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Information on EC 2.7.1.145 - deoxynucleoside kinase and Organism(s) Xenopus laevis and UniProt Accession Q8UVZ9

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EC Tree
IUBMB Comments
The enzyme from embryonic cells of the fruit fly Drosophila melanogaster differs from other 2'-deoxyribonucleoside kinases [EC 2.7.1.76 (deoxyadenosine kinase) and EC 2.7.1.113 (deoxyguanosine kinase)] in its broad specificity for all four common 2'-deoxyribonucleosides.
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This record set is specific for:
Xenopus laevis
UNIPROT: Q8UVZ9
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Word Map
The taxonomic range for the selected organisms is: Xenopus laevis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
dm-dnk, deoxyribonucleoside kinase, deoxynucleoside kinase, multisubstrate deoxyribonucleoside kinase, pyrimidine deoxyribonucleoside kinase, dmdnk, deoxyribonucleoside phosphotransferase, multi-substrate deoxyribonucleoside kinase, xen-pyk, d. melanogaster deoxynucleoside kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pyrimidine deoxyribonucleoside kinase
-
D. melanogaster deoxynucleoside kinase
-
-
-
-
deoxyribonucleoside kinase
-
-
-
-
deoxyribonucleoside phosphotransferase
-
-
-
-
Dm-dNK
-
-
-
-
dNK
-
-
-
-
kinase (phosphorylating), deoxynucleoside
-
-
-
-
ms-dNK
-
-
-
-
multifunctional deoxynucleoside kinase
-
-
-
-
multispecific deoxynucleoside kinase
-
-
-
-
multisubstrate deoxyribonucleoside kinase
-
-
-
-
additional information
the enzyme belongs to the thymidine kinase 2-like, i.e. TK2-like, family of enzymes
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
ATP:deoxynucleoside 5'-phosphotransferase
The enzyme from embryonic cells of the fruit fly Drosophila melanogaster differs from other 2'-deoxyribonucleoside kinases [EC 2.7.1.76 (deoxyadenosine kinase) and EC 2.7.1.113 (deoxyguanosine kinase)] in its broad specificity for all four common 2'-deoxyribonucleosides.
CAS REGISTRY NUMBER
COMMENTARY hide
52227-81-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1-beta-D-arabinofuranosylcytosine
ADP + 1-beta-D-arabinofuranosylcytosine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + 1-beta-D-arabinofuranosylthymine
ADP + 1-beta-D-arabinofuranosylthymine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + 2',3'-dideoxycytidine
ADP + 2',3'-dideoxycytidine 5'-phosphate
show the reaction diagram
low activity
-
-
?
ATP + 2',3'-dideoxythymidine
ADP + 2',3'-dideoxythymidine 5'-phosphate
show the reaction diagram
low activity
-
-
?
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'-deoxythymidine
ADP + 2'-deoxythymidine 5'-phosphate
show the reaction diagram
ATP + 2-chloro-2'-deoxyadenosine
ADP + 2-chloro-2'-deoxyadenosine 5'-phosphate
show the reaction diagram
low activity
-
-
?
ATP + 3'-azido-2',3'-didehydro-3'-deoxythymidine
ADP + 3'-azido-2',3'-didehydro-3'-deoxythymidine 5'-phosphate
show the reaction diagram
low activity
-
-
?
ATP + 5-fluoro-2'-deoxyuridine
ADP + 5-fluoro-2'-deoxyuridine 5'-phosphate
show the reaction diagram
high activity
-
-
?
ATP + 9-beta-D-arabinofuranosyladenine
ADP + 9-beta-D-arabinofuranosyladenine 5'-phosphate
show the reaction diagram
very low activity
-
-
?
ATP + cytidine
ADP + cytidine 5'-phosphate
show the reaction diagram
very low activity
-
-
?
ATP + deoxyuridine
ADP + deoxyuridine 5'-phosphate
show the reaction diagram
high activity
-
-
?
ATP + uridine
ADP + uridine 5'-phosphate
show the reaction diagram
very low activity
-
-
?
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'-deoxycytidine
ADP + 2'-deoxycytidine 5'-phosphate
show the reaction diagram
-
-
-
?
ATP + 2'-deoxythymidine
ADP + 2'-deoxythymidine 5'-phosphate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dCTP
competitive versus ATP, feedback inhibition
dTTP
competitive versus ATP, feedback inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
2'-deoxyadenosine
-
0.031
2'-deoxycytidine
-
1.2
2'-deoxyguanosine
-
0.138
2'-deoxythymidine
-
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
putative
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8UVZ9_XENLA
278
0
31471
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26300
2 * 26300, recombinant enzyme, SDS-PAGE
46000
recombinant enzyme, native PAGE
49800
recombinant enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 26300, recombinant enzyme, SDS-PAGE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant full length and N-terminally truncated His-tagged enzymes, the His-tags are cleaved off
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression as full length and N-terminally truncated His-tagged enzymes in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Knecht, W.; Petersen, G.E.; Munch-Petersen, B.; Piskur, J.
Deoxyribonucleoside kinases belonging to the thymidine kinase 2 (TK2)-like group vary significantly in substrate specificity, kinetics and feed-back regulation
J. Mol. Biol.
315
529-540
2002
Drosophila melanogaster, Xenopus laevis (Q8UVZ9), Xenopus laevis, Bombyx mori (Q9BKL3), Bombyx mori
Manually annotated by BRENDA team