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Information on EC 2.7.1.74 - deoxycytidine kinase and Organism(s) Homo sapiens and UniProt Accession P27707

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EC Tree
IUBMB Comments
Cytosine arabinoside can act as acceptor; all natural nucleoside triphosphates (except dCTP) can act as donors.
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P27707
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Word Map
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
deoxycytidine kinase, 2'-deoxycytidine kinase, ara-c kinase, dc kinase, deoxycytidine-cytidine kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2'-deoxycytidine kinase
-
NTP:deoxycytidine 5'-phosphotransferase
-
2'-deoxycytidine kinase
-
-
-
-
ara-C kinase
-
-
-
-
arabinofuranosylcytosine kinase
-
-
-
-
deoxycytidine kinase
-
-
deoxycytidine-cytidine kinase
-
-
-
-
dNTP:deoxycytidine 5'-phosphotransferase
-
-
kinase, deoxycytidine (phosphorylating)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NTP + deoxycytidine = NDP + dCMP
show the reaction diagram
substrate-enzyme interactions, bi bi random reaction mechanism with ATP, but ordered with UTP binding before the acceptor substrate, substrate binding site structures
NTP + deoxycytidine = NDP + dCMP
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
NTP:deoxycytidine 5'-phosphotransferase
Cytosine arabinoside can act as acceptor; all natural nucleoside triphosphates (except dCTP) can act as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9039-45-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (-)-beta-2',3'-dideoxy-3'-thiacytidine
ADP + (-)-beta-2',3'-dideoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + (E)-5-(2-bromovinyl)-2'-deoxyuridine
ADP + ?
show the reaction diagram
substrate of enzyme mutant R104M/D133A, poor substrate of the wild-type enzyme
-
-
?
ATP + 1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)cytosine
ADP + 1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)cytosine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + 1-beta-D-arabinofuranosylcytosine
ADP + 1-beta-D-arabinofuranosylcytosine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + 1-beta-D-arabinosylcytosine
ADP + 1-beta-D-arabinosylcytosine 5'-phosphate
show the reaction diagram
ATP + 2',2'-difluorodeoxycytidine
ADP + 2',2'-difluorodeoxycytidine 5'-monophosphate
show the reaction diagram
i.e. gemcitabine
-
-
?
ATP + 2',2'-difluorodeoxycytidine
ADP + 2',2'-difluorodeoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + 2',3'-dideoxycytidine
ADP + 2',3'-dideoxycytidine 5'-phosphate
show the reaction diagram
i.e. zalcitabine
-
-
?
ATP + 2'-deoxy-3'-thiacytidine
ADP + 2'-deoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + 2'-deoxyadenosine
ADP + 2'-deoxyadenosine 5'-phosphate
show the reaction diagram
ATP + 2'-deoxycytidine
ADP + 2'-deoxy-CMP
show the reaction diagram
-
-
-
?
ATP + 2'-deoxycytidine
ADP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
ATP + 2'-deoxyguanosine
ADP + 2'-deoxyguanosine 5'-phosphate
show the reaction diagram
ATP + 2-chloro-2'-deoxyadenosine
ADP + 2-chloro-2'-deoxyadenosine 5'-phosphate
show the reaction diagram
i.e. cladribine
-
-
?
ATP + 2-chlorodeoxyadenosine
ADP + 2-chlorodeoxyadenosine 5'-phosphate
show the reaction diagram
i.e. cladribine
-
-
?
ATP + 5-bromodeoxycytidine
ADP + 5-bromo-dCMP
show the reaction diagram
-
-
-
?
ATP + 5-iododeoxycytidine
ADP + 5-iodo-dCMP
show the reaction diagram
-
-
-
?
ATP + 5-methyldeoxycytidine
ADP + 5-methyl-dCMP
show the reaction diagram
-
-
-
?
ATP + 5-propynyldeoxycytidine
ADP + 5-propynyl-dCMP
show the reaction diagram
-
-
-
?
ATP + arabinosyl adenine
ADP + arabinosyl adenine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + arabinosyl cytosine
ADP + arabinosyl cytosine 5'-phosphate
show the reaction diagram
i.e. cytosar
-
-
?
ATP + beta-L-2',3'-dideoxy-3'-thiacytidine
ADP + beta-L-2',3'-dideoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + clofarabine
ADP + clofarabine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + D-2'-deoxycytidine
ADP + D-2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + D-deoxycytidine
ADP + D-dCMP
show the reaction diagram
-
-
-
?
ATP + D-deoxythymidine
ADP + D-dTMP
show the reaction diagram
-
-
-
?
ATP + D-deoxyuridine
ADP + D-dUMP
show the reaction diagram
-
-
-
?
ATP + deoxyadenosine
ADP + dAMP
show the reaction diagram
ATP + deoxycytidine
ADP + dCMP
show the reaction diagram
ATP + deoxyguanosine
ADP + dGMP
show the reaction diagram
ATP + dideoxythymidine
ADP + dideoxythymidine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + difluoro-arabinofuranosyl adenine
ADP + difluoro-arabinofuranosyl adenine 5'-phosphate
show the reaction diagram
i.e. fludarabine
-
-
?
ATP + difluorodeoxycytidine
ADP + difluorodeoxycytidine 5'-phosphate
show the reaction diagram
i.e. gemcitabine
-
-
?
ATP + fludarabine
ADP + fludarabine 5'-phosphate
show the reaction diagram
ATP + gemcitabine
ADP + gemcitabine 5'-phosphate
show the reaction diagram
ATP + gemcitabine
ADP + phospho-gemcitabine
show the reaction diagram
-
-
-
?
ATP + L-2'-deoxycytidine
ADP + L-2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + L-deoxyuridine
ADP + L-dUMP
show the reaction diagram
-
-
-
?
ATP + L-thymidine
?
show the reaction diagram
human dCK, in addition to being able to phosphorylate both purines and pyrimidines, has the special ability to accept L-nucleosides as substrates
-
-
?
ATP + L-thymidine
ADP + L-dTMP
show the reaction diagram
-
-
-
?
ATP + lamivudine
ADP + lamivudine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + thymidine
ADP + L-dTMP
show the reaction diagram
-
-
-
?
ATP + thymidine
ADP + TMP
show the reaction diagram
-
-
-
?
ATP + troxacitabine
ADP + troxacitabine 5'-phosphate
show the reaction diagram
-
-
-
?
GTP + arabinosyl-adenine
GDP + arabinosyl-adenine 5'-phosphate
show the reaction diagram
-
-
-
?
GTP + azacytidine
GDP + azacytidine 5'-phosphate
show the reaction diagram
-
-
-
?
GTP + cladribine
GDP + cladribine 5'-phosphate
show the reaction diagram
-
-
-
?
GTP + clofarabine
GDP + clofarabine 5'-phosphate
show the reaction diagram
-
-
-
?
GTP + fludarabine
GDP + fludarabine 5'-phosphate
show the reaction diagram
54% conversion
-
-
?
GTP + gemcitabine
GDP + gemcitabine 5'-phosphate
show the reaction diagram
-
-
-
?
GTP + lamivudine
GDP + lamivudine 5'-phosphate
show the reaction diagram
-
-
-
?
NTP + 1-beta-D-arabinofuranosylcytosine
NDP + 1-beta-D-arabinofuranosylcytosine 5'-phosphate
show the reaction diagram
antineoplastic agent
-
-
?
NTP + 1-beta-D-arabinosylcytosine
NDP + 1-beta-D-arabinosylcytosine 5'-phosphate
show the reaction diagram
i.e. cytaribine, activation of the pharmaceutically relevant substrate which is commonly used in the treatment of lymphoproliferative malignancies
-
-
?
NTP + 2',2'-difluorodeoxycytidine
NDP + 2',2'-difluorodeoxycytidine 5'-phosphate
show the reaction diagram
i.e. gemcitabine, activation of the pharmaceutically relevant substrate which is commonly used in the treatment of solid malignant tumors
-
-
?
NTP + 2',3'-dideoxycytidine
NDP + 2',3'-dideoxycytidine 5'-phosphate
show the reaction diagram
NTP + 2'-deoxy-3'-thiacytidine
NDP + 2'-deoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
NTP + 2'-deoxyadenosine
NDP + 2'-deoxyadenosine 5'-phosphate
show the reaction diagram
NTP + 2'-deoxycytidine
NDP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
NTP + 2'-deoxyguanosine
NDP + 2'-deoxyguanosine 5'-phosphate
show the reaction diagram
NTP + 2-chloro-2'-deoxyadenosine
NDP + 2-chloro-2'-deoxyadenosine 5'-phosphate
show the reaction diagram
NTP + 2-chloro-9-(2-deoxy-2-fluoro-beta-D-arabinofuranosyl)-9H-purin-6-amine
NDP + 2-chloro-9-(2-deoxy-2-fluoro-beta-D-arabinofuranosyl)-9H-purin-6-amine 5'-phosphate
show the reaction diagram
i.e. clofarabine, rate-limiting step in the activation of the prodrug, precursor of an effective chemotherapeutic agent for leukemias and other haematological malignancies
-
-
?
NTP + 9-beta-D-arabinosyl 2-fluoroadenine
NDP + 9-beta-D-arabinosyl 2-fluoroadenine 5'-phosphate
show the reaction diagram
i.e. fludarabine, activation of the pharmaceutically relevant substrate which is commonly used in the treatment of lymphoproliferative malignancies
-
-
?
NTP + cytarabine
NDP + cytarabine 5'-phosphate
show the reaction diagram
-
-
-
?
NTP + deoxycytidine
NDP + dCMP
show the reaction diagram
-
-
-
?
UTP + (-)-beta-2',3'-dideoxy-3'-thiacytidine
UDP + (-)-beta-2',3'-dideoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
-
-
-
?
UTP + 1-beta-D-arabinofuranosylcytosine
UDP + 1-beta-D-arabinofuranosylcytosine 5'-phosphate
show the reaction diagram
i.e. cytarabine
-
-
?
UTP + 2',2'-difluorodeoxycytidine
UDP + 2',2'-difluorodeoxycytidine 5'-phosphate
show the reaction diagram
i.e. gemcitabine
-
-
?
UTP + 2',3'-dideoxycytidine
UDP + 2',3'-dideoxycytidine 5'-phosphate
show the reaction diagram
UTP + 2'-deoxy-3'-thiacytidine
UDP + 2'-deoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
-
-
-
?
UTP + 2'-deoxyadenosine
UDP + 2'-deoxyadenosine 5'-phosphate
show the reaction diagram
UTP + 2'-deoxycytidine
UDP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
UTP + 2'-deoxyguanosine
UDP + 2'-deoxyguanosine 5'-phosphate
show the reaction diagram
UTP + 2-chloro-2'-deoxyadenosine
UDP + 2-chloro-2'-deoxyadenosine 5'-phosphate
show the reaction diagram
i.e. cladribine
-
-
?
UTP + 2-chlorodeoxyadenosine
UDP + 2-chlorodeoxyadenosine 5'-phosphate
show the reaction diagram
i.e. cladribine
-
-
?
UTP + 2-fluoro-9-beta-D-arabinofuranosyladenine
UDP + 2-fluoro-9-beta-D-arabinofuranosyladenine 5'-phosphate
show the reaction diagram
i.e. fludarabine
-
-
?
UTP + 9-beta-D-arabinofuranosylguanine
UDP + 9-beta-D-arabinofuranosylguanine 5'-phosphate
show the reaction diagram
i.e. nelarabine
-
-
?
UTP + arabinosyl adenine
UDP + arabinosyl adenine 5'-phosphate
show the reaction diagram
-
-
-
?
UTP + arabinosyl cytosine
UDP + arabinosyl cytosine 5'-phosphate
show the reaction diagram
i.e. cytosar
-
-
?
UTP + beta-L-2',3'-dideoxy-3'-thiacytidine
UDP + beta-L-2',3'-dideoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
-
-
-
?
UTP + beta-L-dioxolane-cytidine
UDP + beta-L-dioxolane-cytidine 5'-phosphate
show the reaction diagram
antitumor drug
-
-
?
UTP + D-2'-deoxycytidine
UDP + D-2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
?
UTP + deoxyadenosine
UDP + dAMP
show the reaction diagram
UTP + deoxycytidine
UDP + dCMP
show the reaction diagram
UTP + deoxyguanosine
UDP + dGMP
show the reaction diagram
UTP + difluoro-arabinofuranosyl adenine
UDP + difluoro-arabinofuranosyl adenine 5'-phosphate
show the reaction diagram
i.e. fludarabine
-
-
?
UTP + difluorodeoxycytidine
UDP + difluorodeoxycytidine 5'-phosphate
show the reaction diagram
i.e. gemcitabine
-
-
?
UTP + fludarabine
UDP + fludarabine 5'-phosphate
show the reaction diagram
13% conversion
-
-
?
UTP + L-2'-deoxycytidine
UDP + L-2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
?
UTP + troxacitabine
UDP + troxacitabine 5'-phosphate
show the reaction diagram
-
-
-
?
2',2'-difluoro-2'-deoxyguanosine + ATP
ADP + 2',2'-difluoro-2'-deoxyguanosine 5'-phosphate
show the reaction diagram
-
-
-
-
?
2'-fluoro-2'-deoxyarabinosylcytidine + ATP
ADP + 2'-fluoro-2'-deoxyarabinosylcytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
2'-fluoro-2'-deoxycytidine + ATP
ADP + 2'-fluoro-2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
2'-O-methyl-cytidine + ATP
ADP + 2'-O-methyl-cytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
2-chloro-2'-deoxyadenosine + NTP
NDP + 2-chloro-2'-deoxy-AMP
show the reaction diagram
-
-
-
-
?
