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

Optimization of D-amino acid oxidase for low substrate concentrations--towards a cancer enzyme therapy.

The FEBS journal - 1 Sept 2009

Rosini Elena, Pollegioni Loredano, Ghisla Sandro, Orru Roberto, Molla Gianluca

Abstract excerpt

D-amino acid oxidase (DAAO) has recently become of interest as a biocatalyst for industrial applications and for therapeutic treatments. It has been used in gene-directed enzyme prodrug therapies, in which its production of H2O2 in tumor cells can be regulated by administration of substrate. This approach is limited by the locally low O2 concentration and the high K(m) for this substrate. Using the directed...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Antineoplastic Agents
Share to Drug Screening Assays, Antitumor

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fungal Proteins

Share to Hydrogen Peroxide

Share to Kinetics

Share to Oxygen

Share to Substrate Specificity

Source

Identifiers

PMID: 19694805
DOI: 10.1111/j.1742-4658.2009.07191.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Optimization of D-amino acid oxidase for low substrate concentrations--towards a cancer enzyme therapy.PMID 19694805Read ↗

Engineering the substrate specificity of D-amino-acid oxidase.Semantic proximity Read ↗

Modulating D-amino acid oxidase substrate specificity: production of an enzyme for analytical determination of all D-amino acids by directed evolution.Semantic proximity Read ↗

Direct quantification of chemogenetic H <sub>2</sub> O <sub>2</sub> production in live human cellsSemantic proximity Read ↗

Structure-function relationships in human d-amino acid oxidase variants corresponding to known SNPs.Semantic proximity Read ↗

Selective reduction in glutaminase activity of l‑Asparaginase by asparagine 248 to serine mutation: A combined computational and experimental effort in blood cancer treatment.Semantic proximity Read ↗

Through virtual saturation mutagenesis and rational design for superior substrate conversion in engineered d-amino acid oxidase.Semantic proximity Read ↗

Engineering d-Lactate Dehydrogenase to Favor an Non-natural Cofactor Nicotinamide Cytosine Dinucleotide.Semantic proximity Read ↗

Tuning Enzyme Activity for Nonaqueous Solvents: Engineering an Enantioselective "Michaelase" for Catalysis in High Concentrations of Ethanol.Semantic proximity Read ↗

Homologous recombination repair-dependent cytotoxicity of the benzotriazine di-N-oxide CEN-209: comparison with other hypoxia-activated prodrugs.Semantic proximity Read ↗

Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action.Semantic proximity Read ↗

Directed evolution of an amine oxidase possessing both broad substrate specificity and high enantioselectivity.Semantic proximity Read ↗

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

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