BRENDA - Enzyme Database show

Structural basis for substrate specificities of cellular deoxyribonucleoside kinases

Johansson, K.; Ramaswamy, S.; Ljungcrantz, C.; Knecht, W.; Piskur, J.; Munch-Petersen, B.; Eriksson, S.; Eklund, H.; Nat. Struct. Biol. 8, 616-620 (2001)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
2.7.1.113
medicine
the enzyme activates a number of medically important nucleoside analogues
Homo sapiens
2.7.1.145
medicine
the enzyme activates a number of medically important nucleoside analogues
Drosophila melanogaster
Crystallization (Commentary)
EC Number
Crystallization
Organism
2.7.1.113
purified recombinant enzyme, hanging drop vapour diffusion method, enzyme solution containing 7 mg/ml protein, 5 mM MgCl2, and 5 mM ATP, mixed with an equal volume of cyrstallization solution containing 0.1 M Na-citrate, pH 6.5, 0.2 M ammonium acetate, and 30% w/v PEG 4000, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement method
Homo sapiens
2.7.1.145
purified recombinant enzyme, hanging drop vapour diffusion method, enzyme solution containing 10 mg/ml protein and 10 mM deoxycytidine, mixed with an equal volume of cyrstallization solution containing 0.1 M MES, pH 6.5, 0.2 M ammonium sulfate, 20% w/v PEG 5000, and 8-10% v/v PEG 400, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement method
Drosophila melanogaster
General Stability
EC Number
General Stability
Organism
2.7.1.145
ATP stabilizes the enzyme structure
Drosophila melanogaster
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
2.7.1.113
Mg2+
-
Homo sapiens
2.7.1.145
Mg2+
-
Drosophila melanogaster
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.7.1.113
Homo sapiens
Q16854
-
-
2.7.1.145
Drosophila melanogaster
Q9XZT6
-
-
Reaction
EC Number
Reaction
Commentary
Organism
2.7.1.113
ATP + deoxyguanosine = ADP + dGMP
substrate interactions and binding mechanism, and active site structure
Homo sapiens
2.7.1.145
ATP + a 2'-deoxyribonucleoside = ADP + a 2'-deoxyribonucleoside 5'-phosphate
substrate binding and interactions
Drosophila melanogaster
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.7.1.113
ATP + 2'-deoxyguanosine
-
662932
Homo sapiens
ADP + 2'-deoxyguanosine 5'-phosphate
-
-
-
?
2.7.1.113
additional information
the enzyme is highly specific for purine substrates, Arg118 is responsible for the substrate specificity
662932
Homo sapiens
?
-
-
-
-
2.7.1.145
ATP + 2'-deoxycytidine
-
662932
Drosophila melanogaster
ADP + 2'-deoxycytidine 5'-phosphate
-
-
-
?
2.7.1.145
additional information
the enzyme shows broad substrate specificity probably due to a wide substrate binding cleft
662932
Drosophila melanogaster
?
-
-
-
-
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
2.7.1.113
ATP
-
Homo sapiens
2.7.1.145
ATP
stabilizes the enzyme structure, binding structure, Q111 and Arg118 are involved
Drosophila melanogaster
Application (protein specific)
EC Number
Application
Commentary
Organism
2.7.1.113
medicine
the enzyme activates a number of medically important nucleoside analogues
Homo sapiens
2.7.1.145
medicine
the enzyme activates a number of medically important nucleoside analogues
Drosophila melanogaster
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
2.7.1.113
ATP
-
Homo sapiens
2.7.1.145
ATP
stabilizes the enzyme structure, binding structure, Q111 and Arg118 are involved
Drosophila melanogaster
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
2.7.1.113
purified recombinant enzyme, hanging drop vapour diffusion method, enzyme solution containing 7 mg/ml protein, 5 mM MgCl2, and 5 mM ATP, mixed with an equal volume of cyrstallization solution containing 0.1 M Na-citrate, pH 6.5, 0.2 M ammonium acetate, and 30% w/v PEG 4000, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement method
Homo sapiens
2.7.1.145
purified recombinant enzyme, hanging drop vapour diffusion method, enzyme solution containing 10 mg/ml protein and 10 mM deoxycytidine, mixed with an equal volume of cyrstallization solution containing 0.1 M MES, pH 6.5, 0.2 M ammonium sulfate, 20% w/v PEG 5000, and 8-10% v/v PEG 400, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement method
Drosophila melanogaster
General Stability (protein specific)
EC Number
General Stability
Organism
2.7.1.145
ATP stabilizes the enzyme structure
Drosophila melanogaster
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
2.7.1.113
Mg2+
-
Homo sapiens
2.7.1.145
Mg2+
-
Drosophila melanogaster
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.7.1.113
ATP + 2'-deoxyguanosine
-
662932
Homo sapiens
ADP + 2'-deoxyguanosine 5'-phosphate
-
-
-
?
2.7.1.113
additional information
the enzyme is highly specific for purine substrates, Arg118 is responsible for the substrate specificity
662932
Homo sapiens
?
-
-
-
-
2.7.1.145
ATP + 2'-deoxycytidine
-
662932
Drosophila melanogaster
ADP + 2'-deoxycytidine 5'-phosphate
-
-
-
?
2.7.1.145
additional information
the enzyme shows broad substrate specificity probably due to a wide substrate binding cleft
662932
Drosophila melanogaster
?
-
-
-
-