Information on EC 2.7.1.76 - 2'-deoxyadenosine kinase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
2.7.1.76
-
RECOMMENDED NAME
GeneOntology No.
2'-deoxyadenosine kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + 2'-deoxyadenosine = ADP + dAMP
show the reaction diagram
-
-
-
-
ATP + 2'-deoxyadenosine = ADP + dAMP
show the reaction diagram
random sequential substrate addition
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
purine deoxyribonucleosides salvage
-
Purine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
ATP:2'-deoxyadenosine 5'-phosphotransferase
2'-Deoxyguanosine can also act as acceptor. Possibly identical with EC 2.7.1.74 deoxycytidine kinase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dAdo/dCyd kinase
-
-
dAK
Q0H0H5
-
dCyd kinase/dAdo kinase I
-
-
dCyd kinase/dAdo kinase I
Lactobacillus acidophilus R-26
-
-
-
deoxycytidine kinase/deoxyadenosine kinase, dCK/dAK
P0C1F9
-
deoxycytidine kinase/deoxyadenosine kinase, dCK/dAK
Lactobacillus acidophilus R-26
P0C1F9
-
-
deoxyguanosine kinase/deoxyadenosine kinase, dGK/dAK
P0C1F9
-
deoxyguanosine kinase/deoxyadenosine kinase, dGK/dAK
Lactobacillus acidophilus R-26
P0C1F9
-
-
dGuo kinase/dAdo kinase II
-
-
dGuo kinase/dAdo kinase II
Lactobacillus acidophilus R-26
-
-
-
purine-deoxyribonucleoside kinase
-
-
-
-
kinase, deoxyadenosine (phosphorylating)
-
-
-
-
additional information
-
may be identical with EC 2.7.1.113, i.e. deoxyguanosine kinase
additional information
-
enzyme may be identical with EC 2.7.1.20, i.e. adenosine kinase
additional information
-
enzyme may be identical with EC 2.7.1.20, i.e. adenosine kinase
CAS REGISTRY NUMBER
COMMENTARY
37278-12-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene yaaF, yaaF encodes an enzyme with specificity for deoxyadenosine and deoxycytidine
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
newborn
-
-
Manually annotated by BRENDA team
strain R-26
SwissProt
Manually annotated by BRENDA team
Lactobacillus acidophilus R-26
strain R-26
-
-
Manually annotated by BRENDA team
Lactobacillus acidophilus R-26
strain R-26
SwissProt
Manually annotated by BRENDA team
subspecies mycoides SC
-
-
Manually annotated by BRENDA team
subspecies Mycoplasma mycoides mycoides
-
-
Manually annotated by BRENDA team
subspecies Mycoplasma mycoides mycoides strain SC
-
-
Manually annotated by BRENDA team
-
Q0H0H0
UniProt
Manually annotated by BRENDA team
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2'-O-Cyclocytidine
-
activation
5-Fluoro-2'-deoxycytidine
-
0.4 mM, 275% activation of deoxyadenosine phosphorylation, half-maximal activation at 0.028 mM
cytosine arabinoside
-
activation
Deoxycytidine
-
30 mM, 584% activation of deoxyadenosine phosphorylation, half-maximal activation at 0.1 mM
deoxycytidine monophosphate
-
10 mM, 409% activation of deoxyadenosine phosphorylation, half-maximal activation at 1.6 mM
deoxyguanosine
P0C1F9
0.1 mM, 5fold activation of recombinant dAK
deoxyguanosine
-
5 mM, 330% activation of deoxyadenosine phosphorylation, half-maximal activation at 2.2 mM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26200
-
Q0H0H5
SDS-PAGE
50000
-
-
gel filtration
50000
-
-, Q93IG4
Superdex 75 column gel filtration
63000
-
-
gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
three-dimensional structural model based on crystal structure of Mycoplasma mycoides deoxyadenosine kinase
-, Q54YL2
in complex with deoxyadenosine 5'-triphosphate and 2'-deoxycytidine 5'-triphosphate, as well as with products 2'-deoxycytidine 5'-phosphate and 2'-deoxycytidine 5'-diphosphate. Both deoxyadenosine 5'-triphosphate and 2'-deoxycytidine 5'-triphosphate bind to the enzyme in a feedback-inhibitory manner with the deoxyribonucleoside part in the deoxyribonucleoside binding site and the triphosphates in the P-loop. Superposition with human counterparts deoxyguanosine kinase and deoxycytidine kinase. Overall structures are very similar with a few amino acid alterations in the proximity of the active site; sitting drop vapour diffusion method using 24% (w/v) PEG 3350 and 0.2 M KSCN
-, Q93IG4
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D78A
-
mutation on both subunits of dGK/dAK, 0.2% of wild-type dAK activity
D78E
-
mutation on both subunits of dGK/dAK, 0.2% of wild-type dAK activity
D78N
-
mutation on both subunits of dGK/dAK, 0.2% of wild-type dAK activity
D84A
-
mutation in dGK of dAK/dGK, increase of dAK activity
D84E
-
mutation in dGK of dAK/dGK, increase of dAK activity
D84N
-
mutation in dGK of dAK/dGK, increase of dAK activity
R79k
-
2 types of mutants, one bears the mutation on both the dAK and dGK subunits while the other, called R79K:dGK, has the mutation on the dGK subunit only, strong increase in dAK activity, activation of dAK by deoxyguanosine is nearly eliminated in the case of R79K:dGK, while for the tandem mutated R79K mutant a 30% inhibition is observed, inhibition by dATP is reduced