine
-
?
ATP + 5-hydroxyuridine
ADP + 5-hydroxyuridine 5'-monophosphate
recombinant uridine kinase 2, 12% of activity with uridine
-
?
ATP + 5-methoxyuridine
ADP + 5-methoxyuridine 5'-monophosphate
recombinant uridine kinase 1, 122% of activity with uridine
-
?
ATP + 5-methoxyuridine
ADP + 5-methoxyuridine 5'-monophosphate
recombinant uridine kinase 2, 92% of activity with uridine
-
?
ATP + 5-methylcytidine
ADP + 5-methylcytidine 5'-monophosphate
recombinant uridine kinase 1, 9% of activity with uridine
-
?
ATP + 5-methylcytidine
ADP + 5-methylcytidine 5'-monophosphate
recombinant uridine kinase 2, 30% of activity with uridine
-
?
ATP + 6-azacytidine
ADP + 6-azacytidine 5'-monophosphate
recombinant uridine kinase 2, 75% of activity with uridine
-
?
ATP + 6-azacytidine
ADP + 6-azacytidine 5'-monophosphate
-
-
-
?
ATP + 6-azacytidine
ADP + 6-azacytidine 5'-monophosphate
-
60.4% of the activity with uridine
-
?
ATP + 6-azauridine
ADP + 6-azauridine 5'-monophosphate
-
-
-
?
ATP + 6-azauridine
ADP + 6-azauridine 5'-monophosphate
recombinant uridine kinase 1, 38% of activity with uridine, recombinant uridine kinase 2, 148% of activity with uridine
-
?
ATP + 6-azauridine
ADP + 6-azauridine 5'-monophosphate
-
-
-
?
ATP + 6-azauridine
ADP + 6-azauridine 5'-monophosphate
-
-
-
?
ATP + 6-azauridine
ADP + 6-azauridine 5'-monophosphate
-
-
-
?
ATP + 6-azauridine
ADP + 6-azauridine 5'-monophosphate
-
65.5% of the activity with uridine
-
?
ATP + CMP
ADP + CDP
-
-
-
-
?
ATP + CMP
ADP + CDP
-
low activity with ATP as phosphate donor
-
-
?
ATP + CMP
ADP + CDP
-
-
-
-
?
ATP + CMP
ADP + CDP
-
low activity with ATP as phosphate donor
-
-
?
ATP + CMP
ADP + CDP
-
-
-
-
?
ATP + CMP
ADP + CDP
-
low activity with ATP as phosphate donor
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + cytidine
ADP + CMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + cytidine
ADP + CMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway, essential for cell proliferation, UCK 2 involved in tumor formation
-
-
?
ATP + cytidine
ADP + CMP
-
89% of substrate phosphorylated, within 2 h incubation
-
-
?
ATP + cytidine
ADP + CMP
the enzyme is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
50% of activity with uridine
-
?
ATP + cytidine
ADP + CMP
-
50% of activity with uridine
-
?
ATP + cytidine
ADP + CMP
-
35.6% of the activity with uridine
-
?
ATP + cytidine
ADP + CMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + N4-acetylcytidine
ADP + N4-acetylcytidine 5'-monophosphate
recombinant uridine kinase 1, 142% of activity with uridine
-
?
ATP + N4-acetylcytidine
ADP + N4-acetylcytidine 5'-monophosphate
recombinant uridine kinase 2, 84% of activity with uridine
-
?
ATP + N4-anisoylcytidine
ADP + N4-anisoylcytidine 5'-monophosphate
recombinant uridine kinase 2, 12% of activity with uridine
-
?
ATP + N4-anisoylcytidine
ADP + N4-anisoylcytidine 5'-monophosphate
recombinant uridine kinase 1, 20% of activity with uridine
-
?
ATP + N4-benzoylcytidine
ADP + N4-benzoylcytidine 5'-monophosphate
recombinant uridine kinase 1, 68% of activity with uridine
-
?
ATP + N4-benzoylcytidine
ADP + N4-benzoylcytidine 5'-monophosphate
recombinant uridine kinase 2, 51% of activity with uridine
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
low activity with ATP as phosphate donor
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
low activity with ATP as phosphate donor
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
low activity with ATP as phosphate donor
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
dGTP and GTP are the most efficient phosphate donors, activity with ATP and dATP is 10% and with dUTP, dCTP and dTTP 5% of that with GTP or dGTP
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
very low activity with CTP and UTP
-
?
ATP + uridine
ADP + UMP
-
first enzyme of pyrimidine salvage pathway
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
no activity with adenosine, guanosine and deoxyribonucleotides, no activity with CTP and UTP
-
?
ATP + uridine
ADP + UMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + uridine
ADP + UMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + uridine
ADP + UMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway, essential for cell proliferation, UCK 2 involved in tumor formation
-
-
?
ATP + uridine
ADP + UMP
-
56% of substrate phosphorylated, within 2 h incubation
-
-
?
ATP + uridine
ADP + UMP
the enzyme is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
-
?
ATP + uridine
ADP + UMP
-
no activity with thymine riboside, deoxyribosides, cytosine arabinoside, adenosine, purine deoxyribosides, UMP, CMP and deoxyribosides
-
?
ATP + uridine
ADP + UMP
-
no activity with thymine riboside, deoxyribosides, cytosine arabinoside, adenosine, purine deoxyribosides, UMP, CMP and deoxyribosides
-
?
ATP + uridine
ADP + UMP
-
no activity with CTP and UTP
-
?
ATP + uridine
ADP + UMP
-
ATP most effective as phosphate donor
-
?
ATP + uridine
ADP + UMP
-
enzyme is part of the anabolic pathway by which the preformed pyrimidine nucleosides are salvaged for nucleic acid biosynthesis
-
?
ATP + uridine
ADP + UMP
-
rate limiting enzyme of pyrimidine salvage pathway
-
?
ATP + uridine
ADP + UMP
-
rate-limiting enzyme in anabolism of uridine and cytidine
-
?
ATP + uridine
ADP + UMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
-
?
ATP + uridine
ADP + UMP
-
very low activity with CTP and UTP
-
?
ATP + uridine
ADP + UMP
-
first enzyme of pyrimidine salvage pathway
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
substrate of mutant ttCKs Y93H and Y93Q, not of wild-type ttCK Y93
-
-
?
ATP + uridine
ADP + UMP
reaction of ttCK enzyme mutants Y93H and Y93Q only, no activity with the wild-type enzyme
-
-
?
ATP + uridine
ADP + UMP
Y93 mutants
-
-
?
