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Literature summary for 2.7.1.145 extracted from

  • Johansson, K.; Ramaswamy, S.; Ljungcrantz, C.; Knecht, W.; Piskur, J.; Munch-Petersen, B.; Eriksson, S.; Eklund, H.
    Structural basis for substrate specificities of cellular deoxyribonucleoside kinases (2001), Nat. Struct. Biol., 8, 616-620.
    View publication on PubMed
Search for more literature for 2.7.1.145

Application

Application Comment Organism
medicine the enzyme activates a number of medically important nucleoside analogues Drosophila melanogaster

Crystallization (Commentary)

Crystallization (Comment) Organism
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

General Stability Organism
ATP stabilizes the enzyme structure Drosophila melanogaster

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Drosophila melanogaster

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster Q9XZT6
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + a 2'-deoxyribonucleoside = ADP + a 2'-deoxyribonucleoside 5'-phosphate substrate binding and interactions Drosophila melanogaster
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2'-deoxycytidine
-
 Drosophila melanogaster ADP + 2'-deoxycytidine 5'-phosphate
-
 ?
additional information the enzyme shows broad substrate specificity probably due to a wide substrate binding cleft Drosophila melanogaster ?
-
 ?

Synonyms

Synonyms Comment Organism
dNK
-
 Drosophila melanogaster

Cofactor

Cofactor Comment Organism Structure
ATP stabilizes the enzyme structure, binding structure, Q111 and Arg118 are involved Drosophila melanogaster