3'-O-methyl-2'-deoxycytidine + ATP
ADP + 3'-O-methyl-2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
4'-thio-2'-deoxycytidine + UTP
UDP + 4'-thio-2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
4'-thio-beta-D-arabinofuranosylcytosine + UTP
UDP + 4'-thio-beta-D-arabinofuranosylcytosine 5'-phosphate
show the reaction diagram
-
-
-
-
?
9-(beta-D-arabinofuranosyl)-adenine + ATP
9-(beta-D-arabinofuranosyl)-adenine 5'-phosphate + ADP
show the reaction diagram
-
-
-
-
?
9-beta-D-arabinofuranosylguanine + NTP
NDP + 9-beta-D-arabinofuranosylguanine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + (-)-beta-2',3'-dideoxy-3'-thiacytidine
ADP + (-)-beta-2',3'-dideoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
i.e. lamivudine
-
-
?
ATP + 1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)cytosine
ADP + 1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)cytosine monophosphate
show the reaction diagram
-
-
-
-
?
ATP + 1-(2'-deoxy-2'-fluoro-beta-L-arabinofuranosyl)-5-bromocytosine
ADP + 1-(2'-deoxy-2'-fluoro-beta-L-arabinofuranosyl)-5-bromocytosine monophosphate
show the reaction diagram
-
-
-
-
?
ATP + 1-(2'-deoxy-2'-fluoro-beta-L-arabinofuranosyl)-5-chlorocytosine
ADP + 1-(2'-deoxy-2'-fluoro-beta-L-arabinofuranosyl)-5-chlorocytosine monophosphate
show the reaction diagram
-
-
-
-
?
ATP + 1-(2'-deoxy-2'-fluoro-beta-L-arabinofuranosyl)-5-methylcytosine
ADP + 1-(2'-deoxy-2'-fluoro-beta-L-arabinofuranosyl)-5-methylcytosine monophosphate
show the reaction diagram
-
-
-
-
?
ATP + 1-(2-deoxy-beta-D-ribofuranosyl)-isocarbostyril
ADP + ?
show the reaction diagram
-
poor substrate, 1.4% of the activity with 2'-deoxycytidine
-
-
?
ATP + 1-beta-D-arabinosylcytosine
ADP + 1-beta-D-arabinosylcytosine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2',2'-difluoro-2'-deoxycytidine
ADP + 2',2'-difluoro-2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
i.e. gemcitabine
-
-
?
ATP + 2',2'-difluorodeoxycytidine
ADP + 2',2'-difluorodeoxycytidine 5'-phosphate
show the reaction diagram
-
i.e. gemcitabine
-
-
?
ATP + 2',2'-difluorodeoxycytidine
ADP + 2',2'-difluorodeoxycytidine monophosphate
show the reaction diagram
ATP + 2'-deoxyadenosine
ADP + 2'-deoxyadenosine 5'-phosphate
show the reaction diagram
ATP + 2'-deoxycytidine
ADP + 2'-deoxy-CMP
show the reaction diagram
-
-
-
-
?
ATP + 2'-deoxycytidine
ADP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
ATP + 2'-deoxycytidine
ADP + 5'-dCMP
show the reaction diagram
ATP + 2'-deoxyguanosine
ADP + 2'-deoxyguanosine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2,5-difluoro-4-[1-(2-deoxy-beta-L-ribofuranosyl)]-aniline
ADP + ?
show the reaction diagram
-
nucleoside mimic, 14.6% of the activity with 2'-deoxycytidine
-
-
?
ATP + 2-chloro-2'-deoxyadenosine
ADP + 2-chloro-2'-deoxyadenosine 5'-phosphate
show the reaction diagram
ATP + 2-chlorodeoxyadenosine
ADP + 2-chlorodeoxyadenosine 5'-phosphate
show the reaction diagram
-
i.e. cladribine
-
-
?
ATP + 5-(3-pyridyl)-2'-deoxycytidine
ADP + 5-(3-pyridyl)-2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
cytosolic enzyme, poor substrate
-
-
?
ATP + 5-(4-pyridyl)-2'-deoxycytidine
ADP + 5-(4-pyridyl)-2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
cytosolic enzyme, poor substrate
-
-
?
ATP + adenosine
ADP + adenosine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + arabinosyl cytosine
ADP + arabinosyl cytosine 5'-phosphate
show the reaction diagram
-
i.e. cytosar
-
-
?
ATP + cladribine
ADP + cladribine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + clofarabine
ADP + clofarabine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + cytarabine
ADP + cytarabine 5'-phosphate
show the reaction diagram
ATP + cytidine
ADP + ?
show the reaction diagram
-
-
-
-
?
ATP + cytidine
ADP + cytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + deoxyadenosine
ADP + dAMP
show the reaction diagram
-
-
-
-
?
ATP + deoxycytidine
ADP + ?
show the reaction diagram
ATP + deoxycytidine
ADP + dCMP
show the reaction diagram
-
-
-
-
?
ATP + deoxyguanosine
ADP + dGMP
show the reaction diagram
-
-
-
-
?
ATP + fludarabine
ADP + fludarabine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + gemcitabine
ADP + gemcitabine 5'-phosphate
show the reaction diagram
ATP + L-2',3'-dideoxy-3'-thiacytidine
ADP + L-2',3'-dideoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + lamivudine
ADP + lamivudine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + thymidine
ADP + TMP
show the reaction diagram
-
cytosolic enzyme, poor substrate
-
-
?
ATP + troxacitabine
ADP + troxacitabine 5'-phosphate
show the reaction diagram
-
-
-
?
beta-D-3'-hydroxymethyl-2',3'dideoxycytidine + ATP
ADP + beta-D-3'-hydroxymethyl-2',3'dideoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
CTP + 2'-deoxycytidine
CDP + 2'-deoxy-CMP
show the reaction diagram
dGTP + 2'-deoxycytidine
dGDP + 2'-deoxy-CMP
show the reaction diagram
dTTP + 2'-deoxycytidine
dTDP + 2'-deoxy-CMP
show the reaction diagram
-
-
-
-
?
dUTP + 2'-deoxycytidine
dUDP + 2'-deoxy-CMP
show the reaction diagram
-
best phosphate donor, cytosolic enzyme I, poor, mitochondrial isozyme
-
-
?
GTP + 2'-deoxycytidine
GDP + 2'-deoxy-CMP
show the reaction diagram
NTP + (-)-beta-2',3'-dideoxy-3'-thiacytidine
NDP + (-)-beta-2',3'-dideoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
activation of the clinically relevant substrate
-
-
?
NTP + 1-beta-D-arabinofuranosylcytosine
NDP + 1-beta-D-arabinofuranosylcytosine 5'-phosphate
show the reaction diagram
i.e. cytarabine, rate limiting enzyme in the activation of the prodrug
-
-
?
NTP + 2',2'-difluoro-2'-deoxycytidine
NDP + 2',2'-difluoro-2'-deoxycytidine 5'-phosphate
show the reaction diagram
NTP + 2',2'-difluorodeoxycytidine
NDP + 2',2'-difluorodeoxycytidine 5'-phosphate
show the reaction diagram
NTP + 2',3'-dideoxycytidine
NDP + 2',3'-dideoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
NTP + 2'-deoxycytidine
NDP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
NTP + 2-chloro-2'-deoxyadenosine
NDP + 2-chloro-2'-deoxyadenosine 5'-phosphate
show the reaction diagram
NTP + 9-beta-D-arabinofuranosyl-2-fluoroadenine
NDP + 9-beta-D-arabinofuranosyl-2-fluoroadenine 5'-phosphate
show the reaction diagram
-
-
-
-
?
NTP + 9-beta-D-arabinosyl 2-fluoroadenine
NDP + 9-beta-D-arabinosyl 2-fluoroadenine 5'-phosphate
show the reaction diagram
-
activation of the pharmaceutically relevant substrate which is commonly used in the treatment of lymphoproliferative malignancies
-
-
?
NTP + 9-beta-D-arabinosyl-2-fluoroadenine
NDP + 9-beta-D-arabinosyl-2-fluoroadenine 5'-phosphate
show the reaction diagram
-
phosphorylation of chemotherapeutically important nucleoside analogues
-
-
?
NTP + clofarabine
NDP + clofarabine 5'-phosphate
show the reaction diagram
-
-
-
-
?
NTP + cytarabine
?
show the reaction diagram
-
-
-
-
?
NTP + cytosine arabinoside
NDP + cytosine arabinoside 5'-monophosphate
show the reaction diagram
NTP + deoxyadenosine
NDP + dAMP
show the reaction diagram
NTP + deoxycytidine
NDP + dCMP
show the reaction diagram
NTP + deoxyguanosine
NDP + dGMP
show the reaction diagram
NTP + deoxythymidine
NDP + dTMP
show the reaction diagram
-
mitochondrial isozyme, better than deoxycytidine, not cytosolic isozyme I
-
-
?
NTP + deoxyuridine
NDP + dUMP
show the reaction diagram
NTP + gemcitabine
?
show the reaction diagram
-
-
-
-
?
NTP + troxacitabine
?
show the reaction diagram
activation of the clinically relevant substrate
-
-
?
UTP + (-)-beta-2',3'-dideoxy-3'-thiacytidine
UDP + (-)-beta-2',3'-dideoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
-
-
-
?
UTP + 2',3'-dideoxycytidine
UDP + 2',3'-dideoxycytidine 5'-phosphate
show the reaction diagram
-
i.e. zalcitabine, activation of the pharmaceutically relevant substrate which is used for the treatment of HIV infections
-
-
?
UTP + 2'-deoxy-3'-thiacytidine
UDP + 2'-deoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
-
i.e. lamivudine, activation of the pharmaceutically relevant substrate which is used for the treatment of HIV infections
-
-
?
UTP + 2'-deoxyadenosine
UDP + 2'-deoxyadenosine 5'-phosphate
show the reaction diagram
UTP + 2'-deoxycytidine
UDP + 2'-deoxy-CMP
show the reaction diagram
UTP + 2'-deoxycytidine
UDP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
UTP + 2'-deoxyguanosine
UDP + 2'-deoxyguanosine 5'-phosphate
show the reaction diagram
-
-
-
-
?
UTP + adenosine
UDP + adenosine 5'-phosphate
show the reaction diagram
-
-
-
-
?
UTP + arabinosyl cytosine
UDP + arabinosyl cytosine 5'-phosphate
show the reaction diagram
-
i.e. cytosar
-
-
?
UTP + cladribine
UDP + cladribine 5'-phosphate
show the reaction diagram
-
-
-
-
?
UTP + clofarabine
UDP + clofarabine 5'-phosphate
show the reaction diagram
-
-
-
-
?
UTP + cytidine
UDP + cytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
UTP + deoxyadenosine
UDP + dAMP
show the reaction diagram
-
-
-
-
?
UTP + deoxycytidine
UDP + dCMP
show the reaction diagram
UTP + deoxyguanosine
UDP + dGMP
show the reaction diagram
-
-
-
-
?
UTP + fludarabine
UDP + fludarabine 5'-phosphate
show the reaction diagram
-
-
-
-
?
UTP + fludarabine
UDP + phospho-fludarabine
show the reaction diagram
-
-
-
-
?
UTP + gemcitabine
UDP + gemcitabine 5'-phosphate
show the reaction diagram
-
-
-
-
?
UTP + L-2',3'-dideoxy-3'-thiacytidine
UDP + L-2',3'-dideoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
-
-
-
-
?
UTP + troxacitabine
UDP + troxacitabine 5'-phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 2'-deoxyadenosine
ADP + 2'-deoxyadenosine 5'-phosphate
show the reaction diagram
ATP + 2'-deoxycytidine
ADP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
ATP + 2'-deoxyguanosine
ADP + 2'-deoxyguanosine 5'-phosphate
show the reaction diagram
ATP + 5-methyldeoxycytidine
ADP + 5-methyl-dCMP
show the reaction diagram
-
-
-
?
ATP + deoxyadenosine
ADP + dAMP
show the reaction diagram
-
-
-
?
ATP + deoxycytidine
ADP + dCMP
show the reaction diagram
ATP + deoxyguanosine
ADP + dGMP
show the reaction diagram
-
-
-
?
ATP + L-thymidine
?
show the reaction diagram
human dCK, in addition to being able to phosphorylate both purines and pyrimidines, has the special ability to accept L-nucleosides as substrates
-
-
?
NTP + 1-beta-D-arabinofuranosylcytosine
NDP + 1-beta-D-arabinofuranosylcytosine 5'-phosphate
show the reaction diagram
antineoplastic agent
-
-
?
NTP + 1-beta-D-arabinosylcytosine
NDP + 1-beta-D-arabinosylcytosine 5'-phosphate
show the reaction diagram
i.e. cytaribine, activation of the pharmaceutically relevant substrate which is commonly used in the treatment of lymphoproliferative malignancies
-
-
?
NTP + 2',2'-difluorodeoxycytidine
NDP + 2',2'-difluorodeoxycytidine 5'-phosphate
show the reaction diagram
i.e. gemcitabine, activation of the pharmaceutically relevant substrate which is commonly used in the treatment of solid malignant tumors
-
-
?
NTP + 2',3'-dideoxycytidine
NDP + 2',3'-dideoxycytidine 5'-phosphate
show the reaction diagram
NTP + 2'-deoxy-3'-thiacytidine
NDP + 2'-deoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
NTP + 2'-deoxyadenosine
NDP + 2'-deoxyadenosine 5'-phosphate
show the reaction diagram
NTP + 2'-deoxycytidine
NDP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
NTP + 2'-deoxyguanosine
NDP + 2'-deoxyguanosine 5'-phosphate
show the reaction diagram
NTP + 2-chloro-2'-deoxyadenosine
NDP + 2-chloro-2'-deoxyadenosine 5'-phosphate
show the reaction diagram
NTP + 2-chloro-9-(2-deoxy-2-fluoro-beta-D-arabinofuranosyl)-9H-purin-6-amine
NDP + 2-chloro-9-(2-deoxy-2-fluoro-beta-D-arabinofuranosyl)-9H-purin-6-amine 5'-phosphate
show the reaction diagram
i.e. clofarabine, rate-limiting step in the activation of the prodrug, precursor of an effective chemotherapeutic agent for leukemias and other haematological malignancies
-
-
?