ATP + uridine
ADP + UMP
reaction of ttCK enzyme mutants Y93H and Y93Q only, no activity with the wild-type enzyme
-
-
?
ATP + uridine
ADP + UMP
Y93 mutants
-
-
?
ATP + uridine
ADP + UMP
reaction of ttCK enzyme mutants Y93H and Y93Q only, no activity with the wild-type enzyme
-
-
?
ATP + uridine
ADP + UMP
Y93 mutants
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
substrate of mutant ttCKs Y93H and Y93Q, not of wild-type ttCK Y93
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
CTP + CMP
CDP + CDP
-
low activity with CTP as phosphate donor
-
-
?
CTP + CMP
CDP + CDP
-
low activity with CTP as phosphate donor
-
-
?
CTP + UMP
CDP + UDP
-
low activity with CTP as phosphate donor
-
-
?
CTP + UMP
CDP + UDP
-
low activity with CTP as phosphate donor
-
-
?
cytidine + ATP
CMP + ADP
-
-
-
?
cytidine + ATP
CMP + ADP
-
-
-
?
dATP + uridine
dADP + UMP
-
-
-
?
dATP + uridine
dADP + UMP
-
recombinant uridine kinase
-
?
dATP + uridine
dADP + UMP
-
-
-
?
dATP + uridine
dADP + UMP
-
88% of activity with ATP
-
?
dATP + uridine
dADP + UMP
-
20.5% of activity with ATP
-
?
dATP + uridine
dADP + UMP
-
-
-
?
dATP + uridine
dADP + UMP
-
-
-
?
dCTP + uridine
dCDP + UMP
-
weak activity
-
?
dCTP + uridine
dCDP + UMP
-
50% of activity with ATP
-
?
dCTP + uridine
dCDP + UMP
-
49.7% of activity with ATP
-
?
dCTP + uridine
dCDP + UMP
-
weak activity
-
?
dGTP + uridine
dGDP + UMP
-
-
-
?
dGTP + uridine
dGDP + UMP
-
-
-
?
dGTP + uridine
dGDP + UMP
-
23.5% of activity with ATP
-
?
dGTP + uridine
dGDP + UMP
-
21% of activity with ATP
-
?
dGTP + uridine
dGDP + UMP
-
-
-
?
dGTP + uridine
dGDP + UMP
-
-
-
?
dTTP + uridine
dTDP + UMP
-
weak activity
-
?
dTTP + uridine
dTDP + UMP
-
weak activity
-
?
dUTP + uridine
dUDP + UMP
-
-
-
?
dUTP + uridine
dUDP + UMP
-
recombinant uridine kinase
-
?
dUTP + uridine
dUDP + UMP
-
-
-
?
dUTP + uridine
dUDP + UMP
-
67% of activity with ATP
-
?
dUTP + uridine
dUDP + UMP
-
66.7% of activity with ATP
-
?
dUTP + uridine
dUDP + UMP
-
-
-
?
dUTP + uridine
dUDP + UMP
-
-
-
?
GTP + CMP
GDP + CDP
-
GTP is the best phosphate donor
-
-
?
GTP + CMP
GDP + CDP
-
GTP is the best phosphate donor
-
-
?
GTP + cytidine
GDP + CMP
-
-
-
-
?
GTP + cytidine
GDP + CMP
-
-
-
-
?
GTP + UMP
CDP + UDP
-
GTP is the best phosphate donor
-
-
?
GTP + UMP
CDP + UDP
-
GTP is the best phosphate donor
-
-
?
GTP + uridine
GDP + UMP
-
GTP is the best phosphate donor
-
-
?
GTP + uridine
GDP + UMP
-
GTP is the best phosphate donor
-
-
?
GTP + uridine
UMP + GDP
-
-
-
?
GTP + uridine
UMP + GDP
-
weak activity
-
?
GTP + uridine
UMP + GDP
-
-
?
GTP + uridine
UMP + GDP
-
-
-
?
GTP + uridine
UMP + GDP
-
-
-
?
GTP + uridine
UMP + GDP
-
23% of the activity with ATP
-
?
GTP + uridine
UMP + GDP
-
weak activity
-
?
ITP + uridine
IDP + UMP
-
weak activity
-
?
ITP + uridine
IDP + UMP
-
-
-
?
ITP + uridine
IDP + UMP
-
weak activity
-
?
uridine + ATP
UMP + ADP
with GTP: 25% activity, with UTP or CTP: 0% activity
-
-
?
uridine + ATP
UMP + ADP
-
-
-
?
UTP + CMP
UDP + CDP
-
low activity with UTP as phosphate donor
-
-
?
UTP + CMP
UDP + CDP
-
low activity with UTP as phosphate donor
-
-
?
UTP + UMP
UDP + UDP
-
low activity with UTP as phosphate donor
-
-
?
UTP + UMP
UDP + UDP
-
low activity with UTP as phosphate donor
-
-
?
additional information
?
-
-
it is ineffective to use ATP, UTP or CTP as the phosphate donor
-
-
?
additional information
?
-
uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine, cytidine, and several pyrimidine ribonucleoside analogues
-
-
-
additional information
?
-
uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine, cytidine, and several pyrimidine ribonucleoside analogues
-
-
-
additional information
?
-
-
uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine, cytidine, and several pyrimidine ribonucleoside analogues
-
-
-
additional information
?
-
-
it is ineffective to use ATP, UTP or CTP as the phosphate donor
-
-
?
additional information
?
-
-
it is ineffective to use ATP, UTP or CTP as the phosphate donor
-
-
?
additional information
?
-
-
uridine kinase and uridine phosphorylase are involved in the homeostatic regulation of purine and pyrimidine metabolism in brain. At relatively low UTP and CTP level, uptaken uridine is mainly anabolized to uridine nucleotides. At relatively high UTP and CTP levels, the inhibition of uridine kinase channels uridine towards phosphorolysis, resulting in 5-phosphoribosyl-1-bisphosphate used for purine salvage synthesis
-
-
?
additional information
?
-
molecular mechanisms of substrate specificities of uridine-cytidine kinase, overview
-
-
-
additional information
?
-
molecular mechanisms of substrate specificities of uridine-cytidine kinase, overview
-
-
-
additional information
?
-
molecular mechanisms of substrate specificities of uridine-cytidine kinase, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine 5'-phosphate
-
UCK2 enzyme activity required to produce the antitumoral active metabolite
-
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine 5'-phosphate
-
UCK2 enzyme activity required to produce the antitumoral active metabolite
-
-
?
