2.7.1.48: uridine/cytidine kinase
This is an abbreviated version!
For detailed information about uridine/cytidine kinase, go to the full flat file.
Word Map on EC 2.7.1.48
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2.7.1.48
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thymidine
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salvage
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uracil
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phosphoribosyltransferase
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phosphorylase
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orotate
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ump
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5-fluorouracil
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5-fluorouridine
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deoxycytidine
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5-azacytidine
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6-azauridine
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3-deazauridine
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orotidine
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pyrazofurin
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medicine
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5-fluoro-2'-deoxyuridine
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3huridine
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dihydrouracil
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drug development
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diagnostics
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biotechnology
- 2.7.1.48
- thymidine
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salvage
- uracil
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phosphoribosyltransferase
- phosphorylase
- orotate
- ump
- 5-fluorouracil
- 5-fluorouridine
- deoxycytidine
- 5-azacytidine
- 6-azauridine
- 3-deazauridine
- orotidine
- pyrazofurin
- medicine
- 5-fluoro-2'-deoxyuridine
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3huridine
- dihydrouracil
- drug development
- diagnostics
- biotechnology
Reaction
Synonyms
ATP:uridine 5'-phosphotransferase, hsUCK2, kinase, uridine (phosphorylating), More, pyrimidine ribonucleoside kinase, ttCK, UCK, UCK1, UCK2, UCKL1, Udk, UK/UPRT1, uridine cytidine kinase 2, uridine kinase, uridine phosphokinase, uridine-cytidine kinase, uridine-cytidine kinase 2, uridine/cytidine kinase, uridine/cytidine kinase 2
ECTree
2.7.1.48 uridine/cytidine kinaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.1.48 - uridine/cytidine kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
Y93H
Y93I
site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
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
Y93Q
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
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site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
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Y93D
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site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
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Y93F
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site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
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Y93H
Y93Q
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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
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Y93S
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site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
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Y93A
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site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
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Y93D
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site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
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Y93F
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site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
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Y93H
Y93Q
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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
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Y93S
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site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
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additional information
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
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site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
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Y93H
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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
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Y93H
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site-directed mutagenesis, the mutation restores the uridine kinase activity that has been lost in the wild-type enzyme
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Y93H
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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
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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
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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
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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
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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
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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
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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
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
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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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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