NTP + 9-beta-D-arabinosyl 2-fluoroadenine
NDP + 9-beta-D-arabinosyl 2-fluoroadenine 5'-phosphate
show the reaction diagram
i.e. fludarabine, activation of the pharmaceutically relevant substrate which is commonly used in the treatment of lymphoproliferative malignancies
-
-
?
NTP + deoxycytidine
NDP + dCMP
show the reaction diagram
-
-
-
?
UTP + 2'-deoxyadenosine
UDP + 2'-deoxyadenosine 5'-phosphate
show the reaction diagram
UTP + 2'-deoxycytidine
UDP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
UTP + 2'-deoxyguanosine
UDP + 2'-deoxyguanosine 5'-phosphate
show the reaction diagram
UTP + deoxyadenosine
UDP + dAMP
show the reaction diagram
-
-
-
?
UTP + deoxycytidine
UDP + dCMP
show the reaction diagram
UTP + deoxyguanosine
UDP + dGMP
show the reaction diagram
-
-
-
?
ATP + 2',2'-difluorodeoxycytidine
ADP + 2',2'-difluorodeoxycytidine monophosphate
show the reaction diagram
-
i.e. gemcitabine, transport and metabolism in vivo, overview
-
-
?
ATP + 2'-deoxyadenosine
ADP + 2'-deoxyadenosine 5'-phosphate
show the reaction diagram
ATP + 2'-deoxycytidine
ADP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
ATP + 2'-deoxyguanosine
ADP + 2'-deoxyguanosine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 2-chlorodeoxyadenosine
ADP + 2-chlorodeoxyadenosine 5'-phosphate
show the reaction diagram
-
i.e. cladribine
-
-
?
ATP + cladribine
ADP + cladribine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + clofarabine
ADP + clofarabine 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + cytarabine
ADP + cytarabine 5'-phosphate
show the reaction diagram
-
drug against acute myeloid and lymphoblastic leukemia
-
-
?
ATP + deoxyadenosine
ADP + dAMP
show the reaction diagram
-
-
-
-
?
ATP + deoxycytidine
ADP + ?
show the reaction diagram
ATP + deoxycytidine
ADP + dCMP
show the reaction diagram
-
-
-
-
?
ATP + deoxyguanosine
ADP + dGMP
show the reaction diagram
-
-
-
-
?
ATP + fludarabine
ADP + fludarabine 5'-phosphate
show the reaction diagram
-
-
-
-
?
NTP + (-)-beta-2',3'-dideoxy-3'-thiacytidine
NDP + (-)-beta-2',3'-dideoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
activation of the clinically relevant substrate
-
-
?
NTP + 1-beta-D-arabinofuranosylcytosine
NDP + 1-beta-D-arabinofuranosylcytosine 5'-phosphate
show the reaction diagram
i.e. cytarabine, rate limiting enzyme in the activation of the prodrug
-
-
?
NTP + 2',2'-difluorodeoxycytidine
NDP + 2',2'-difluorodeoxycytidine 5'-phosphate
show the reaction diagram
NTP + 2-chloro-2'-deoxyadenosine
NDP + 2-chloro-2'-deoxyadenosine 5'-phosphate
show the reaction diagram
NTP + 9-beta-D-arabinosyl 2-fluoroadenine
NDP + 9-beta-D-arabinosyl 2-fluoroadenine 5'-phosphate
show the reaction diagram
-
activation of the pharmaceutically relevant substrate which is commonly used in the treatment of lymphoproliferative malignancies
-
-
?
NTP + 9-beta-D-arabinosyl-2-fluoroadenine
NDP + 9-beta-D-arabinosyl-2-fluoroadenine 5'-phosphate
show the reaction diagram
-
phosphorylation of chemotherapeutically important nucleoside analogues
-
-
?
NTP + deoxycytidine
NDP + dCMP
show the reaction diagram
-
-
-
-
?
NTP + troxacitabine
?
show the reaction diagram
activation of the clinically relevant substrate
-
-
?
UTP + 2',3'-dideoxycytidine
UDP + 2',3'-dideoxycytidine 5'-phosphate
show the reaction diagram
-
i.e. zalcitabine, activation of the pharmaceutically relevant substrate which is used for the treatment of HIV infections
-
-
?
UTP + 2'-deoxy-3'-thiacytidine
UDP + 2'-deoxy-3'-thiacytidine 5'-phosphate
show the reaction diagram
-
i.e. lamivudine, activation of the pharmaceutically relevant substrate which is used for the treatment of HIV infections
-
-
?
UTP + 2'-deoxyadenosine
UDP + 2'-deoxyadenosine 5'-phosphate
show the reaction diagram
UTP + 2'-deoxycytidine
UDP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
UTP + 2'-deoxyguanosine
UDP + 2'-deoxyguanosine 5'-phosphate
show the reaction diagram
-
-
-
-
?
UTP + cladribine
UDP + cladribine 5'-phosphate
show the reaction diagram
-
-
-
-
?
UTP + clofarabine
UDP + clofarabine 5'-phosphate
show the reaction diagram
-
-
-
-
?
UTP + deoxyadenosine
UDP + dAMP
show the reaction diagram
-
-
-
-
?
UTP + deoxycytidine
UDP + dCMP
show the reaction diagram
UTP + deoxyguanosine
UDP + dGMP
show the reaction diagram
-
-
-
-
?
UTP + fludarabine
UDP + phospho-fludarabine
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
enzyme lalso utilizes other nucleoside triphosphates as phosphate donors
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activation
Ni2+
-
not
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(5-(4-(((4,6-diaminopyrimidin-2-yl)thio)methyl)-5-propylthiazol-2-yl)-2-methoxyphenoxy)-2-methylpropan-2-ol
-
1-[5-(4-[[(4,6-diaminopyrimidin-2-yl)sulfanyl]methyl]-5-propyl-1,3-thiazol-2-yl)-2-methoxyphenoxy]propan-2-ol
-
2,2'-[[4-(4-[[(4,6-diaminopyrimidin-2-yl)sulfanyl]methyl]-5-propyl-1,3-thiazol-2-yl)-1,2-phenylene]bis(oxy)]di(ethan-1-ol)
-
2-(((2-(3-(2-fluoroethoxy)-4-methoxyphenyl)-5-methylthiazol-4-yl)methyl)thio)pyrimidine-4,6-diamine
-
2-(((2-(3-(2-fluoroethoxy)-4-methoxyphenyl)-5-propylthiazol-4-yl)methyl)thio)pyrimidine-4,6-diamine
-
2-([[2-(3,5-difluorophenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
-
2-([[2-(3-fluorophenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
-
2-([[2-(3-methoxyphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
-
2-([[2-(4-ethoxy-3-methoxyphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
-
2-([[2-(4-fluorophenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
-
2-([[2-(4-methoxyphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine
-
2-([[2-(4-methoxyphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
-
2-([[2-(4-methylphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
-
2-([[2-(5-bromo-2-methoxyphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
-
2-[(2[-[3-(2-fluoroethoxy)-4-methoxyphenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[([2-[3-(2-fluoroethoxy)-4-(fluoromethoxy)phenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[([2-[3-(2-fluoroethoxy)-4-methoxyphenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[([2-[3-(2-fluoroethoxy)-4-methoxyphenyl]-5-methyl-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[([2-[3-(2-fluoroethoxy)-4-methoxyphenyl]-5-propyl-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[([2-[3-(2-fluoroethoxy)-4-methylphenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[([2-[3-(3-fluoropropoxy)-4-methoxyphenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[([2-[4-(2-fluoroethoxy)-2-methoxyphenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[([2-[4-(2-fluoroethoxy)-3-methoxyphenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[([2-[4-ethoxy-3-(2-fluoroethoxy)phenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[([2-[5-(2-fluoroethoxy)-2-methoxyphenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[([5-ethyl-2-[3-(2-fluoroethoxy)-4-methoxyphenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
-
2-[3-(4-[[(4,6-diaminopyrimidin-2-yl)sulfanyl]methyl]-5-propyl-1,3-thiazol-2-yl)-5-fluorophenoxy]ethan-1-ol
-
2-[3-(4-[[(4,6-diaminopyrimidin-2-yl)sulfanyl]methyl]-5-propyl-1,3-thiazol-2-yl)phenoxy]ethan-1-ol
-
2-[5-(4-[[(4,6-diaminopyrimidin-2-yl)sulfanyl]methyl]-5-propyl-1,3-thiazol-2-yl)-2-fluorophenoxy]ethan-1-ol
-
2-[5-(4-[[(4,6-diaminopyrimidin-2-yl)sulfanyl]methyl]-5-propyl-1,3-thiazol-2-yl)-2-methoxyphenoxy]ethan-1-ol
-
2-[5-(4-[[(4-aminopyrimidin-2-yl)sulfanyl]methyl]-5-propyl-1,3-thiazol-2-yl)-2-methoxyphenoxy]ethan-1-ol
-
2-[[(2-phenyl-1,3-thiazol-4-yl)methyl]sulfanyl]pyrimidine
-
3'-[[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]sulfamoyl]biphenyl-4-carboxamide
-
3-[5-(4-[[(4,6-diaminopyrimidin-2-yl)sulfanyl]methyl]-5-propyl-1,3-thiazol-2-yl)-2-methoxyphenoxy]propan-1-ol
-
4-(1-benzothiophen-2-yl)-6-[4-(2-oxo-2-pyrrolidin-1-ylethyl)piperazin-1-yl]pyrimidine
-
5-(4-[[(4,6-diaminopyrimidin-2-yl)sulfanyl]methyl]-5-propyl-1,3-thiazol-2-yl)-2-methoxyphenol
-
5-Fluoro-2'-deoxycytidine
competitive inhibitor
dCTP
feedback inhibition, competitive versus phosphate donors
lambda protein phosphatase
-
-
N-(2-(5-(4-(((4,6-diaminopyrimidin-2-yl)thio)methyl)-5-propylthiazol-2-yl)-2-methoxyphenoxy)ethyl)methanesulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-2',4'-dichlorobiphenyl-3-sulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-2'-chlorobiphenyl-3-sulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-3'-chlorobiphenyl-3-carboxamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-3'-chlorobiphenyl-3-sulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-3-bromobenzenesulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4''-chloro-2''-methyl-1,1':4',1''-terphenyl-3-carboxamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4''-chloro-2''-methyl-1,1':4',1''-terphenyl-3-sulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-(methylsulfonyl)biphenyl-3-sulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-chlorobiphenyl-3-sulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-cyanobiphenyl-3-sulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-formylbiphenyl-3-sulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-methoxybiphenyl-3-carboxamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-methoxybiphenyl-3-sulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-methylbiphenyl-3-sulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4-(1-benzothiophen-2-yl)pyridine-2-carboxamide
potent, selective, and orally bioavailable inhibitor of dCK
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4-bromobenzenesulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4-nitrobenzenesulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]benzenesulfonamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]biphenyl-3-carboxamide
-
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]biphenyl-3-sulfonamide
-
N-[2-[3-(4-[[(4,6-diaminopyrimidin-2-yl)sulfanyl]methyl]-5-propyl-1,3-thiazol-2-yl)-5-fluorophenoxy]ethyl]methanesulfonamide
-
N-[2-[3-(4-[[(4,6-diaminopyrimidin-2-yl)sulfanyl]methyl]-5-propyl-1,3-thiazol-2-yl)phenoxy]ethyl]methanesulfonamide
-
2'-deoxycytidine
-
-
2'-O-methylcytidine
-
-
2-chloroadenosine
-
-
3'-O-methyl-2'deoxycytidine
-
-
4'-thio-beta-D-arabinofuranosylcytosine
-
IC50 0.000024 mM
5'-O-ethyl-2'-deoxycytidine
-
-
5'-O-methyl-2'-deoxycytidine
-
-
5-chloro-4'-thio-beta-D-arabinofuranosylcytosine
-
IC50 0.051 mM
5-fluoro-4'-thio-beta-D-arabinofuranosylcytosine
-
IC50 0.0000020 mM
adenosine arabinoside
-
weak, not with deoxyadenosine as substrate
ADP
-
kinetics
Ba2+
-
-
Cu2+
-
-
cytidine
cytosine arabinoside
Cytosine arabinoside monophosphate
-
strong
Cytosine arabinoside triphosphate
dAMP
-
strong
dATP
-
strong
dCDP
-
-
deoxyadenosine
deoxycytidine
deoxyguanosine
deoxythymidine
-
weak
dGDP
-
not
dGMP
-
strong
dGTP
-
ATP as substrate
Dideoxyadenosine
-
-
Dideoxycytidine
-
-
dUMP
-
strong
dUTP
-
-
H-7
-
reduces the enzyme activation caused by the addition of 2-chloro-2’-deoxyadenosine
HgCl2
-
-
LP-375752
-
i.e. 2-[4-(6-benzo[b]thiophen-2-yl-pyrimidin-4-yl)-piperazin-1-yl]-1-pyrrolidin-1-yl-ethanone
LP-503392
-
i.e. 2-thio-2'-deoxycytidine
NaCl
-
at 0.2-0.4 M, stimulation of 2’-deoxycytidine and 2-chlorodeoxyadenosine phosphorylation, but inhibition of 2’-deoxyguanosine phosphorylation
Nucleosides
P1,P4-diadenosine 5'-tetraphosphate
-
not di-, tri- or pentaphosphate derivative
protein phosphatase lambda
-
-
-
Sodium diphosphate
-
not monophosphate
sorbitol
-
-
staurosporine
-
reduces the enzyme activation caused by the addition of 2-chloro-2’-deoxyadenosine
suramin
-
no effect in unirradiated cells, complete abolishment of UV-C light induced activation
UMP
-
strong
Uridine arabinoside
-
weak, cytosolic isozyme I