ATP + 3'-C-ethynylcytidine
ADP + 3'-C-ethynylcytidine 5'-phosphate
ATP + 3'-C-ethynylcytidine 5'-diphosphate
ADP + 3'-C-ethynylcytidine 5'-triphosphate
ATP + 3'-C-ethynylcytidine 5'-phosphate
ADP + 3'-C-ethynylcytidine 5'-diphosphate
ATP + 3'-C-ethynyluridine
ADP + 3'-C-ethynyluridine 5'-phosphate
ATP + 3'-C-ethynyluridine 5'-diphosphate
ADP + 3'-C-ethynyluridine 5'-triphosphate
ATP + 3'-C-ethynyluridine 5'-phosphate
ADP + 3'-C-ethynyluridine 5'-diphosphate
additional information
?
-
-
uridine kinase and uridine phosphorylase are involved in the homeostatic regulation of purine and pyrimidine metabolism in brain. At relatively low UTP and CTP level, uptaken uridine is mainly anabolized to uridine nucleotides. At relatively high UTP and CTP levels, the inhibition of uridine kinase channels uridine towards phosphorolysis, resulting in 5-phosphoribosyl-1-bisphosphate used for purine salvage synthesis
-
-
?
ATP + 3'-C-ethynylcytidine
ADP + 3'-C-ethynylcytidine 5'-phosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
-
-
ir
ATP + 3'-C-ethynylcytidine
ADP + 3'-C-ethynylcytidine 5'-phosphate
-
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
-
-
ir
ATP + 3'-C-ethynylcytidine 5'-diphosphate
ADP + 3'-C-ethynylcytidine 5'-triphosphate
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-diphosphate
ADP + 3'-C-ethynylcytidine 5'-triphosphate
-
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-phosphate
ADP + 3'-C-ethynylcytidine 5'-diphosphate
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-phosphate
ADP + 3'-C-ethynylcytidine 5'-diphosphate
-
-
-
-
?
ATP + 3'-C-ethynyluridine
ADP + 3'-C-ethynyluridine 5'-phosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
-
-
?
ATP + 3'-C-ethynyluridine
ADP + 3'-C-ethynyluridine 5'-phosphate
-
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
-
-
?
ATP + 3'-C-ethynyluridine 5'-diphosphate
ADP + 3'-C-ethynyluridine 5'-triphosphate
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-diphosphate
ADP + 3'-C-ethynyluridine 5'-triphosphate
-
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-phosphate
ADP + 3'-C-ethynyluridine 5'-diphosphate
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-phosphate
ADP + 3'-C-ethynyluridine 5'-diphosphate
-
-
-
-
?
ATP + CMP
ADP + CDP
-
-
-
-
?
ATP + CMP
ADP + CDP
-
-
-
-
?
ATP + CMP
ADP + CDP
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + cytidine
ADP + CMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + cytidine
ADP + CMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway, essential for cell proliferation, UCK 2 involved in tumor formation
-
-
?
ATP + cytidine
ADP + CMP
the enzyme is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis
-
-
?
ATP + cytidine
ADP + CMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + cytidine
ADP + CMP
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + UMP
ADP + UDP
-
-
-
-
?
ATP + uridine
ADP + UMP
-
first enzyme of pyrimidine salvage pathway
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + uridine
ADP + UMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + uridine
ADP + UMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway, essential for cell proliferation, UCK 2 involved in tumor formation
-
-
?
ATP + uridine
ADP + UMP
the enzyme is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis
-
-
?
ATP + uridine
ADP + UMP
-
enzyme is part of the anabolic pathway by which the preformed pyrimidine nucleosides are salvaged for nucleic acid biosynthesis
-
?
ATP + uridine
ADP + UMP
-
rate limiting enzyme of pyrimidine salvage pathway
-
?
ATP + uridine
ADP + UMP
-
rate-limiting enzyme in anabolism of uridine and cytidine
-
?
ATP + uridine
ADP + UMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + uridine
ADP + UMP
-
first enzyme of pyrimidine salvage pathway
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
substrate of mutant ttCKs Y93H and Y93Q, not of wild-type ttCK Y93
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
ATP + uridine
ADP + UMP
substrate of mutant ttCKs Y93H and Y93Q, not of wild-type ttCK Y93
-
-
?
ATP + uridine
ADP + UMP
-
-
-
?
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(1E)-[[4-(4-tert-butylphenyl)-5-cyano-6-hydroxypyrimidin-2-yl]sulfanyl]-N-(2-methoxyphenyl)ethanimidic acid
-
(1Z)-[([5-[(4-fluorophenyl)methyl]-7-oxo-6,7-dihydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]-N-(2-methylphenyl)ethanimidic acid
-
1-(p-toluenesulfonyl) cytosine
-
44% inhibition at 0.001 mM
2-[(5-cyano-4-hydroxy-6-phenylpyrimidin-2-yl)sulfanyl]-N-(4-ethylphenyl)acetamide
-
2-[[1-(4-fluorophenyl)-4-oxo-5H-pyrazolo[3,4-d]pyrimidin-6-yl]sulfanyl]-N-[2-(trifluoromethyl)phenyl]acetamide
-
2-[[4-(4-tert-butylphenyl)-5-cyano-6-hydroxypyrimidin-2-yl]sulfanyl]-N-(4-chlorophenyl)acetamide
-
3-(2-[[9-methoxy-2-(4-methylphenyl)-5H-[1]benzopyrano[2,3-d]pyrimidin-4-yl]sulfanyl]acetamido)benzoic acid
-
3-(2-[[9-methyl-2-(4-methylphenyl)-5H-[1]benzopyrano[2,3-d]pyrimidin-4-yl]sulfanyl]acetamido)benzoic acid
-
3-[[2-[[2-(4-fluorophenyl)-5H-chromeno[2,3-d]pyrimidin-4-yl]sulfanyl]acetyl]amino]benzoic acid
-
4-(2-[[9-methyl-2-(4-methylphenyl)-5H-[1]benzopyrano[2,3-d]pyrimidin-4-yl]sulfanyl]acetamido)benzoic acid
-
4-[[2-[[2-(4-methoxyphenyl)-5H-chromeno[2,3-d]pyrimidin-4-yl]sulfanyl]acetyl]amino]benzoic acid
-
5'-Amino-5-deoxyuridine
-
-
5'-Azido-5'-deoxycytidine
-
-
5'-Azido-5'-deoxyuridine
-
-
5'-Azido-5-deoxyuridine
-
-
5'-Iodo-5'-deoxyuridine
-
-
5'-O-Nitro-5-fluorouridine
-
-
5-propyl-2'-deoxyuridine
-
6-(4-hexyloxyanilino)uracil
-
bhutkesoside A
isolated from Ligusticopsis wallichiana (Apiaceae). Hydrophobic interactions are predicted for bhutkesoside A with Phe83
bhutkesoside B
isolated from Ligusticopsis wallichiana (Apiaceae). Bhutkesoside B is estimated to inhibit UCK2 protein by binding to the catalytic active site of ATP, thus inhibiting ATP from binding to its active site in the UCK2 protein. Hydrophobic interactions are predicted for bhutkesoside B with Ala30
cytidine
competitive inhibitor of phosphorylation of uridine
N-(3,5-dimethylphenyl)-2-[([5-[(4-fluorophenyl)methyl]-7-oxo-2,5,6,7-tetrahydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]acetamide
inhibits 3'-ethynylcytidine 5'-triphosphate (5-EU) salvage by about 40% at 0.05 mM
N-(4-bromophenyl)-2-[[1-(4-fluorophenyl)-4-hydroxy-1H-pyrazolo[3,4-d]pyrimidin-6-yl]sulfanyl]acetamide
-
p-chloromercuribenzoate
-
0.17 mM, 67% inhibition, 0.69 mM, 82% inhibition, glutathione protects
ATP
noncompetitive
ATP
-
inhibitory when not complexed with Mg2+
CTP
-
0.6 mM, approx. 80% inhibition of soluble enzyme, complete inhibition of Pb2+-precipitated enzyme
CTP
-
