Article
Structural basis for the changed substrate specificity of Drosophila melanogaster deoxyribonucleoside kinase mutant N64D.
The FEBS journal - 1 Jul 2005
Welin Martin, Skovgaard Tine, Knecht Wolfgang, Zhu Chunying, Berenstein Dvora, Munch-Petersen Birgitte, Piskur Jure, Eklund Hans
Abstract excerpt
The Drosophila melanogaster deoxyribonucleoside kinase (Dm-dNK) double mutant N45D/N64D was identified during a previous directed evolution study. This mutant enzyme had a decreased activity towards the natural substrates and decreased feedback inhibition with dTTP, whereas the activity with 3'-modified nucleoside analogs like 3'-azidothymidine (AZT) was nearly unchanged. Here, we identify the mutation N64D as...
Topics
- Animals
- Asparagine
- Aspartic Acid
- Crystallography, X-Ray
- Drosophila melanogaster
- Kinetics
- Models, Molecular
- Mutation
- Phosphotransferases (Alcohol Group Acceptor)
- Protein Structure, Tertiary
- Substrate Specificity
- Thymine Nucleotides