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-beta-D-arabinosylcytosine
-
i.e. cytarabine, 0.001 mM, stimulation
2'-deoxyadenosine/deoxycoformycin
-
no stimulation of enzyme activity by either compound if applied alone, with both compound at 0.01 mM 2.4fold activation occurs
2'-deoxythymidine-5'-thiosulphate
-
in intact cells, activation, reversed by 2’-deoxycytidine
2-chloro-2'-arabino-fluoro-2'-deoxyadenosine
-
0.001 mM, stimulation
2-chloro-2'-deoxy-2'-fluoro-arabinosyladenine
-
stimulation
2-chloro-2'-deoxyadenosine
2-fluoro-1-beta-D-arabinosyladenine
-
i.e. fludarabine, 0.001 mM, stimulation
AG-490
-
-
aphidicolin
arabinosylcytidine
-
stimulation
ATP
-
substrate activation, at high concentrations of deoxycytidine
calyculin A
-
inhibitor of protein phosphatases, activation
CHAPS
-
slight stimulation, deoxycytidine as substrate
daidzein
-
-
deoxyadenosine
-
activation, deoxycytidine as substrate, mitochondrial isozyme
deoxyguanosine
-
activation, deoxycytidine as substrate, mitochondrial isozyme
dithiothreitol
-
activation
etoposide
gamma-radiation
-
0.5-2 GY dosage, activation
-
genistein
NaCl
-
at 0.2-0.4 M, stimulation of 2’-deoxycytidine and 2-chlorodeoxyadenosine phosphorylation, but inhibition of 2’-deoxyguanosine phosphorylation
NaF
-
15 mM, 1 h, activity about twice as high as initial level
okadaic acid
-
-
paclitaxel
-
paclitaxel increases dCK (10% to 50%) activity
PD 153035
-
i.e. 4-(3-bromoanilino)-6,7-dimethoxy-quinazinoline
PD 98059
-
i.e. 2'-amino-3'-methoxyflavone, in absence of deoxycytidine
PD-98059
-
-
protein transporter ABCG2
-
the ABC transporter activates the enzyme and reduces intracellular accumulation of clofarabine
-
SB 203580
-
in absence of deoxycytidine
sodium cholate
-
slight stimulation, deoxycytidine as substrate
TTP
-
stimulation, cytosolic isozyme I
tyrphostin A47
-
-
UDP
-
stimulation, mitochondrial isozyme
Uridine arabinoside
-
activation, deoxycytidine as substrate, mitochondrial isozyme
Zwittergent 3-14
-
slight stimulation, deoxycytidine as substrate
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.024
1-beta-D-arabinofuranosylcytosine
0.0131 - 0.1365
1-beta-D-arabinosylcytosine
0.0062 - 0.015
2',2'-difluorodeoxycytidine
0.0085 - 1.437
2'-deoxyadenosine
0.00016 - 0.0089
2'-deoxycytidine
0.021 - 2.266
2'-deoxyguanosine
0.0051 - 0.078
2-chlorodeoxyadenosine
0.0029 - 0.097
ATP
0.0243 - 0.144
D-thymidine
0.001 - 0.071
deoxycytidine
0.0161 - 0.0562
gemcitabine
0.0178 - 0.138
L-thymidine
0.00388 - 3.485
thymidine
0.0015 - 0.0578
UTP
0.003 - 0.015
(-)-beta-2',3'-dideoxy-3'-thiacytidine
0.00076
1-(2'-deoxy-2'-fluoro-beta-D-arabinofuranosyl)cytosine
-
pH 7.6, 37°C, recombinant enzyme
0.00654
1-(2'-deoxy-2'-fluoro-beta-L-arabinofuranosyl)-5-bromocytosine
-
pH 7.6, 37°C, recombinant enzyme
0.00061
1-(2'-deoxy-2'-fluoro-beta-L-arabinofuranosyl)-5-chlorocytosine
-
pH 7.6, 37°C, recombinant enzyme
0.00102
1-(2'-deoxy-2'-fluoro-beta-L-arabinofuranosyl)-5-methylcytosine
-
pH 7.6, 37°C, recombinant enzyme
0.15 - 0.23
2',3'-dideoxycytidine
0.019 - 0.48
2'-deoxyadenosine
0.00005 - 0.001
2'-deoxycytidine
0.0013
2,5-difluoro-4-[1-(2-deoxy-beta-L-ribofuranosyl)]-aniline
-
pH 7.6, 37°C, recombinant enzyme
0.00099 - 0.024
2-chloro-2'-deoxyadenosine
0.00032
4'-thio-2'-deoxycytidine
-
cosubstrate ATP 37°C, pH 8.0
0.02 - 0.088
4'-thio-beta-D-arabinofuranosylcytosine
2 - 3
9-beta-D-arabinofuranosylguanine
0.001
ATP
-
cosubstrate 2'-deoxycytidine, 37°C, pH 7.4
0.00041 - 0.015
beta-D-arabinofuranosylcytosine
0.00065 - 0.0155
cladribine
0.0087 - 0.0325
clofarabine
0.0013
CTP
-
cosubstrate 2'-deoxycytidine, 37°C, pH 7.4
0.0282
cytarabine
-
wild type enzyme, pH and temperature not specified in the publication
0.45
cytidine
-
37°C, pH 7.0
0.002 - 0.04
cytosine arabinoside
0.12 - 0.89
deoxyadenosine
0.00007 - 0.0167
deoxycytidine
0.15 - 0.64
deoxyguanosine
0.001
dTTP
-
cosubstrate 2'-deoxycytidine, 37°C, pH 7.4
0.028 - 0.551
fludarabine
0.0467
gemcitabine
-
wild type enzyme, pH and temperature not specified in the publication
0.0009
GTP
-
cosubstrate 2'-deoxycytidine, 37°C, pH 7.4
0.011 - 0.058
troxacitabine
0.0005
UTP
-
cosubstrate 2'-deoxycytidine, 37°C, pH 7.4
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 1.06
1-beta-D-arabinofuranosylcytosine
0.34 - 1.43
1-beta-D-arabinosylcytosine
0.44 - 1.21
2',2'-difluorodeoxycytidine
0.31 - 5.72
2'-deoxyadenosine
0.033 - 1.8
2'-deoxycytidine
0.31 - 4.38
2'-deoxyguanosine
0.37 - 0.6
2-chlorodeoxyadenosine
0.012 - 0.4
ATP
1.74 - 3.2
D-thymidine
0.064 - 3.54
deoxycytidine
0.39 - 2.68
gemcitabine
1.33 - 3.13
L-thymidine
0.38 - 3.29
thymidine
0.01 - 0.524
UTP
0.028 - 0.102
(-)-beta-2',3'-dideoxy-3'-thiacytidine
0.11
2'-deoxycytidine
-
pH 7.6, 37°C, recombinant enzyme
0.02
2,5-difluoro-4-[1-(2-deoxy-beta-L-ribofuranosyl)]-aniline
-
pH 7.6, 37°C, recombinant enzyme
0.0804 - 1.386
cladribine
0.486 - 2.45
clofarabine
0.38
cytarabine
-
wild type enzyme, pH and temperature not specified in the publication
0.015 - 0.183
deoxycytidine
0.177 - 1.334
fludarabine
0.57
gemcitabine
-
wild type enzyme, pH and temperature not specified in the publication
0.095 - 0.524
troxacitabine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.5 - 26
1-beta-D-arabinosylcytosine
4.3 - 35.2
2'-deoxyadenosine
13.3 - 315.8
2'-deoxycytidine
0.9 - 11.3
2'-deoxyguanosine
12.1 - 131.7
D-thymidine
24.2 - 59.5
gemcitabine
22.7 - 74.7
L-thymidine
74.3 - 136
cladribine
50.1 - 76.8
clofarabine
13.48
cytarabine
-
wild type enzyme, pH and temperature not specified in the publication
6.46 - 745
deoxycytidine
1.8 - 6.4
fludarabine
12.21
gemcitabine
-
wild type enzyme, pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000008
1-(5-(4-(((4,6-diaminopyrimidin-2-yl)thio)methyl)-5-propylthiazol-2-yl)-2-methoxyphenoxy)-2-methylpropan-2-ol
at pH 7.6 and 37°C
0.0000095
2-(((2-(3-(2-fluoroethoxy)-4-methoxyphenyl)-5-methylthiazol-4-yl)methyl)thio)pyrimidine-4,6-diamine
at pH 7.6 and 37°C
0.0000015
2-(((2-(3-(2-fluoroethoxy)-4-methoxyphenyl)-5-propylthiazol-4-yl)methyl)thio)pyrimidine-4,6-diamine
at pH 7.6 and 37°C
0.0000005
N-(2-(5-(4-(((4,6-diaminopyrimidin-2-yl)thio)methyl)-5-propylthiazol-2-yl)-2-methoxyphenoxy)ethyl)methanesulfonamide
at pH 7.6 and 37°C
0.3
2'-O-methylcytidine
-
37°C, pH 7.6
0.02
3'-O-methyl-2'deoxycytidine
-
37°C, pH 7.6
0.032
5'-O-ethyl-2'-deoxycytidine
-
37°C, pH 7.6
0.23
5'-O-methyl-2'-deoxycytidine
-
37°C, pH 7.6
0.0015 - 0.022
dCMP
0.0015 - 0.398
dCTP
0.0004 - 0.0069
UDP
additional information
additional information
-
steady-state fluorescent measurement, inhibitor binding constant, recombinant enzyme
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00167
2-([[2-(3-methoxyphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
Homo sapiens
at pH 7.6 and 37°C
0.00112
2-([[2-(4-ethoxy-3-methoxyphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
Homo sapiens
at pH 7.6 and 37°C
0.1
2-([[2-(4-methoxyphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine
Homo sapiens
IC50 above 0.1 mM, at pH 7.6 and 37°C
0.00202
2-([[2-(4-methoxyphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
Homo sapiens
at pH 7.6 and 37°C
0.00232
2-([[2-(4-methylphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
Homo sapiens
at pH 7.6 and 37°C
0.00176
2-([[2-(5-bromo-2-methoxyphenyl)-1,3-thiazol-4-yl]methyl]sulfanyl)pyrimidine-4,6-diamine
Homo sapiens
at pH 7.6 and 37°C
0.0007457
2-[(2[-[3-(2-fluoroethoxy)-4-methoxyphenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0000263
2-[([2-[3-(2-fluoroethoxy)-4-methoxyphenyl]-5-methyl-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0000167
2-[([2-[3-(2-fluoroethoxy)-4-methoxyphenyl]-5-propyl-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0000227
2-[([5-ethyl-2-[3-(2-fluoroethoxy)-4-methoxyphenyl]-1,3-thiazol-4-yl]methyl)sulfanyl]pyrimidine-4,6-diamine
Homo sapiens
pH and temperature not specified in the publication
0.1
2-[[(2-phenyl-1,3-thiazol-4-yl)methyl]sulfanyl]pyrimidine
Homo sapiens
IC50 above 0.1 mM, at pH 7.6 and 37°C
0.000089
3'-[[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]sulfamoyl]biphenyl-4-carboxamide
Homo sapiens
-
0.00051
4-(1-benzothiophen-2-yl)-6-[4-(2-oxo-2-pyrrolidin-1-ylethyl)piperazin-1-yl]pyrimidine
Homo sapiens
-
0.00012
5-Fluoro-2'-deoxycytidine
Homo sapiens
-
0.000021
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-2',4'-dichlorobiphenyl-3-sulfonamide
Homo sapiens
-
0.000045
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-2'-chlorobiphenyl-3-sulfonamide
Homo sapiens
-
0.000023
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-3'-chlorobiphenyl-3-carboxamide
Homo sapiens
-
0.000079
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-3'-chlorobiphenyl-3-sulfonamide
Homo sapiens
-
0.00035 - 0.0019
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-3-bromobenzenesulfonamide
0.000021
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4''-chloro-2''-methyl-1,1':4',1''-terphenyl-3-carboxamide
Homo sapiens
-
0.000021
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4''-chloro-2''-methyl-1,1':4',1''-terphenyl-3-sulfonamide
Homo sapiens
-
0.000063
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-(methylsulfonyl)biphenyl-3-sulfonamide
Homo sapiens
-
0.000051
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-chlorobiphenyl-3-sulfonamide
Homo sapiens
-
0.000049
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-cyanobiphenyl-3-sulfonamide
Homo sapiens
-
0.0153
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-formylbiphenyl-3-sulfonamide
Homo sapiens
-
0.00003 - 0.000042
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-methoxybiphenyl-3-carboxamide
0.000064
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-methoxybiphenyl-3-sulfonamide
Homo sapiens
-
0.00011
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4'-methylbiphenyl-3-sulfonamide
Homo sapiens
-
0.0000017
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4-(1-benzothiophen-2-yl)pyridine-2-carboxamide
Homo sapiens
-
0.0027
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4-bromobenzenesulfonamide
Homo sapiens
-
0.0032
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]-4-nitrobenzenesulfonamide
Homo sapiens
-
0.0036
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]benzenesulfonamide
Homo sapiens
-
0.00026
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]biphenyl-3-carboxamide
Homo sapiens
-
0.00012
N-[(1S,3S)-3-(4-amino-5-fluoro-2-oxopyrimidin-1(2H)-yl)cyclopentyl]biphenyl-3-sulfonamide
Homo sapiens
-
0.000024
4'-thio-beta-D-arabinofuranosylcytosine
Homo sapiens
-
IC50 0.000024 mM
0.051
5-chloro-4'-thio-beta-D-arabinofuranosylcytosine
Homo sapiens
-
IC50 0.051 mM
0.000002
5-fluoro-4'-thio-beta-D-arabinofuranosylcytosine
Homo sapiens
-
IC50 0.0000020 mM
0.0000055
cytosine arabinoside
Homo sapiens
-
IC50 0.0000055 mM
0.0138
LP-375752
Homo sapiens
-
in 50 mM Tris (pH 7.6)
0.00091
LP-503392
Homo sapiens
-
in 50 mM Tris (pH 7.6)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
108
substrate dideoxythymidine, mutant R104M/D133T, pH 7.5, 37°C
114
substrate 2'-deoxy-3'-thiacytidine, mutant R104M/D133T, pH 7.5, 37°C
135
substrate dideoxythymidine, mutant A100V/R104M/D133T, pH 7.5, 37°C
1387
substrate 1-beta-D-arabinosylcytosine, mutant R104M/D133T, pH 7.5, 37°C
149
substrate 2'-deoxy-3'-thiacytidine, mutant A100V/R104M/D133A, pH 7.5, 37°C
1648
substrate gemcitabine, wild-type, pH 7.5, 37°C
186
substrate dideoxythymidine, mutant A100V/R104M/D133S, pH 7.5, 37°C
206
substrate dideoxythymidine, mutant D47E/R104Q/D133G/N163I/F242L, pH 7.5, 37°C
2262
substrate gemcitabine, mutant A100V/R104M/D133T, pH 7.5, 37°C
26
substrate 2'-deoxy-3'-thiacytidine, mutant A100V/R104M/D133T, pH 7.5, 37°C
270
substrate 2'-deoxy-3'-thiacytidine, mutant A100V/R104M/D133S, pH 7.5, 37°C
28
substrate dideoxythymidine, mutant R104M/D133S, pH 7.5, 37°C