0.1 mM, complete inhibition
CTP
-
80-85% inhibition at approx. 2 mM
CTP
-
enzyme shows a temperature dependence of CTP inhibition
CTP
-
feedback inhibition
CTP
-
feedback inhibition, most effective in the absence of Mg2+
CTP
-
complete inhibition at approx. 2 mM
CTP
-
0.56 mM, 50% inhibition
CTP
-
inhibition is partially lost upon ageing of the enzyme and CTP becomes effective as a phosphate donor
CTP
inhibition of wild-type ttCK and mutant Y93H ttCK
UTP
-
-
UTP
-
feedback inhibition
UTP
-
feedback inhibition, most effective in the absence of Mg2+
UTP
inhibition of wild-type ttCK Y93, no inhibition of mutant ttCK H93
additional information
establishment and miniaturization of an in vitro assay for UCK2 activity and high-throughput screen against an about 40,000-compound library to generate drug-like leads. Analysis of the structures, activities, and modes of inhibition of the most promising hits, overview. Non-competitive UCK2 inhibitors are identified which are able to suppress nucleoside salvage in cells both in the presence and absence of dihydroorotate dehydrogenase (DHODH) inhibitors. No inhibition by 2-[[9-methyl-2-(4-methylphenyl)-5H-[1]benzopyrano[2,3-d]pyrimidin-4-yl]sulfanyl]-N-phenylacetamide, and (1Z)-N-(4-fluorophenyl)[([5-[(4-fluorophenyl)methyl]-7-oxo-6,7-dihydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]ethanimidic acid
-
additional information
-
establishment and miniaturization of an in vitro assay for UCK2 activity and high-throughput screen against an about 40,000-compound library to generate drug-like leads. Analysis of the structures, activities, and modes of inhibition of the most promising hits, overview. Non-competitive UCK2 inhibitors are identified which are able to suppress nucleoside salvage in cells both in the presence and absence of dihydroorotate dehydrogenase (DHODH) inhibitors. No inhibition by 2-[[9-methyl-2-(4-methylphenyl)-5H-[1]benzopyrano[2,3-d]pyrimidin-4-yl]sulfanyl]-N-phenylacetamide, and (1Z)-N-(4-fluorophenyl)[([5-[(4-fluorophenyl)methyl]-7-oxo-6,7-dihydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]ethanimidic acid
-
additional information
discovery of two diacetylene glycosides as human uridine-cytidine kinase 2 inhibitors, in an in silico approach. Molecular ligand-protein docking, using uridine-cytidine kinase 2 structure PDB ID 1UDW. Druggability likeliness property of Bhutkesoside A and Bhutkesoside B as GPCR ligands, ion channel modulators (ICM), kinase inhibitors (KI), nuclear receptor ligands (NRL), protease inhibitors (PI) and enzyme inhibitors (EI) are studied, and results are retrieved as bioactivity scores, overview
-
additional information
-
no substrate inhibition of cytidine and 5-fluorouridine at substrate concentrations higher than 0.5 mM
-
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0.2
3-deazauridine
-
pH 8.0, 22°C
0.03 - 0.069
5-fluorouridine
0.34
6-azauridine
-
pH 8.0, 22°C
additional information
additional information
-
0.03
5-fluorouridine
-
pH 7.4, 37°C
0.069
5-fluorouridine
-
pH 8.0, 22°C
0.062
ATP
pH 8.5, temperature not specified in the publication
0.37
ATP
-
37°C, foetal liver uridine kinase
0.37
ATP
-
ATP in form of MgATP2-
0.8
ATP
-
pH 7.6, 37°C, normal liver
2.1
ATP
-
pH 7.5, 25°C, cosubstrate cytidine
3.6
ATP
-
pH 7.5, 25°C, cosubstrate uridine
5
ATP
-
pH 7.6, 37°C, hepatoma cells
0.023
cytidine
-
pH 7.4, 37°C
0.042
cytidine
pH 7.2, 25°C, recombinant wild-type enzyme UCK2
0.045
cytidine
-
pH 7.5, 25°C
0.057
cytidine
-
pH 8.0, 22°C
0.071
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93W
0.072
cytidine
wild-type ttCK Y93, pH 8.0, 25°C
0.072
cytidine
pH 7.2, 25°C, recombinant wild-type enzyme ttCK
0.086
cytidine
pH 7.6, 37°C, recombinant uridine kinase 2
0.1
cytidine
mutant ttCK Y93F, pH 8.0, 25°C
0.1
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93F
0.1
cytidine
recombinant isozyme UCK2, pH 7.6, 37°C
0.13
cytidine
-
pH 7.8, 37°C
0.138
cytidine
pH 7.2, 25°C, recombinant UCK2 mutant
0.186
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93E
0.2
cytidine
mutant ttCK Y59F, pH 8.0, 25°C
0.215
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93C
0.22
cytidine
mutant ttCK Y93H, pH 8.0, 25°C
0.22
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93H
0.225
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93S
0.23
cytidine
mutant ttCK Y93Q, pH 8.0, 25°C
0.23
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93Q
0.236
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93D
0.3
cytidine
pH 7.6, 37°C, recombinant uridine kinase 1
0.383
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93A
0.42
cytidine
mutant ttCK Y93L, pH 8.0, 25°C
0.42
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93L
0.47
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93N
0.555
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93P
0.574
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93V
0.587
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93T
0.62
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93G
0.95
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93M
0.965
cytidine
pH 7.2, 25°C, recombinant ttCK mutant Y93I
4
cytidine
recombinant isozyme UCK1, pH 7.6, 37°C
0.04
uridine
-
pH 8.0, 22°C
0.048
uridine
-
pH 7.4, 37°C
0.05
uridine
pH 7.6, 37°C, recombinant uridine kinase 2
0.052
uridine
-
37°C, adult liver uridine kinase
0.058
uridine
pH 7.2, 25°C, recombinant wild-type enzyme UCK2
0.061
uridine
pH 8.5, temperature not specified in the publication
0.13
uridine
recombinant isozyme UCK2, pH 7.6, 37°C
0.15
uridine
-
pH 7.5, 25°C
0.21
uridine
-
pH 7.5, 10°C
0.3
uridine
pH 7.6, 37°C, recombinant uridine kinase 1
0.35
uridine
-
pH 7.8, 37°C
0.36
uridine
mutant ttCK Y93H, pH 8.0, 25°C
0.36
uridine
pH 7.2, 25°C, recombinant ttCK mutant Y93H
0.4
uridine
-
37°C, foetal liver uridine kinase
0.5
uridine
-
pH 7.6, 37°C, ovarian carcinoma
0.64
uridine
-
pH 7.5, 37°C
0.8
uridine
-
pH 7.6, 37°C, normal liver
1.6
uridine
-
pH 7.5, 60°C
1.6
uridine
mutant ttCK Y93Q, pH 8.0, 25°C
1.6
uridine
pH 7.2, 25°C, recombinant ttCK mutant Y93Q
2.1
uridine
-
pH 7.5, 25°C, cosubstrate cytidine
5
uridine
-
pH 7.6, 37°C, hepatoma cells
5.1
uridine
recombinant isozyme UCK1, pH 7.6, 37°C
11.5
uridine
-
pH 7.6, 37°C, normal ovary
additional information
additional information
steady-state kinetics
-
additional information
additional information
steady-state kinetics
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additional information
additional information
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steady-state kinetics
-
additional information
additional information
