Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification of residues involved in the specificity and regulation of the highly efficient multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster.

Journal of molecular biology - 25 Aug 2000

Knecht W, Munch-Petersen B, Piskur J

Abstract excerpt

In contrast to all known deoxyribonucleoside kinases, a single highly efficient deoxyribonucleoside kinase from Drosophila melanogaster (Dm-dNK) is able to phosphorylate all precursor nucleosides for DNA synthesis. Dm-dNK was mutated in vitro by high-frequency random mutagenesis, expressed in the thymidine kinase-deficient Escherichia coli strain KY895 and clones were selected for sensitivity to the nucleoside...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cytarabine
Share to Directed Molecular Evolution

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Feedback

Share to Inhibitory Concentration 50

Share to Thymidine

Share to Thymine Nucleotides

Share to Zalcitabine

Share to Zidovudine

Source

Identifiers

PMID: 10966789
DOI: 10.1006/jmbi.2000.3990

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of residues involved in the specificity and regulation of the highly efficient multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster.PMID 10966789Read ↗

Drosophila deoxyribonucleoside kinase mutants with enhanced ability to phosphorylate purine analogs.Semantic proximity Read ↗

Structural basis for the changed substrate specificity of Drosophila melanogaster deoxyribonucleoside kinase mutant N64D.Semantic proximity Read ↗

A Single Deoxynucleoside Kinase Variant from Drosophila melanogaster Synthesizes Monophosphates of Nucleosides That Are Components of an Expanded Genetic System.Semantic proximity Read ↗

Four Deoxynucleoside Kinase Activities from Drosophila melanogaster Are Contained within a Single Monomeric Enzyme, a New Multifunctional Deoxynucleoside KinaseSemantic proximity Read ↗

Investigation of the substrate recognition of Drosophila melanogaster nucleoside kinase by site directed mutagenesis.Semantic proximity Read ↗

In vivo analysis of Drosophila deoxyribonucleoside kinase function in cell cycle, cell survival and anti-cancer drugs resistance.Semantic proximity Read ↗

Systematic exploration of active site mutations on human deoxycytidine kinase substrate specificity.Semantic proximity Read ↗

Modifying Human Thymidylate Kinase to Potentiate Azidothymidine ActivationSemantic proximity Read ↗

Creation of drug-specific herpes simplex virus type 1 thymidine kinase mutants for gene therapy.Semantic proximity Read ↗

Potent anticancer effects of lentivirus encoding a Drosophila melanogaster deoxyribonucleoside kinase mutant combined with brivudine.Semantic proximity Read ↗

Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase.Semantic proximity Read ↗

Structural and Kinetic Characterization of Human Deoxycytidine Kinase Variants Able To Phosphorylate 5-Substituted Deoxycytidine and Thymidine Analogues,Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.