3177
substrate 1-beta-D-arabinosylcytosine, mutant A100V/R104M/D133S, pH 7.5, 37°C
3308
substrate 1-beta-D-arabinosylcytosine, mutant A100V/R104M/D133A, pH 7.5, 37°C
3339
substrate 1-beta-D-arabinosylcytosine, mutant R104M/D133SA, pH 7.5, 37°C
4267
substrate gemcitabine, mutant R104M/D133T, pH 7.5, 37°C
4400
substrate 1-beta-D-arabinosylcytosine, mutant D47E/R104Q/D133G/N163I/F242L, pH 7.5, 37°C
4530
substrate gemcitabine, mutant A100V/R104M/D133A, pH 7.5, 37°C
545
substrate 2'-deoxy-3'-thiacytidine, mutant R104M/D133S, pH 7.5, 37°C
5624
substrate gemcitabine, mutant R104M/D133SA, pH 7.5, 37°C
599
substrate 1-beta-D-arabinosylcytosine, mutant A100V/R104M/D133T, pH 7.5, 37°C
6.5
substrate dideoxythymidine, wild-type, pH 7.5, 37°C
6009
substrate gemcitabine, mutant A100V/R104M/D133S, pH 7.5, 37°C
64
substrate dideoxythymidine, mutant A100V/R104M/D133A, pH 7.5, 37°C
6460
substrate gemcitabine, mutant D47E/R104Q/D133G/N163I/F242L, pH 7.5, 37°C
815
substrate 2'-deoxy-3'-thiacytidine, mutant D47E/R104Q/D133G/N163I/F242L, pH 7.5, 37°C
88
substrate 2'-deoxy-3'-thiacytidine, wild-type, pH 7.5, 37°C
984
substrate 1-beta-D-arabinosylcytosine, wild-type, pH 7.5, 37°C
0.0000057
-
differentiated adipocytes
0.0000521
-
CEM lymphocytes
0.048
-
mitochondrial isozyme, pH 7.5, 37°C
0.072
-
cytoplasmic isozyme I, pH 7.5, 37°C
0.11 - 0.15
-
pH 8.0, 37°C
13.5
-
deoxyadenosine as substrate, 37°C, pH 7.0
4
-
cytidine as substrate, 37°C, pH 7.0
7.2
-
deoxyguanosine as substrate, 37°C, pH 7.0
8
-
37°C, pH 7.0
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
-
plateau, higher activity in Tris than in phosphate buffer
7
-
broad
7.4
-
assay at
8
-
aassay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 10
-
about half-maximal activity at pH 5.8 and pH 10, about 90% of maximal activity at pH 6.5 and pH 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 55
-
about half-maximal activity at 37°C and 55°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
very low enzyme expression
Manually annotated by BRENDA team
high enzyme expression
Manually annotated by BRENDA team
very low enzyme expression
Manually annotated by BRENDA team
very low enzyme expression
Manually annotated by BRENDA team
-
BT-474-JB cell line, Memorial Sloan Kettering Cancer Center
Manually annotated by BRENDA team
-
lowest specific activity among the cell lines used
Manually annotated by BRENDA team
-
proliferating lymphocyte
Manually annotated by BRENDA team
-
highest specific activity among the cell lines used
Manually annotated by BRENDA team
-
enzyme activity increases up to 3fold when cells start to proliferate
Manually annotated by BRENDA team
-
adult non-small cell lung cancer
Manually annotated by BRENDA team
-
T-lymphoblasts, cell lines MOLT 4F, CCRF, CEM and RPMI 8402, B-lymphoblasts cell lines BALL 1 and EBV (Epstein-Barr-virus) transformed B-lymphoblasts
Manually annotated by BRENDA team
-
cells irradiated in the late exponential growth phase for experiments
Manually annotated by BRENDA team
-
lymphocyte
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
only when overexpressed
Manually annotated by BRENDA team
-
Epstein-Barr-Virus
Manually annotated by BRENDA team
additional information
the enzyme possesses a nuclear import signal sequence
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCK_HUMAN
260
0
30519
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
x * 30000, SDS-PAGE
30500
2 * 30500, calculated from the deduced amino acid sequence, crystal structure analysis
34000
2 * 34000, SDS-PAGE, native mass by gel filtration
68000
gel filtration
30000
30500
-
2 * 30500, SDS-PAGE
40000
-
x * 40000, SDS-PAGE
52000
59300
-
sedimentation equilibrium determination, PAGE, both in the presence of protease inhibitors
60000
61000
-
gel filtration, glycerol gradient centrifugation
68000
-
-
70000
-
human cytoplasmic isozymes
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer
-
dimer
homodimer
-
-
monomer
additional information
3D-structure analysis, dCK structure model, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphoprotein
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
dCK in complex with acyclovir at the nucleoside phosphoryl acceptor site, and UDP at the phosphoryl donor site, hanging drop vapour diffusion method, 20 mg/ml protein with 5 mM UDP and 5 mM acyclovir is mixed with reservoir solution containing 0.90-1.5 M trisodium citrate dihydrate and 100 mM HEPES, pH 7.5, 12°C, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement
enzyme mutant C9S/C45S/C59S/S74E/R104M/D133A/C146S in complex with L-dT and UDP, hanging drop vapour diffusion method, mixing of 0.001 ml of 9-15 mg/ml protein mixed with 0.001 ml reservoir solution containing 0.9-1.5 M trisodium citrate dihydrate and 100 mM Tris, pH 7.5, room temperature, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution
hanging drop vapour diffusion method, in complex with 2-chloro-9-(2-deoxy-2-fluoro-beta-D-arabinofuranosyl)-9H-purin-6-amine and ADP
hanging drop vapour diffusion method, in complex with deoxycytidine (dC) and UDP, and in the presence of deoxycytidine but the absence of UDP or ADP
in complex with 5-methyldeoxycytidine and ADP, hanging drop vapor diffusion method
in complex with dCMP, UDP, and Mg2+ ion, as well as with dAMP, UDP and Mg2+ ion, both to 3.4 A resolution. Product complexes with UDP and a dead-end complex with substrate and UDP have similar active-site conformations
in complex with inhibitors 2-(((2-(3-(2-fluoroethoxy)-4-methoxyphenyl)-5-methylthiazol-4-yl)methyl)thio)pyrimidine-4,6-diamine and 1-(5-(4-(((4,6-diaminopyrimidin-2-yl)thio)methyl)-5-propylthiazol-2-yl)-2-methoxyphenoxy)-2-methylpropan-2-ol , hanging drop vapor diffusion method, using 0.9-1.5 M trisodium citrate dehydrate and 25 mM HEPES (pH 7.5), at 12°C
in complex with inhibitors and UDP, hanging drop vapor diffusion method, using 0.9-1.5 M trisodium citrate dehydrate and 25 mM HEPES pH 7.5
mutant C9S/C45S/C59S/C146S in complex with D-2'-deoxycytidine and ADP, L-2'-deoxycytidine and ADP, and with 5-fluoro-1-(2R,5S)-[2-(hydroxymethyl)-1,3-oxathiolan-5-yl]cytosine, i.e. emtricitabine, and ADP. The ability of deoxycytidine kinase to phosphorylate the beta-form of enantiomeric nucleosides is due to both the nature of the enzyme’s active site and the nature of the substrates. Most of the binding interactions between substrate and enzyme are directed at the base moiety of the nucleoside
mutant C9S/C45S/C59S/C146S in complex with L-nucleosides (-)-beta-2',3'-dideoxy-3'-thiacytidine and troxacitabine. The nucleoside binding-site tolerates substrates with different chiral configurations by maintaining virtually all of the protein-ligand interactions responsible for productive substrate positioning. The pseudo-symmetry of nucleosides and nucleoside analogs in combination with their conformational flexibility allows the L- and D-enantiomeric forms to adopt similar shapes when bound to the enzyme
mutant enzyme R104M/D133A in complex with L-thymidine, hanging drop vapor diffusion method, using 0.90-1.5 M trisodium citrate dihydrate and 100 mM HEPES, pH 7.5
purified recombinanat Wild-type enzyme in complex with 5-methyldeoxycytidine and ADP, hanging drop vapour diffusion method, mixing of 0.001 ml of 8 mg/ml protein mixed with 0.001 ml reservoir solution containing 0.9-1.5 M trisodium citrate dihydrate and 100 mM Tris, pH 7.5, room temperature, X-ray diffraction structure determination and analysis at 1.96 A resolution
structural studies of ternary complexes. The enzyme conformation adjusts to the different hydrogen-bonding properties between 2'-deoxyadenosine and 2'-deoxyguanosine and to the presence of substituent at the 2-position present in 2'-deoxyguanosine and cladribine. The carbonyl group in 2'-deoxyguansoine elicits a conformational adjustment of the active site residues Arg104 and Asp133. 2'-Deoxyguanosine and cladribine adopt the anti conformation, in contrast to the syn conformation observed with 2'-deoxyadenosine
crystal structure model construction, using the crystal structure of deoxyguanosine kinase, EC 2.7.1.113, as a template, for docking simulations of enzyme with purine nucleosides and analogues, overview
-
hanging drop vapour diffusion method, mutant enzyme crystallized in complex with its substrates (-)-beta-2’,3’-dideoxy-3’-thiacytidine and troxacitabine
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A100V/R104M/D133A
A100V/R104M/D133S
A100V/R104M/D133S/E196A
the mutant shows low activity for D-deoxycytidine and D-thymidine
A100V/R104M/D133S/E196L
inactive
A100V/R104M/D133S/F96D
inactive
A100V/R104M/D133S/F96Y
the mutant shows low activity for D-deoxycytidine and D-thymidine
A100V/R104M/D133S/W58E
inactive
A100V/R104M/D133S/W58V
the mutant shows low activity for D-deoxycytidine and D-thymidine
A100V/R104M/D133T
ratio kcat/Km for deoxycytidine similar to wild-type
A119G
genetic polymorphism, 66% of wild-type activity, decrease in Km value
C146A
very low activity
C185A
lower efficiency with dCyd as the substrate with ATP und UTP, nearly 2-fold higher efficiency than wild-type dCK with dAdo as substrate and UTP as the phosphate donor
C9S/C45S/C59S/C146S
C9S/C45S/C59S/S74E/R104M/D133A/C146S
site-directed mutagenesis, crystallization mutant
D133A
site-directed mutagenesis, the mutation renders the enzyme capable of thymidine binding
D47E/R104Q/D133G/N163I/F242L
1.5fold increase in ratio kcat/Km for deoxycytidine
DEL65-79
construction of an enzyme variant lacking a flexible insert (residues 65-79) but having similar catalytic properties as the wild type
I24V
genetic polymorphism, 85% of wild-type activity
P122S
genetic polymorphism, 43% of wild-type activity, decrease in Km value
R104I/D133A
site-directed mutagenesis, the mutations render the enzyme active with 5-substituted deoxycytidine and thymidine, altered substrate specificity compared to the wild-type enzyme
R104L/D133A
R104M
site-directed mutagenesis, the mutation renders the enzyme capable of thymidine binding
R104M/D133A
R104M/D133N
R104M/D133N/A138I
inactive
R104M/D133N/L102Y
the mutant shows low activity for D-deoxycytidine and D-thymidine
R104M/D133N/L191A
the mutant shows low activity for D-deoxycytidine and D-thymidine
R104M/D133N/M85Y
the mutant shows low activity for D-deoxycytidine and D-thymidine
R104M/D133N/P89F
inactive
R104M/D133N/V130T
the mutant shows low activity for D-deoxycytidine and D-thymidine
R104M/D133N/V130T/L191A
the mutant shows low activity for D-deoxycytidine and D-thymidine
R104M/D133N/V55E
the mutant shows very low activity for D-deoxycytidine and D-thymidine
R104M/D133N/V55F
the mutant shows very low activity for D-deoxycytidine and D-thymidine
R104M/D133N/V55F/V130T
the mutant shows very low activity for D-deoxycytidine and D-thymidine
R104M/D133N/V55F/V130T/L191A
the mutant shows very low activity for D-deoxycytidine and D-thymidine
R104M/D133S
6fold increase in ratio kcat/Km for deoxycytidine
R104M/D133T
mutant with reversed substrate specificity, with elevated specific constant for thymidine phosphorylation and decreased activity for deeoxycytidine, deoxyadenosine, and deoxyguanosine
R104Q/D133A
site-directed mutagenesis, the mutations render the enzyme active with 5-substituted deoxycytidine and thymidine, altered substrate specificity compared to the wild-type enzyme
R104Q/D133G
mutant is a generalist kinase with broader specificity and elevated turnover compared with wild-type
R104Q/D133N
1.5fold increase in ratio kcat/Km for deoxycytidine
S11A
no significant effect on activity
S11E
no significant effect on activity
S15A
no significant effect on activity
S15E
no significant effect on activity
S74D
2-4fold lower kcat values
S74Q
no significant change in kcat for any of the substrates tested