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Michaelis-Menten kineics
-
additional information
additional information
Michaelis-Menten kineics
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additional information
additional information
Michaelis-Menten kinetics in a coupled assay with lactate dehydrogenase and pyruvate kinase
-
additional information
additional information
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Michaelis-Menten kinetics in a coupled assay with lactate dehydrogenase and pyruvate kinase
-
additional information
additional information
Michaelis-Menten kinetics in a coupled assay with lactate dehydrogenase and pyruvate kinase
-
additional information
additional information
reaction kinetics and thermodynamics of wild-type and Y93 mutant enzymes, overview
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drug target
1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine (ECyd) is a potent inhibitor of RNA polymerase I and shows anticancer activity to various human solid tumors. ECyd is phosphorylated to 3'-ethynylcytidine 5'-monophosphate by uridine/cytidine kinase 2 (UCK2) and subsequently further to diphosphate and triphosphate (3'-ethyntlcytidine 5'-diphosphate, 3'-ethyntlcytidine 5'-triphosphate). 3'-Ethyntlcytidine 5'-triphosphate is an active metabolite that can inhibit RNA polymerase I competitively. IVS5 + 5 G > A mutation would affect the expression level of the UCK2 transcript and result in decreased sensitivity to ECyd. The UCK2 is a key drug-response predictive marker for innate or acquired resistance to uridine/cytidine-type nucleoside analogs
drug target
inhibition of enzyme (UCK2) induces nucleolar stress, probably by depleting nucleotide biosynthesis, thereby destabilising ribosomal biogenesis and subsequently causing cancer cell arrest and apoptotic cell death induction
malfunction
mutagenesis of Tyr93 in ttCK reveals that the uridine phosphorylation activity is restored only by replacement of Tyr93 with His or Gln
malfunction
mutation H117Y of UCK2 results in a loss of uridine phosphorylation activity of the enzyme
malfunction
overexpression of uridine-cytidine kinase 2 correlates with breast cancer progression and poor prognosis. UCK2, along with other genes involved in the 5-FU anabolic pathway, produces a phenotype of cell sensitivity to 5-FU folxadlowing knockdown
malfunction
probable ribosomal stress condition during inhibition of the UCK2 enzyme, overview. The released and subsequent activation of p53 leads towards apoptosis induction
malfunction
role of a uridine/cytidine kinase 2 mutation in cellular sensitiveness toward 3'-ethynylcytidine (ECyd) treatment of human cancer cells. The splice-site mutation of the UCK2 gene resulting in the IVS5+5 G>A variant affects the expression level of the UCK2 transcript, causing decreased sensitivity to ECyd. The IVS5+5 G>A variant generates an aberrant mRNA transcript, namely, truncated mRNA is produced and normal mRNA levels are markedly decreased in the ECyd-resistant cancer cell line HT1080. Relationship of UCK2 mutations and drug sensitivity with ECyd in several cancer cell lines, overview. Detection of the aberrant mRNA transcript in the ECyd/EUrd-resistant cancer cells with the IVS5 +5 A/A genotype
malfunction
UCK from Thermus thermophilus HB8 loses catalytic activity on uridine due to lack of a substrate binding ability and possesses an unusual amino acid, i.e. tyrosine 93 (Tyr93) at the binding site, whereas histidine (His) is located in the other UCKs. Mutagenesis experiments reveal that a replacement of Tyr93 by His or glutamine (Gln) recovers catalytic activity on uridine
malfunction
-
mutagenesis of Tyr93 in ttCK reveals that the uridine phosphorylation activity is restored only by replacement of Tyr93 with His or Gln
-
malfunction
-
UCK from Thermus thermophilus HB8 loses catalytic activity on uridine due to lack of a substrate binding ability and possesses an unusual amino acid, i.e. tyrosine 93 (Tyr93) at the binding site, whereas histidine (His) is located in the other UCKs. Mutagenesis experiments reveal that a replacement of Tyr93 by His or glutamine (Gln) recovers catalytic activity on uridine
-
malfunction
-
mutagenesis of Tyr93 in ttCK reveals that the uridine phosphorylation activity is restored only by replacement of Tyr93 with His or Gln
-
malfunction
-
UCK from Thermus thermophilus HB8 loses catalytic activity on uridine due to lack of a substrate binding ability and possesses an unusual amino acid, i.e. tyrosine 93 (Tyr93) at the binding site, whereas histidine (His) is located in the other UCKs. Mutagenesis experiments reveal that a replacement of Tyr93 by His or glutamine (Gln) recovers catalytic activity on uridine
-
metabolism
uridine-cytidine kinase is the rate-limiting enzyme in the pyrimidine-nucleotide salvage pathway, overview
metabolism
UCK2 is feedback inhibited by UTP and CTP to adjust cellular needs and prevent overproduction of the nucleotides. In the course of cancer cell proliferation, these nucleotides are continuously synthesized to sustain protein synthesis. During gene degradation, some NMPs are released and recycled via the salvage pathway by the action of UCK2, thereby facilitating the prevention of energy loss and the waste of valuable precursors. Molecular crosstalks between UCK2 and cell death, the role of ribosomal proteins, MDM2 and p53 in regulation of cell death, and the role of UCK2 in regulation of cell death
metabolism
the enzyme is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis
metabolism
-
uridine-cytidine kinase is the rate-limiting enzyme in the pyrimidine-nucleotide salvage pathway, overview
-
physiological function
a nucleosidic medicine, 1-(3-C-ethynyl-beta-D-ribopentofuranosyl) cytosine [3'-ethynylcytidine (ECyd)], is a potent inhibitor of RNA polymerase I and shows anticancer activity to various human solid tumors in vitro and in vivo. ECyd is phosphorylated to 3'-ethynylcytidine 5'-monophosphate by uridine/cytidine kinase 2 (UCK2) and subsequently further to diphosphate and triphosphate (3'-ethynylcytidine 5'-diphosphate, 3'-ethynylcytidine 5'-triphosphate). 3'-ethynylcytidine 5'-triphosphate is an active metabolite that can inhibit RNA polymerase I competitively, causing cancer cell death
physiological function
enzyme activity in two panels of tumor cell lines and xenograft cells correlated only with UCK2-mRNA expression, but not with UCK1-mRNA. Moreover, accumulation of RX-3117 nucleotides correlates with UCK2 expression
physiological function
in contrast to other UCK enzymes, UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine
physiological function
