2.7.1.74: deoxycytidine kinase
This is an abbreviated version!
For detailed information about deoxycytidine kinase, go to the full flat file.
Word Map on EC 2.7.1.74
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2.7.1.74
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leukemia
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gemcitabine
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thymidine
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triphosphate
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deaminase
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purine
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ribonucleotide
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deoxynucleoside
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pyrimidine
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deoxyguanosine
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salvage
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myeloid
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arabinoside
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cytarabine
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prodrugs
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deoxyadenosine
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1-beta-d-arabinofuranosylcytosine
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deoxyribonucleoside
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5'-nucleotidase
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cladribine
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cross-resistance
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ara-ctp
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2-chlorodeoxyadenosine
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2',2'-difluorodeoxycytidine
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fludarabine
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dttp
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antileukemic
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ccrf-cem
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dfdctp
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2-chloro-2'-deoxyadenosine
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gemcitabine-resistant
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dado
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deoxycytidylate
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kinase-deficient
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clofarabine
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2',3'-dideoxycytidine
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5'-phosphorylation
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arabinosyl
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deoxypyrimidine
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t-lymphoblastoid
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deoxycoformycin
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medicine
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2'-deoxyadenosine
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deoxythymidine
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l-nucleoside
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dideoxycytidine
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t-lymphoblasts
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2',3'-dideoxyinosine
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tetrahydrouridine
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arabinosylcytosine
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anabolites
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pharmacology
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analysis
- 2.7.1.74
- leukemia
- gemcitabine
- thymidine
- triphosphate
- deaminase
- purine
- ribonucleotide
- deoxynucleoside
- pyrimidine
- deoxyguanosine
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salvage
- myeloid
- arabinoside
- cytarabine
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prodrugs
- deoxyadenosine
- 1-beta-d-arabinofuranosylcytosine
- deoxyribonucleoside
- 5'-nucleotidase
- cladribine
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cross-resistance
- ara-ctp
- 2-chlorodeoxyadenosine
- 2',2'-difluorodeoxycytidine
- fludarabine
- dttp
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antileukemic
-
ccrf-cem
-
dfdctp
- 2-chloro-2'-deoxyadenosine
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gemcitabine-resistant
-
dado
- deoxycytidylate
-
kinase-deficient
- clofarabine
- 2',3'-dideoxycytidine
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5'-phosphorylation
-
arabinosyl
-
deoxypyrimidine
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t-lymphoblastoid
- deoxycoformycin
- medicine
- 2'-deoxyadenosine
- deoxythymidine
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l-nucleoside
- dideoxycytidine
- t-lymphoblasts
- 2',3'-dideoxyinosine
- tetrahydrouridine
- arabinosylcytosine
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anabolites
- pharmacology
- analysis
Reaction
Synonyms
2'-deoxycytidine kinase, ara-C kinase, arabinofuranosylcytosine kinase, dC kinase, dCK, deoxycytidine kinase, deoxycytidine-cytidine kinase, dNTP:deoxycytidine 5'-phosphotransferase, kinase, deoxycytidine (phosphorylating), NTP:deoxycytidine 5'-phosphotransferase
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 2.7.1.74 - deoxycytidine kinase
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phosphoprotein
additional information
phosphoprotein
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no changes in kinetic parameters of recombinant enzyme after treatment with protein kinases A or C
phosphoprotein
at least four residues phosphorylated, Thr-3, Ser-11, Ser-15, and Ser-74, Ser-74 phosphorylation level important for enzyme activity
phosphoprotein
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phosphorylation of the enzyme involved in the regulation of enzyme activity
phosphoprotein
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interindividual variability in deoxycytidine kinase activity is related to its phosphorylation level on residue Ser74
phosphoprotein
kinetic properties of the enzyme are modulated in vivo by phosphorylation of Ser74, conformational changes and mechanism, overview
phosphoprotein
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phosphorylation of deoxycytidine kinase on Ser74 increases the enzyme activity, increasing dCK activity via Ser74 phosphorylation, e.g. by aphidicolin, can enhance the intracellular activation of some nucleoside analogs, like gemcitabine, but not of cladribine or fludarabine, overview
phosphoprotein
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the ataxia-telangiectasia-mutated kinase phosphorylates the enzyme on Ser74 to activate it in response to DNA damage, required in vivo and in vitro. Ser74 phosphorylation is required for initiation of the G2/M checkpoint
phosphoprotein
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the enzyme contains four in vivo phosphorylation sites: Thr3, Ser11, Ser-15, and Ser74. Phosphorylation of Ser74, the major phosphorylated residue, strongly influences dCK activity in vivo. Phosphorylation of the three other sites, located in the N-terminal extremity of the protein, does not significantly modify enzyme activity, but phosphorylation of Thr3 can promote enzyme stability
phosphoprotein
the enzyme is phosphorylated on serine 74 by the ataxia-telangiectasia mutated kinase
additional information
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a posttranslational modification is suggested to be responsible for the UV-C light irradiation induced activation of the enzyme activity
additional information
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irradiation induced phosphorylation suggested to be involved in the regulation of enzyme activity