T3A
no significant effect on activity
T3E
no significant effect on activity
A119G
naturally occurring mutation, 66% of activity of the wild type protein
C9S/C45S/C59S/C146S
engineered protein has a significantly improved crystallization behaviour compared with the wild type protein
D133A
-
site-directed mutagenesis, the mutant is active with thymidine derivatives, in contrast to the wild-type enzyme
I24V
naturally occurring mutation, 85% of activity of the wild type protein
P122S
R104M
-
site-directed mutagenesis, the mutant is active with thymidine derivatives, in contrast to the wild-type enzyme
R104M/D133A/S74E
-
site-directed mutagenesis, the mutant is active with thymidine derivatives, in contrast to the wild-type enzyme
S11A
-
site-directed mutagenesis, replacement of the phosphorylation site
S11E
-
site-directed mutagenesis, replacement of the phosphorylation site
S15A
-
site-directed mutagenesis, replacement of the phosphorylation site
S15E
-
site-directed mutagenesis, replacement of the phosphorylation site, the mutant shows a slight, but significant, reduction of Ser74 phosphorylation
S74A
-
site-directed mutagenesis
T3A
-
site-directed mutagenesis, replacement of the phosphorylation site, the mutant shows a slight, but significant, reduction of Ser74 phosphorylation
T3E
-
site-directed mutagenesis, replacement of the phosphorylation site, the mutant shows a slight, but significant, reduction of Ser74 phosphorylation
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
at least 6 h stable
54
-
inactivation
additional information
-
temperature stability of deoxycytidine kinase activity differs appreciably from deoxyadenosine kinase activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin stabilizes
-
dithiothreitol, MgCl2, ATP, KCl and glycerol stabilize
-
dTTP, ATP or deoxycytidine stabilizes
-
very unstable at low protein concentrations
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, concentrated enzyme solution in Tris-buffer with MgCl2 and mercaptoethanol, at least 12 months
-
-85°C, in 1 mg/ml bovine serum albumin, 20% v/v glycerol, 0.2 M potassium phosphate, 2 mM ATP, 2.4 mM MgCl2 and 0.025 M DTT, more than 12 months
-
4°C, concentrated enzyme solution in Tris-buffer with MgCl2 and mercaptoethanol, at least 2 weeks
-
4°C, t1/2: 7 days with and t1/2: 72 h without bovine serum albumin
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap nickel-affinity column chromatography and S-200 gel filtration
Ni-NTA agarose resin column chromatography
Ni-NTA column chromatography
Ni-NTA column chromatography, gel filtration
recombinant enzymes using His-tag
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain C41(DE3) by nickel affinity chromatography and gel filtration
recombinant protein using His-tag
affinity chromatography
-
His-Trap TM column chromatography and Sephacryl S-200 gel filtration
-
HisTrap column chromatography
-
mitochondrial isozyme (extracted with digitonin)
-
recombinant protein from Escherichia coli
spleen
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli BL21(DE3)
expressed as His-tag fusion protein in HEK293T cells
expressed in Escherichia coli BL21 C41(DE3) cells
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli C41 (DE3) cells
expressed of engineered protein as His-tag fusion protein in Escherichia coli
expression in Cos-1 cells
expression in Escherichia coli
expression in Escherichia coli and in HEK-293 cell
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain C41(DE3)
genetic organization, located on chromosome 4q13.3-4q21.1, expression as GFP-fusion protein with location in the nucleus
native and mutant proteins expressed as His-tag fusion proteins in Escherichia coli BL21(DE3)pLysS
the single copy gene is located on chromosome 4q13.3-q21.1
DNA and amino acid sequence determination and analysis, transient expression of His-tagged wild-type and mutants in HEK 293T cells
-
expressed in Escherichia coli BL21 DE3 pLysE cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in HEK 293T cells
-
expression in murine GI261, rat C6 and human U373 cell
-
mutant protein expressed in Escherichia coli
native and mutant proteins expressed in Escherichia coli BL21 star
overexpression of wild-type and mutant enzymes in Jurkat, Molt-4, and U87-MG cells
-
quantitative real-time-PCR
-
quantitative RT-PCR enzyme expression analysis in Saos-2 cells and OCI-AML3 cells, and overexpression of wild-type and mutant enzymes in Saos2 cells, overview
-
quantitative RT-PCR expression analysis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
glutathionylation leads to increased enzyme activity. AraC and 2',2'-difluorodeoxycytidine treatment leads to increased enzyme protein but decreased enzyme activity
the enzyme is downregulated under hypoxic conditions
treatment with doxorubicin, trifluorothymidine or 2'-deoxy-5-fluorouridine results in downregulation of the enzyme
paclitaxel significantly decreases dCK mRNA and protein levels in H460 and H520 cells
-
RNA-binding protein HuR overexpression elevates dCK protein expression in pancreatic cancer cells
-
RNA-binding protein HuR silencing reduces dCK protein expression in pancreatic cancer cells
-
the enzyme is hypoxia-induced
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
after elution from Sephadex column, reactivation by incubation with 50 mM dithiothreitol and 1 mg/ml bovine serum albumin
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
analysis
-
deoxycytidine kinase from B-cell chronic lymphocytic leukaemia lymphocytes can be detected by use of anti-phospho-ser74 antibodies
medicine
pharmacology
-
the enzyme is a critical determinant of therapeutic activity for several nucleoside analogue prodrugs
additional information
-
deoxycytidine kinase is a key enzyme in the activation of several therapeutic nucleoside analogues
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gaubert, G.; Gosselin, G.; Boudou, V.; Imbach, J.L.; Eriksson, S.; Maury, G.
Low enantioselectivities of human deoxycytidine kinase and human deoxyguanosine kinase with respect to 2'-deoxyadenosine, 2'-deoxyguanosine and their analogs
Biochimie
81
1041-1047
1999
Homo sapiens
Manually annotated by BRENDA team
Yamada, Y.; Goto, H.; Ogasawara, N.
Purine nucleoside kinases in human T- and B-lymphoblasts
Biochim. Biophys. Acta
761
34-40
1983
Homo sapiens
Manually annotated by BRENDA team
Kierdaszuk, B.; Eriksson, S.
Selective inactivation of the deoxyadenosine phosphorylating activity of pure human deoxycytidine kinase: stabilization of different forms of the enzyme by substrates and biological detergents
Biochemistry
29
4109-4114
1990
Homo sapiens
Manually annotated by BRENDA team
Wang, L.M.; Kucera, G.L.; Capizzi, R.L.
Purification and characterization of deoxycytidine kinase from acute myeloid leukemia cell mitochondria
Biochim. Biophys. Acta
1202
309-316
1993
Homo sapiens
Manually annotated by BRENDA team
Eriksson, S.; Cederlund, E.; Bergman, T.; Jrnvall, H.; Bohman, C.
Characterization of human deoxycytidine kinase. Correlation with cDNA sequences
FEBS Lett.
280
363-366
1991
Homo sapiens
Manually annotated by BRENDA team
Kim, M.Y.; Ives, D.H.
Human deoxycytidine kinase: kinetic mechanism and end product regulation
Biochemistry
28
9043-9047
1989
Homo sapiens
Manually annotated by BRENDA team
Datta, N.S.; Shewach, D.S.; Mitchell, B.S.; Fox, I.H.
Kinetic properties and inhibition of human T lymphoblast deoxycytidine kinase
J. Biol. Chem.
264
9359-9364
1989
Homo sapiens
Manually annotated by BRENDA team
Datta, N.S.; Shewach, D.S.; Hurley, M.C.; Mitchell, B.S.; Fox, I.H.
Human T-lymphoblast deoxycytidine kinase: purification and properties
Biochemistry
28
114-123
1989
Homo sapiens
Manually annotated by BRENDA team
Bohman, C.; Eriksson, S.
Deoxycytidine kinase from human leukemic spleen: preparation and characteristics of homogeneous enzyme
Biochemistry
27
4258-4265
1988
Homo sapiens
Manually annotated by BRENDA team
Kim, M.Y.; Ikeda, S.; Ives, D.H.
Affinity purification of human deoxycytidine kinase: avoidance of structural and kinetic artifacts arising from limited proteolysis
Biochem. Biophys. Res. Commun.
156
92-98
1988
Homo sapiens
Manually annotated by BRENDA team
Baxter, A.; Currie, L.M.; Durham, J.P.
A general method for purification of deoxycytidine kinase
Biochem. J.
173
1005-1008
1978
Bos taurus, Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Shewach, D.S.; Reynolds, K.K.; Hertel, L.
Nucleotide specificity of human deoxycytidine kinase
Mol. Pharmacol.
42
518-524
1992
Homo sapiens
Manually annotated by BRENDA team
Habteyesus, A.; Nordenskjoeld, A.; Bohman, C.; Eriksson, S.
Deoxynucleoside phosphorylating enzymes in monkey and human tissues show great similarities, while mouse deoxycytidine kinase has a different substrate specificity
Biochem. Pharmacol.
42
1829-1836
1991
Aotus trivirgatus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Coleman, C.N.; Stoller, R.G.; Drake, J.C.; Chabner, B.A.
Deoxycytidine kinase: properties of the enzyme from human leukemic granulocytes
Blood
46
791-803
1975
Homo sapiens
Manually annotated by BRENDA team
Johansson, M.; Karlsson, A.
Differences in kinetic properties of pure recombinant human and mouse deoxycytidine kinase
Biochem. Pharmacol.
50
163-168
1995
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Csapo, Z.; Sasvari-Szekely, M.; Spasokoukotskaja, T.; Talianidis, I.; Eriksson, S.; Staub, M.
Activation of deoxycytidine kinase by inhibition of DNA synthesis in human lymphocytes
Biochem. Pharmacol.
61
191-197
2001
Homo sapiens
Manually annotated by BRENDA team
Spasokoukotskaja, T.; Sasvari-Szekely, M.; Keszler, G.; Albertioni, F.; Eriksson, S.; Staub, M.
Treatment of normal and malignant cells with nucleoside analogues and etoposide enhances deoxycytidine kinase activity
Eur. J. Cancer
35
1862-1867
1999
Homo sapiens
Manually annotated by BRENDA team
Csapo, Z.; Keszler, G.; Safrany, G.; Spasokoukotskaja, T.; Talianidis, I.; Staub, M.; Sasvari-Szekely, M.
Activation of deoxycytidine kinase by gamma-irradiation and inactivation by hyperosmotic shock in human lymphocytes
Biochem. Pharmacol.
65
2031-2039
2003
Homo sapiens
Manually annotated by BRENDA team
Hughes, T.L.; Hahn, T.M.; Reynolds, K.K.; Shewach, D.S.
Kinetic analysis of human deoxycytidine kinase with the true phosphate donor uridine triphosphate
Biochemistry
36
7540-7547
1997
Homo sapiens
Manually annotated by BRENDA team
Wang, J.; Choudhury, D.; Chattopadhyaya, J.; Eriksson, S.
Stereoisomeric selectivity of human deoxyribonucleoside kinases
Biochemistry
38
16993-16999
1999
Homo sapiens
Manually annotated by BRENDA team
Hatzis, P.; Al-Madhoon, A.S.; Jullig, M.; Petrakis, T.G.; Eriksson, S.; Talianidis, I.
The intracellular localization of deoxycytidine kinase
J. Biol. Chem.
273
30239-30243
1998
Homo sapiens
Manually annotated by BRENDA team
Usova, E.V.; Eriksson, S.
The effects of high salt concentrations on the regulation of the substrate specificity of human recombinant deoxycytidine kinase
Eur. J. Biochem.
248
762-766
1997
Homo sapiens
Manually annotated by BRENDA team
Eriksson, S.; Wang, L.
Substrate specificities, expression and primary sequences of deoxynucleoside kinases; implications for chemotherapy
Nucleosides Nucleotides
16
653-659
1997
Homo sapiens
-
Manually annotated by BRENDA team
Shafiee, M.; Boudoua, V.; Griffon, J.F.; Pompon, A.; Gosselin, G.; Eriksson, S.; Imbach, J.L.; Maury, G.
Study of the enantioselectivity of enzymes involved in nucleoside analog metabolism: deoxycytidine kinase
Nucleosides Nucleotides
16
1767-1770
1997
Homo sapiens
-
Manually annotated by BRENDA team
Kierdaszuk, B.; Krawiec, K.; Kazimierczuk, Z.; Jacobsson, U.; Johansson, N.G.; Munch-Petersen, B.; Eriksson, S.; Shugar, D.