the pyrimidine salvage enzyme uridine-cytidine kinase 2 (UCK2) is necessary for uridine salvage. Biological significance of UCK2 in the uridine salvage is measured by incorporating exogenous 5-ethynyl-uridine (5-EU) specifically into cellular RNA
physiological function
UCK2 is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis. Uridine-cytidine kinase 2 (UCK2) is linked to cell apoptosis induction. Molecular crosstalk involving UCK2 protein and cancer cell death through cell cycle arrest and triggering of apoptosis involving proteins, MDM2 and the subsequent activation of p53. UCK2 is also involved in the phosphorylation of ribonucleoside analogues, 5-azacytidine, cyclopentenyl cytosine/uracil, 5-fluorocytidine, 6-azauridine, 3-deazauridine, 5-fluorouridine as well as ethynyl cytidine and uridine. These cytotoxic drugs depends on the action of the UCK2 enzyme to sequentially transformed into nucleoside 5'-triphosphate, thereby interfering with gene synthesis vital for metabolic processes required for cancer cell growth and maintenance
physiological function
uridine-cytidine kinase (UCK) 2 is a rate-limiting enzyme involved in the salvage pathway of pyrimidine-nucleotide biosynxadthesis. Isozyme UCK2 is overexpressed in many types of cancer and may play a crucial role in activating antitumor prodrugs in human cancer cells. The isozyme catalyzes the phosphorylation of urixaddine and cytidine to form uridine monophosphate (UMP) and cytidine monophosphate (CMP) with efficiency 15 to 20fold higher than that of ubiquitously expressed isozyme UCK1
physiological function
uridine-cytidine kinase (UCK) is one of the enzymes in the nucleoside salvage pathway. UCK generally converts both cytidine and uridine to nucleoside monophosphate using ATP as the phosphate donor
physiological function
uridine-cytidine kinase (UCK) is one of the enzymes in the nucleoside salvage pathway. UCK generally converts both cytidine and uridine to nucleoside monophosphate using ATP as the phosphate donor, but the UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine. This cytidine-restricted activity is thought to depend on residue Tyr93
physiological function
-
uridine-cytidine kinase (UCK) is one of the enzymes in the nucleoside salvage pathway. UCK generally converts both cytidine and uridine to nucleoside monophosphate using ATP as the phosphate donor, but the UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine. This cytidine-restricted activity is thought to depend on residue Tyr93
-
physiological function
-
in contrast to other UCK enzymes, UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine
-
physiological function
-
uridine-cytidine kinase (UCK) is one of the enzymes in the nucleoside salvage pathway. UCK generally converts both cytidine and uridine to nucleoside monophosphate using ATP as the phosphate donor, but the UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine. This cytidine-restricted activity is thought to depend on residue Tyr93
-
physiological function
-
in contrast to other UCK enzymes, UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine
-
additional information
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mechanism underlying nucleoside specificity, overview
additional information
mechanism underlying nucleoside specificity, overview
additional information
-
mechanism underlying nucleoside specificity, overview. The histidine residue located near the functional group at position 4 of cytidine or uridine in most UCKs is substituted with tyrosine, Tyr93, in ttCK, due to the naturally occuring polymorphism Y93, the UCK homologue ttCK of Thermus thermophilus HB8 has, unlike other UCKs, a substrate specificity towards only cytidine and shows no inhibition by UTP, uridine does not bind to ttCK as substrate. Replacement of Tyr93 by histidine or glutamine endows ttCK with phosphorylation activity toward uridine
additional information
mechanism underlying nucleoside specificity, overview. The histidine residue located near the functional group at position 4 of cytidine or uridine in most UCKs is substituted with tyrosine, Tyr93, in ttCK, due to the naturally occuring polymorphism Y93, the UCK homologue ttCK of Thermus thermophilus HB8 has, unlike other UCKs, a substrate specificity towards only cytidine and shows no inhibition by UTP, uridine does not bind to ttCK as substrate. Replacement of Tyr93 by histidine or glutamine endows ttCK with phosphorylation activity toward uridine
additional information
molecular dynamics simulations on the wild-type Thermus thermophilus enzyme, two mutant ttCKs, and a human UCK bound to cytidine and three protonation forms of uridine to elucidate their substrate specificity, overview. Three residues, Tyr88, Tyr/His/Gln93 and Arg152 in ttCKs, are important for recognizing the substrates. Arg152 contributes to induce a closed form of the binding site to retain the substrate, and the N3 atom of uridine needs to be deprotonated. Although Tyr88 tightly binds cytidine, it does not sufficiently bind uridine because of lack of the hydrogen bonding. His/Gln93 complements the interaction of Tyr88 and raises the affinity of ttCK to uridine. The crucial distinction between Tyr and His or Gln is a role in the hydrogen-bonding network. Therefore, the ability to form both hydrogen-bonding donor and acceptor is required to bind both uridine and cytidine. Residue interactions and kinetics. Tyr59 and Phe90 form Pi-Pi stackings and CH-Pi interaction with cytidine, and Ile113 interacts with cytidine via a hydrophobic interaction. Tyr88, His93, and Arg152 form hydrogen bonds with the cytidine base moiety, and Asp60 and Arg142 anchor the ribose moiety, role of His/Gln93 in complementing the interaction between Tyr88 and the substrate
additional information
uridine phosphorylation activity commonly depends on a single residue in the UCK family. Molecular docking analysis. Structure comparison of Thermus thermophilus enzyme ttCK and human enzyme hsUCK2
additional information
uridine phosphorylation activity commonly depends on a single residue in the UCK family. Structure comparison of Thermus thermophilus enzyme ttCK and human enzyme hsUCK2
additional information
-
uridine phosphorylation activity commonly depends on a single residue in the UCK family. Structure comparison of Thermus thermophilus enzyme ttCK and human enzyme hsUCK2
additional information
-
uridine phosphorylation activity commonly depends on a single residue in the UCK family. Molecular docking analysis. Structure comparison of Thermus thermophilus enzyme ttCK and human enzyme hsUCK2
-