Substrate/inhibitor properties of human deoxycytidine kinase (dCK) and thymidine kinases (TK1 and TK2) towards the sugar moiety of nucleosides, including O'-alkyl analogues
Nucleosides Nucleotides
18
1883-1903
1999
Homo sapiens
Manually annotated by BRENDA team
Mani, R.S.; Usova, E.V.; Eriksson, S.; Cass, C.E.
Hydrodynamic and spectroscopic studies of substrate binding to human recombinant deoxycytidine kinase
Nucleosides, Nucleotides Nucleic Acids
22
175-192
2003
Homo sapiens
Manually annotated by BRENDA team
Kim, M.Y.
Purification of deoxycytidine kinase from various human leukemic cells by endo-product analog affinity chromatography
J. Biochem. Mol. Biol.
28
281-289
1995
Homo sapiens
-
Manually annotated by BRENDA team
Spasokoukotskaja, T.; Sasvari-Szekely, M.; Hullan, L.; Albertioni, F.; Eriksson, S.; Staub, M.
Activation of deoxycytidine kinase by various nucleoside analogues
Adv. Exp. Med. Biol.
431
641-645
1998
Homo sapiens
Manually annotated by BRENDA team
Spasokoukotskaja, T.; Csapo, Z.; Sasvari-Szekely, M.; Virga, S.; Talianidis, I.; Eriksson, S.; Staub, M.
Effect of phosphorylation on deoxycytidine kinase activity
Adv. Exp. Med. Biol.
486
281-285
2000
Homo sapiens
Manually annotated by BRENDA team
Someya, H.; Shaddix, S.C.; Tiwari, K.N.; Secrist, J.A., 3rd; Parker, W.B.
Phosphorylation of 4'-thio-beta-D-arabinofuranosylcytosine and its analogs by human deoxycytidine kinase
J. Pharmacol. Exp. Ther.
304
1314-1322
2003
Homo sapiens
Manually annotated by BRENDA team
Shafiee, M.; Gosselin, G.; Imbach, J.L.; Divita, G.; Eriksson, S.; Maury, G.
Study of human deoxycytidine kinase binding properties using intrinsic fluorescence or new fluorescent ligands
Eur. J. Med. Chem.
34
423-431
1999
Homo sapiens
-
Manually annotated by BRENDA team
Csapo, Z.; Sasvari-Szekely, M.; Spasokoukotskaja, T.; Staub, M.
Modulation of human deoxycytidine kinase activity as a response to cellular stress induced by NaF
Acta Biochim. Pol.
48
251-256
2001
Homo sapiens
Manually annotated by BRENDA team
Keszler, G.; Szikla, K.; Kazimierczuk, Z.; Spasokoukotskaja, T.; Sasvari-Szekely, M.; Staub, M.
Selective activation of deoxycytidine kinase by thymidine-5'-thiosulphate and release by deoxycytidine in human lymphocytes
Biochem. Pharmacol.
65
563-571
2003
Homo sapiens
Manually annotated by BRENDA team
Keszler, G.; Virga, S.; Spasokoukotskaja, T.; Bauer, P.I.; Sasvari-Szekely, M.; Staub, M.
Activation of deoxycytidine kinase by deoxyadenosine: implications in deoxyadenosine-mediated cytotoxicity
Arch. Biochem. Biophys.
436
69-77
2005
Homo sapiens
Manually annotated by BRENDA team
Feng, J.Y.; Parker, W.B.; Krajewski, M.L.; Deville-Bonne, D.; Veron, M.; Krishnan, P.; Cheng, Y.C.; Borroto-Esoda, K.
Anabolism of amdoxovir: phosphorylation of dioxolane guanosine and its 5'-phosphates by mammalian phosphotransferases
Biochem. Pharmacol.
68
1879-1888
2004
Homo sapiens
Manually annotated by BRENDA team
Rylova, S.N.; Albertioni, F.; Flygh, G.; Eriksson, S.
Activity profiles of deoxynucleoside kinases and 5'-nucleotidases in cultured adipocytes and myoblastic cells: insights into mitochondrial toxicity of nucleoside analogs
Biochem. Pharmacol.
69
951-960
2005
Homo sapiens
Manually annotated by BRENDA team
Johnsamuel, J.; Eriksson, S.; Oliveira, M.; Tjarks, W.
Docking simulation with a purine nucleoside specific homology model of deoxycytidine kinase, a target enzyme for anticancer and antiviral therapy
Bioorg. Med. Chem.
13
4160-4167
2005
Homo sapiens
Manually annotated by BRENDA team
Eriksson, S.; Munch-Petersen, B.; Johansson, K.; Eklund, H.
Structure and function of cellular deoxyribonucleoside kinases
Cell. Mol. Life Sci.
59
1327-1346
2002
Homo sapiens (P27707)
Manually annotated by BRENDA team
Piskur, J.; Sandrini, M.P.B.; Knecht, W.; Munch-Petersen, B.
Animal deoxyribonucleoside kinases: 'forward' and 'retrograde' evolution of their substrate specificity
FEBS Lett.
560
3-6
2004
Homo sapiens (P27707), Mus musculus (P43346)
Manually annotated by BRENDA team
Hubeek, I.; Peters, G.J.; Broekhuizen, A.J.F.; Talianidis, I.; Sigmond, J.; Gibson, B.E.S.; Creutzig, U.; Giaccone, G.; Kaspers, G.J.L.
Immunocytochemical detection of deoxycytidine kinase in haematological malignancies and solid tumours
J. Clin. Pathol.
58
695-699
2005
Homo sapiens
Manually annotated by BRENDA team
Mani, R.S.; Usova, E.V.; Eriksson, S.; Cass, C.E.
Fluorescence studies of substrate binding to human recombinant deoxycytidine kinase
Nucleosides Nucleotides Nucleic Acids
23
1343-1346
2004
Homo sapiens
Manually annotated by BRENDA team
Hubeek, I.; Peters, G.J.; Broekhuizen, A.J.F.; Talianidis, I.; Schouten van Meeteren, A.Y.N.; van Wering, E.R.; Gibson, B.; Creutzig, U.; Kaspers, G.J.L.
Immunocytochemical detection of deoxycytidine kinase in pediatric malignancies in relation to in vitro cytarabine sensitivity
Nucleosides Nucleotides Nucleic Acids
23
1351-1356
2004
Homo sapiens
Manually annotated by BRENDA team
Al-Madhoun, A.S.; Eriksson, S.; Wang, Z.X.; Naimi, E.; Knaus, E.E.; Wiebe, L.I.
Phosphorylation of isocarbostyril- and difluorophenyl-nucleoside thymidine mimics by the human deoxynucleoside kinases
Nucleosides Nucleotides Nucleic Acids
23
1865-1874
2004
Homo sapiens
Manually annotated by BRENDA team
Van Rompay, A.R.; Johansson, M.; Karlsson, A.
Substrate specificity and phosphorylation of antiviral and anticancer nucleoside analogues by human deoxyribonucleoside kinases and ribonucleoside kinases
Pharmacol. Ther.
100
119-139
2003
Homo sapiens (P27707)
Manually annotated by BRENDA team
Zhang, Y.; Secrist, J.A.; Ealick, S.E.
The structure of human deoxycytidine kinase in complex with clofarabine reveals key interactions for prodrug activation
Acta Crystallogr. Sect. D
62
133-139
2006
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Fyrberg, A.; Albertioni, F.; Lotfi, K.
Cell cycle effect on the activity of deoxynucleoside analogue metabolising enzymes
Biochem. Biophys. Res. Commun.
357
847-853
2007
Homo sapiens
Manually annotated by BRENDA team
Van den Neste, E.; Smal, C.; Cardoen, S.; Delacauw, A.; Frankard, J.; Ferrant, A.; Van den Berghe, G.; Bontemps, F.
Activation of deoxycytidine kinase by UV-C-irradiation in chronic lymphocytic leukemia B-lymphocytes
Biochem. Pharmacol.
65
573-580
2003
Homo sapiens
Manually annotated by BRENDA team
Smal, C.; Cardoen, S.; Betrand, L.; Delacauw, A.; Ferrant, A.; Van den Berghe, G.; Van den Neste, E.; Bontemps, F.
Activation of deoxycytidine kinase by protein kinase inhibitors and okadaic acid in leukemic cells
Biochem. Pharmacol.
69
95-103
2003
Homo sapiens
Manually annotated by BRENDA team
Mani, R.S.; Usova, E.V.; Cass, C.E.; Eriksson, S.
Fluorescence energy transfer studies of human deoxycytidine kinase: role of cysteine 185 in the conformational changes that occur upon substrate binding
Biochemistry
45
3534-3541
2006
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Godsey, M.H.; Ort, S.; Sabini, E.; Konrad, M.; Lavie, A.
Structural basis for the preference of UTP over ATP in human deoxycytidine kinase: Illuminating the role of main-chain reorganization
Biochemistry
45
452-461
2006
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Pauwels, B.; Korst, A.E.; Pattyn, G.G.; Lambrechts, H.A.; Kamphuis, J.A.; De Pooter, C.M.; Peters, G.J.; Lardon, F.; Vermorken, J.B.
The relation between deoxycytidine kinase activity and the radiosensitising effect of gemcitabine in eight different human tumour cell lines
BMC Cancer
6
142
2006
Homo sapiens
Manually annotated by BRENDA team
Bierau, J.; van Gennip, A.H.; Leen, R.; Meinsma, R.; Caron, H.N.; van Kuilenburg, A.B.
Cyclopentenyl cytosine-induced activation of deoxycytidine kinase increases gemcitabine anabolism and cytotoxicity in neuroblastoma
Cancer Chemother. Pharmacol.
57
105-113
2006
Homo sapiens
Manually annotated by BRENDA team
Smal, C.; Van Den Neste, E.; Maerevoet, M.; Poire, X.; Theate, I.; Bontemps, F.
Positive regulation of deoxycytidine kinase activity by phosphorylation of Ser-74 in B-cell chronic lymphocytic leukemia lymphocytes
Cancer Lett.
253
68-73
2007
Homo sapiens
Manually annotated by BRENDA team
Sebastiani, V.; Ricci, F.; Rubio-Viqueira, B.; Rubio-Viquiera, B.; Kulesza, P.; Yeo, C.J.; Hidalgo, M.; Klein, A.; Laheru, D.; Iacobuzio-Donahue, C.A.
Immunohistochemical and genetic evaluation of deoxycytidine kinase in pancreatic cancer: relationship to molecular mechanisms of gemcitabine resistance and survival
Clin. Cancer Res.
12
2492-2497
2006
Homo sapiens
Manually annotated by BRENDA team
Smal, C.; Vertommen, D.; Bertrand, L.; Ntamashimikiro, S.; Rider, M.H.; Van Den Neste, E.; Bontemps, F.
Identification of in vivo phosphorylation sites on human deoxycytidine kinase. Role of Ser-74 in the control of enzyme activity
J. Biol. Chem.
281
4887-4893
2006
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Lamba, J.K.; Crews, K.; Pounds, S.; Schuetz, E.; Gresham, J.; Gandhi, V.; Plunkett, W.; Rubnitz, J.; Ribeiro, R.
Pharmacogenetics of deoxycytidine kinase: Identification and characterization of novel genetic variants
J. Pharmacol. Exp. Ther.
323
935-945
2007
Homo sapiens, Homo sapiens (P27707)
Manually annotated by BRENDA team
Sabini, E.; Hazra, S.; Konrad, M.; Burley, S.K.; Lavie, A.
Structural basis for activation of the therapeutic L-nucleoside analogs 3TC and troxacitabine by human deoxycytidine kinase
Nucleic Acids Res.
35
186-192
2007
Homo sapiens, Homo sapiens (P27707)
Manually annotated by BRENDA team
Sigmond, J.; Haveman, J.; Kreder, N.C.; Loves, W.J.; van Bree, C.; Franken, N.A.; Peters, G.J.
Enhanced activity of deoxycytidine kinase after pulsed low dose rate and single dose gamma irradiation
Nucleosides Nucleotides Nucleic Acids
25
1177-1180
2006
Homo sapiens
Manually annotated by BRENDA team
Fyrberg, A.; Mirzaee, S.; Lotfi, K.
Cell cycle dependent regulation of deoxycytidine kinase, deoxyguanosine kinase, and cytosolic 5-nucleotidase I activity in MOLT-4 cells
Nucleosides Nucleotides Nucleic Acids
25
1201-1204
2006
Homo sapiens
Manually annotated by BRENDA team
Soriano, E.V.; Clark, V.C.; Ealick, S.E.
Structures of human deoxycytidine kinase product complexes
Acta Crystallogr. Sect. D
63
1201-1207
2007
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Ohhashi, S.; Ohuchida, K.; Mizumoto, K.; Fujita, H.; Egami, T.; Yu, J.; Toma, H.; Sadatomi, S.; Nagai, E.; Tanaka, M.
Down-regulation of deoxycytidine kinase enhances acquired resistance to gemcitabine in pancreatic cancer
Anticancer Res.
28
2205-2212
2008
Homo sapiens
Manually annotated by BRENDA team
Iyidogan, P.; Lutz, S.
Systematic exploration of active site mutations on human deoxycytidine kinase substrate specificity
Biochemistry
47
4711-4720
2008
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Szatmari, T.; Huszty, G.; Desaknai, S.; Spasokoukotskaja, T.; Sasvari-Szekely, M.; Staub, M.; Esik, O.; Safrany, G.; Lumniczky, K.
Adenoviral vector transduction of the human deoxycytidine kinase gene enhances the cytotoxic and radiosensitizing effect of gemcitabine on experimental gliomas
Cancer Gene Ther.