additional information
-
molecular dynamics simulations on the wild-type Thermus thermophilus enzyme, two mutant ttCKs, and a human UCK bound to cytidine and three protonation forms of uridine to elucidate their substrate specificity, overview. Three residues, Tyr88, Tyr/His/Gln93 and Arg152 in ttCKs, are important for recognizing the substrates. Arg152 contributes to induce a closed form of the binding site to retain the substrate, and the N3 atom of uridine needs to be deprotonated. Although Tyr88 tightly binds cytidine, it does not sufficiently bind uridine because of lack of the hydrogen bonding. His/Gln93 complements the interaction of Tyr88 and raises the affinity of ttCK to uridine. The crucial distinction between Tyr and His or Gln is a role in the hydrogen-bonding network. Therefore, the ability to form both hydrogen-bonding donor and acceptor is required to bind both uridine and cytidine. Residue interactions and kinetics. Tyr59 and Phe90 form Pi-Pi stackings and CH-Pi interaction with cytidine, and Ile113 interacts with cytidine via a hydrophobic interaction. Tyr88, His93, and Arg152 form hydrogen bonds with the cytidine base moiety, and Asp60 and Arg142 anchor the ribose moiety, role of His/Gln93 in complementing the interaction between Tyr88 and the substrate
-
additional information
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uridine phosphorylation activity commonly depends on a single residue in the UCK family. Molecular docking analysis. Structure comparison of Thermus thermophilus enzyme ttCK and human enzyme hsUCK2
-
additional information
-
molecular dynamics simulations on the wild-type Thermus thermophilus enzyme, two mutant ttCKs, and a human UCK bound to cytidine and three protonation forms of uridine to elucidate their substrate specificity, overview. Three residues, Tyr88, Tyr/His/Gln93 and Arg152 in ttCKs, are important for recognizing the substrates. Arg152 contributes to induce a closed form of the binding site to retain the substrate, and the N3 atom of uridine needs to be deprotonated. Although Tyr88 tightly binds cytidine, it does not sufficiently bind uridine because of lack of the hydrogen bonding. His/Gln93 complements the interaction of Tyr88 and raises the affinity of ttCK to uridine. The crucial distinction between Tyr and His or Gln is a role in the hydrogen-bonding network. Therefore, the ability to form both hydrogen-bonding donor and acceptor is required to bind both uridine and cytidine. Residue interactions and kinetics. Tyr59 and Phe90 form Pi-Pi stackings and CH-Pi interaction with cytidine, and Ile113 interacts with cytidine via a hydrophobic interaction. Tyr88, His93, and Arg152 form hydrogen bonds with the cytidine base moiety, and Asp60 and Arg142 anchor the ribose moiety, role of His/Gln93 in complementing the interaction between Tyr88 and the substrate
-
additional information
-
mechanism underlying nucleoside specificity, overview
-
additional information
-
mechanism underlying nucleoside specificity, overview. The histidine residue located near the functional group at position 4 of cytidine or uridine in most UCKs is substituted with tyrosine, Tyr93, in ttCK, due to the naturally occuring polymorphism Y93, the UCK homologue ttCK of Thermus thermophilus HB8 has, unlike other UCKs, a substrate specificity towards only cytidine and shows no inhibition by UTP, uridine does not bind to ttCK as substrate. Replacement of Tyr93 by histidine or glutamine endows ttCK with phosphorylation activity toward uridine
-
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H117Y
site-directed mutagenesis, the mutation results in a loss of uridine phosphorylation activity of the enzyme
Y93A
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93C
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93D
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93E
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93F
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93G
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93I
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93K
site-directed mutagenesis, inactive mutant
Y93L
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93M
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93N
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93P
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93R
site-directed mutagenesis, inactive mutant
Y93S
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93T
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93V
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93W
site-directed mutagenesis, the mutation does not restore the uridine kinase activity that has been lost in the wild-type enzyme
Y93A
-
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
-
Y93D
-
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
-
Y93F
-
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
-
Y93Q
-
site-directed mutagenesis, the mutant enzyme shows restored activity on uridine in contrast to the wild-type enzyme. The mutant has higher binding affinities to cytidine than the wild-type
-
Y93S
-
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
-
Y93A
-
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
-
Y93D
-
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
-
Y93F
-
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
-
Y93Q
-
site-directed mutagenesis, the mutant enzyme shows restored activity on uridine in contrast to the wild-type enzyme. The mutant has higher binding affinities to cytidine than the wild-type
-
Y93S
-
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
-
Y93H
site-directed mutagenesis, the mutant enzyme shows restored activity on uridine in contrast to the wild-type enzyme. The mutant has higher binding affinities to cytidine than the wild-type
Y93H
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93Q
site-directed mutagenesis, the mutant enzyme shows restored activity on uridine in contrast to the wild-type enzyme. The mutant has higher binding affinities to cytidine than the wild-type
Y93Q
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
Y93H
-
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
-
Y93H
-
site-directed mutagenesis, the mutant enzyme shows restored activity on uridine in contrast to the wild-type enzyme. The mutant has higher binding affinities to cytidine than the wild-type
-
Y93H
-
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
-
Y93H
-
site-directed mutagenesis, the mutant enzyme shows restored activity on uridine in contrast to the wild-type enzyme. The mutant has higher binding affinities to cytidine than the wild-type