15
154-164
2008
Homo sapiens
Manually annotated by BRENDA team
Kocabas, N.A.; Aksoy, P.; Pelleymounter, L.L.; Moon, I.; Ryu, J.S.; Gilbert, J.A.; Salavaggione, O.E.; Eckloff, B.W.; Wieben, E.D.; Yee, V.; Weinshilboum, R.M.; Ames, M.M.
Gemcitabine pharmacogenomics: deoxycytidine kinase and cytidylate kinase gene resequencing and functional genomics
Drug Metab. Dispos.
36
1951-1959
2008
Homo sapiens (P27707)
Manually annotated by BRENDA team
McSorley, T.; Ort, S.; Hazra, S.; Lavie, A.; Konrad, M.
Mimicking phosphorylation of Ser-74 on human deoxycytidine kinase selectively increases catalytic activity for dC and dC analogues
FEBS Lett.
582
720-724
2008
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Sabini, E.; Hazra, S.; Konrad, M.; Lavie, A.
Nonenantioselectivity property of human deoxycytidine kinase explained by structures of the enzyme in complex with L- and D-nucleosides
J. Med. Chem.
50
3004-3014
2007
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Sabini, E.; Hazra, S.; Konrad, M.; Lavie, A.
Elucidation of different binding modes of purine nucleosides to human deoxycytidine kinase
J. Med. Chem.
51
4219-4225
2008
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Joachims, M.L.; Marble, P.; Knott-Craig, C.; Pastuszko, P.; Blackburn, M.R.; Thompson, L.F.
Inhibition of deoxynucleoside kinases in human thymocytes prevents dATP accumulation and induction of apoptosis
Nucleosides Nucleotides Nucleic Acids
27
816-820
2008
Homo sapiens
Manually annotated by BRENDA team
Hazra, S.; Sabini, E.; Ort, S.; Konrad, M.; Lavie, A.
Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase
Biochemistry
48
1256-1263
2009
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Jessop, T.C.; Tarver, J.E.; Carlsen, M.; Xu, A.; Healy, J.P.; Heim-Riether, A.; Fu, Q.; Taylor, J.A.; Augeri, D.J.; Shen, M.; Stouch, T.R.; Swanson, R.V.; Tari, L.W.; Hunter, M.; Hoffman, I.; Keyes, P.E.; Yu, X.C.; Miranda, M.; Liu, Q.; Swaffield, J.C.; David Kimball, S.; Nouraldeen, A.; Wilson, A.G.; Foushee, A.M.
Lead optimization and structure-based design of potent and bioavailable deoxycytidine kinase inhibitors
Bioorg. Med. Chem. Lett.
19
6784-6787
2009
Homo sapiens (P27707)
Manually annotated by BRENDA team
Costantino, C.L.; Witkiewicz, A.K.; Kuwano, Y.; Cozzitorto, J.A.; Kennedy, E.P.; Dasgupta, A.; Keen, J.C.; Yeo, C.J.; Gorospe, M.; Brody, J.R.
The role of HuR in gemcitabine efficacy in pancreatic cancer: HuR up-regulates the expression of the gemcitabine metabolizing enzyme deoxycytidine kinase
Cancer Res.
69
4567-4572
2009
Homo sapiens
Manually annotated by BRENDA team
Kim, S.R.; Saito, Y.; Maekawa, K.; Sugiyama, E.; Kaniwa, N.; Ueno, H.; Okusaka, T.; Ikeda, M.; Morizane, C.; Yamamoto, N.; Yoshida, T.; Kamatani, N.; Furuse, J.; Ishii, H.; Saijo, N.; Ozawa, S.; Sawada, J.
Twenty novel genetic variations and haplotype structures of the DCK gene encoding human deoxycytidine kinase (dCK)
Drug Metab. Pharmacokinet.
23
379-384
2008
Homo sapiens
Manually annotated by BRENDA team
Yu, X.C.; Miranda, M.; Liu, Z.; Patel, S.; Nguyen, N.; Carson, K.; Liu, Q.; Swaffield, J.C.
Novel potent inhibitors of deoxycytidine kinase identified and compared by multiple assays
J. Biomol. Screen.
15
72-79
2010
Homo sapiens
Manually annotated by BRENDA team
Shord, S.; Patel, S.
Paclitaxel alters the expression and specific activity of deoxycytidine kinase and cytidine deaminase in non-small cell lung cancer cell lines
J. Exp. Clin. Cancer Res.
28
76
2009
Homo sapiens
Manually annotated by BRENDA team
Funamizu, N.; Okamoto, A.; Kamata, Y.; Misawa, T.; Uwagawa, T.; Gocho, T.; Yanaga, K.; Manome, Y.
Is the resistance of gemcitabine for pancreatic cancer settled only by overexpression of deoxycytidine kinase?
Oncol. Rep.
23
471-475
2010
Homo sapiens
Manually annotated by BRENDA team
Stalhandske, P.; Wang, L.; Westberg, S.; von Euler, H.; Groth, E.; Gustafsson, S.A.; Eriksson, S.; Lennerstrand, J.
Homogeneous assay for real-time and simultaneous detection of thymidine kinase 1 and deoxycytidine kinase activities
Anal. Biochem.
432
155-164
2013
Homo sapiens
Manually annotated by BRENDA team
Amsailale, R.; Van Den Neste, E.; Arts, A.; Starczewska, E.; Bontemps, F.; Smal, C.
Phosphorylation of deoxycytidine kinase on Ser-74: impact on kinetic properties and nucleoside analog activation in cancer cells
Biochem. Pharmacol.
84
43-51
2012
Homo sapiens
Manually annotated by BRENDA team
Hazra, S.; Ort, S.; Konrad, M.; Lavie, A.
Structural and kinetic characterization of human deoxycytidine kinase variants able to phosphorylate 5-substituted deoxycytidine and thymidine analogues
Biochemistry
49
6784-6790
2010
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Hazra, S.; Szewczak, A.; Ort, S.; Konrad, M.; Lavie, A.
Post-translational phosphorylation of serine 74 of human deoxycytidine kinase favors the enzyme adopting the open conformation making it competent for nucleoside binding and release
Biochemistry
50
2870-2880
2011
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Nagai, S.; Takenaka, K.; Nachagari, D.; Rose, C.; Domoney, K.; Sun, D.; Sparreboom, A.; Schuetz, J.D.
Deoxycytidine kinase modulates the impact of the ABC transporter ABCG2 on clofarabine cytotoxicity
Cancer Res.
71
1781-1791
2011
Homo sapiens
Manually annotated by BRENDA team
Weng, T.; Karmouty-Quintana, H.; Garcia-Morales, L.J.; Molina, J.G.; Pedroza, M.; Bunge, R.R.; Bruckner, B.A.; Loebe, M.; Seethamraju, H.; Blackburn, M.R.
Hypoxia-induced deoxycytidine kinase expression contributes to apoptosis in chronic lung disease
FASEB J.
27
2013-2026
2013
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Hazra, S.; Konrad, M.; Lavie, A.
The sugar ring of the nucleoside is required for productive substrate positioning in the active site of human deoxycytidine kinase (dCK): implications for the development of dCK-activated acyclic guanine analogues
J. Med. Chem.
53
5792-5800
2010
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Shu, C.J.; Campbell, D.O.; Lee, J.T.; Tran, A.Q.; Wengrod, J.C.; Witte, O.N.; Phelps, M.E.; Satyamurthy, N.; Czernin, J.; Radu, C.G.
Novel PET probes specific for deoxycytidine kinase
J. Nucl. Med.
51
1092-1098
2010
Homo sapiens, Mus musculus, Mus musculus C57/BL6J
Manually annotated by BRENDA team
Neschadim, A.; Wang, J.; Sato, T.; Fowler, D.; Lavie, A.; Medin, J.
Cell fate control gene therapy based on engineered variants of human deoxycytidine kinase
Mol. Ther.
20
1002-1013
2012
Homo sapiens
Manually annotated by BRENDA team
Yang, C.; Lee, M.; Hao, J.; Cui, X.; Guo, X.; Smal, C.; Bontemps, F.; Ma, S.; Liu, X.; Engler, D.; Parker, W.B.; Xu, B.
Deoxycytidine kinase regulates the G2/M checkpoint through interaction with cyclin-dependent kinase 1 in response to DNA damage
Nucleic Acids Res.
40
9621-9632
2012
Homo sapiens
Manually annotated by BRENDA team
Smal, C.; Ntamashimikiro, S.; Arts, A.; Van Den Neste, E.; Bontemps, F.
Influence of phosphorylation of THR-3, SER-11, and SER-15 on deoxycytidine kinase activity and stability
Nucleosides Nucleotides Nucleic Acids
29
404-407
2010
Homo sapiens
Manually annotated by BRENDA team
Ohmine, K.; Kawaguchi, K.; Ohtsuki, S.; Motoi, F.; Egawa, S.; Unno, M.; Terasaki, T.
Attenuation of phosphorylation by deoxycytidine kinase is key to acquired gemcitabine resistance in a pancreatic cancer cell line: targeted proteomic and metabolomic analyses in PK9 cells
Pharm. Res.
29
2006-2016
2012
Homo sapiens
Manually annotated by BRENDA team
Muthu, P.; Chen, H.X.; Lutz, S.
Redesigning human 2'-deoxycytidine kinase enantioselectivity for L-nucleoside analogues as reporters in positron emission tomography
ACS Chem. Biol.
9
2326-2333
2014
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Nomme, J.; Murphy, J.M.; Su, Y.; Sansone, N.D.; Armijo, A.L.; Olson, S.T.; Radu, C.; Lavie, A.
Structural characterization of new deoxycytidine kinase inhibitors rationalizes the affinity-determining moieties of the molecules
Acta Crystallogr. Sect. D
70
68-78
2014
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Yamanishi, M.; Narazaki, H.; Asano, T.
Melatonin overcomes resistance to clofarabine in two leukemic cell lines by increased expression of deoxycytidine kinase
Exp. Hematol.
43
207-214
2015
Homo sapiens
Manually annotated by BRENDA team
Fan, W.; Zhou, Z.Y.; Huang, X.F.; Bao, C.D.; Du, F.
Deoxycytidine kinase promotes the migration and invasion of fibroblast-like synoviocytes from rheumatoid arthritis patients
Int. J. Clin. Exp. Pathol.
6
2733-2744
2013
Homo sapiens
Manually annotated by BRENDA team
Hao, W.; Yang, L.; Wang, J.; Hsu, C.; Chang, L.; Hsu, K.
Facile method for determination of deoxycytidine kinase activity in biological milieus
J. Food Drug Anal.
22
236-241
2014
Homo sapiens
-
Manually annotated by BRENDA team
Murphy, J.M.; Armijo, A.L.; Nomme, J.; Lee, C.H.; Smith, Q.A.; Li, Z.; Campbell, D.O.; Liao, H.I.; Nathanson, D.A.; Austin, W.R.; Lee, J.T.; Darvish, R.; Wei, L.; Wang, J.; Su, Y.; Damoiseaux, R.; Sadeghi, S.; Phelps, M.E.; Herschman, H.R.; Czernin, J.; Alexandrova, A.N.; Jung, M.E.; Lavie, A.; Radu, C.G.
Development of new deoxycytidine kinase inhibitors and noninvasive in vivo evaluation using positron emission tomography
J. Med. Chem.
56
6696-6708
2013
Homo sapiens (P27707)
Manually annotated by BRENDA team
Coulibaly, S.T.; Rossolillo, P.; Winter, F.; Kretzschmar, F.K.; Braye, M.; Martin, D.P.; Lener, D.; Negroni, M.
Potent sensitisation of cancer cells to anticancer drugs by a quadruple mutant of the human deoxycytidine kinase
PLoS ONE
10
e0140741
2015
Homo sapiens
Manually annotated by BRENDA team
Koduvayur, S.P.; Su, Y.; Kay, B.K.; Lavie, A.
Targeted delivery of deoxycytidine kinase to Her2-positive cells enhances the efficacy of the nucleoside analog fludarabine
PLoS ONE
11
e0157114
2016
Homo sapiens
Manually annotated by BRENDA team
Sun, R.; Eriksson, S.; Wang, L.
The expression and activity of thymidine kinase 1 and deoxycytidine kinase are modulated by hydrogen peroxide and nucleoside analogs
Nucleosides Nucleotides Nucleic Acids
39
1347-1358
2020
Homo sapiens (P27707)
Manually annotated by BRENDA team
Hellendahl, K.; Kamel, S.; Wetterwald, A.; Neubauer, P.; Wagner, A.
Human deoxycytidine kinase is a valuable biocatalyst for the synthesis of nucleotide analogues
Catalysts
9
997
2019
Homo sapiens (P27707)
-
Manually annotated by BRENDA team
Degwert, N.; Latuske, E.; Vohwinkel, G.; Stamm, H.; Klokow, M.; Bokemeyer, C.; Fiedler, W.; Wellbrock, J.
Deoxycytidine kinase is downregulated under hypoxic conditions and confers resistance against cytarabine in acute myeloid leukaemia
Eur. J. Haematol.
97
239-244
2016
Homo sapiens (P27707), Homo sapiens
Manually annotated by BRENDA team
Zhong, R.; Xin, R.; Chen, Z.; Liang, N.; Liu, Y.; Ma, S.; Liu, X.
The role of deoxycytidine kinase (dCK) in radiation-induced cell death
Int. J. Mol. Sci.
17
1939
2016
Homo sapiens (P27707)
Manually annotated by BRENDA team
Zhong, R.; Liang, B.; Xin, R.; Zhu, X.; Liu, Z.; Chen, Q.; Hou, Y.; Jin, Z.; Qi, M.; Ma, S.; Liu, X.
Deoxycytidine kinase participates in the regulation of radiation-induced autophagy and apoptosis in breast cancer cells
Int. J. Oncol.
52
1000-1010
2018
Homo sapiens (P27707)
Manually annotated by BRENDA team