-
additional information
contrary to wild-type, enzyme T-DNA insertion mutant plants are not affected in growth when treated with 5-fluorouracil or 5-fluorouridine. Expression of UK/UPRT1 in upp and uppudk mutants of Escherichia coli supplied with 5-fluorouracil and 5-fluorouridine leads to growth inhibition. Identical results are obtained with 5-fluorouridine and 5-fluorouracil treatments when the uridine kinase and uracil phosphoribosyltransferase domains are separated by the introduction of translation initiation and stop codons prior to complementation into the upp-udk and upp mutants
additional information
-
contrary to wild-type, enzyme T-DNA insertion mutant plants are not affected in growth when treated with 5-fluorouracil or 5-fluorouridine. Expression of UK/UPRT1 in upp and uppudk mutants of Escherichia coli supplied with 5-fluorouracil and 5-fluorouridine leads to growth inhibition. Identical results are obtained with 5-fluorouridine and 5-fluorouracil treatments when the uridine kinase and uracil phosphoribosyltransferase domains are separated by the introduction of translation initiation and stop codons prior to complementation into the upp-udk and upp mutants
additional information
-
overexpression of gene udk encoding uridine/cytidine kinase interferes with T7 bacteriophage growth. This inhibition can be overcome by inhibition of host RNA polymerase by overexpression of gene 2 or by treatment with rifampicin
additional information
enzyme silencing by transfection of A549 and SW1573 cell lines with UCK-siRNAs. Transfection of UCK1-siRNA efficiently downregulates UCK1-mRNA, but not UCK2-mRNA expression, and does not affect sensitivity to RX-3117. Transfection of UCK2-siRNA completely downregulates UCK2-mRNA and protein and protects both A549 and SW1573 against RX-3117
additional information
-
enzyme silencing by transfection of A549 and SW1573 cell lines with UCK-siRNAs. Transfection of UCK1-siRNA efficiently downregulates UCK1-mRNA, but not UCK2-mRNA expression, and does not affect sensitivity to RX-3117. Transfection of UCK2-siRNA completely downregulates UCK2-mRNA and protein and protects both A549 and SW1573 against RX-3117
additional information
several functional point mutations, including the splice-site mutation of the UCK2 gene IVS5+5 G>A, are identified in the UCK2 enzyme protein. The IVS5+5 G>A variant generates an aberrant mRNA transcript, namely, truncated mRNA is produced and normal mRNA levels are markedly decreased in the ECyd-resistant cancer cell line HT1080. Effect of the IVS5+5G>A variation on pre-mRNA splicing. The IVS5+ 5 A/A genotype that is 98 bp shorter than a normal PCR product is detected. This variant-type UCK2 mRNA in HT1080/EUrd generates an aberrant stop codon and it produces an UCK2 protein without the C-terminal region. The wild-type UCK2 protein consists of 261 amino acid residues. In contrast, although the variant-type UCK2 mRNA conserves 166 amino acids in part of the N-terminus of UCK2, codons 167-171 are substituted by other amino acids by the frameshift mutation and parts of the C-terminal, codons 172-261, are missing (truncated). This missing region has been considered the substrate recognition site (LID domain) as well as the tetramer stabilization site. In addition, the mRNA with premature translation termination codon and coding nonfunctional protein is known to be eliminated by nonsense-mediated mRNA decay. It is possible that deletion of this region causes loss of stabilization and specific substrate recognition in UCK2 functions
additional information
-
several functional point mutations, including the splice-site mutation of the UCK2 gene IVS5+5 G>A, are identified in the UCK2 enzyme protein. The IVS5+5 G>A variant generates an aberrant mRNA transcript, namely, truncated mRNA is produced and normal mRNA levels are markedly decreased in the ECyd-resistant cancer cell line HT1080. Effect of the IVS5+5G>A variation on pre-mRNA splicing. The IVS5+ 5 A/A genotype that is 98 bp shorter than a normal PCR product is detected. This variant-type UCK2 mRNA in HT1080/EUrd generates an aberrant stop codon and it produces an UCK2 protein without the C-terminal region. The wild-type UCK2 protein consists of 261 amino acid residues. In contrast, although the variant-type UCK2 mRNA conserves 166 amino acids in part of the N-terminus of UCK2, codons 167-171 are substituted by other amino acids by the frameshift mutation and parts of the C-terminal, codons 172-261, are missing (truncated). This missing region has been considered the substrate recognition site (LID domain) as well as the tetramer stabilization site. In addition, the mRNA with premature translation termination codon and coding nonfunctional protein is known to be eliminated by nonsense-mediated mRNA decay. It is possible that deletion of this region causes loss of stabilization and specific substrate recognition in UCK2 functions
additional information
-
the histidine residue located near the functional group at position 4 of cytidine or uridine in most UCKs is substituted with tyrosine, Tyr93, in ttCK, due to the naturally occuring polymorphism Y93, the UCK homologue ttCK of Thermus thermophilus HB8 has, unlike other UCKs, a substrate specificity towards only cytidine and shows no inhibition by UTP, uridine does not bind to ttCK as substrate. Replacement of Tyr93 by histidine or glutamine endows ttCK with phosphorylation activity toward uridine
additional information
the histidine residue located near the functional group at position 4 of cytidine or uridine in most UCKs is substituted with tyrosine, Tyr93, in ttCK, due to the naturally occuring polymorphism Y93, the UCK homologue ttCK of Thermus thermophilus HB8 has, unlike other UCKs, a substrate specificity towards only cytidine and shows no inhibition by UTP, uridine does not bind to ttCK as substrate. Replacement of Tyr93 by histidine or glutamine endows ttCK with phosphorylation activity toward uridine
additional information
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the histidine residue located near the functional group at position 4 of cytidine or uridine in most UCKs is substituted with tyrosine, Tyr93, in ttCK, due to the naturally occuring polymorphism Y93, the UCK homologue ttCK of Thermus thermophilus HB8 has, unlike other UCKs, a substrate specificity towards only cytidine and shows no inhibition by UTP, uridine does not bind to ttCK as substrate. Replacement of Tyr93 by histidine or glutamine endows ttCK with phosphorylation activity toward uridine
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