ArticlePloS one2018
Modulating D-amino acid oxidase (DAAO) substrate specificity through facilitated solvent access.
Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Effect of high hydrostatic pressure on D-amino acid oxidase activity and stability.Journal of biological engineering · 2026Article
- Review
- Dissecting in vivo and in vitro redox responses using chemogenetics.Free radical biology & medicine · 2021Review
- Application Fields, Positions, and Bioinformatic Mining of Non-active Sites: A Mini-Review.Frontiers in chemistry · 2021Review
- Proteins Structure Models in the Evaluation of Novel Variant (C.472_477del) in theDiagnostics (Basel, Switzerland) · 2020Article
- Dynamics, a Powerful Component of Current and Future in Silico Approaches for Protein Design and Engineering.International journal of molecular sciences · 2020Review
- Applications of water molecules for analysis of macromolecule properties.Computational and structural biotechnology journal · 2020Review
- A novel thermostable D-amino acid oxidase of the thermophilic fungus Rasamsonia emersonii strain YA.Scientific reports · 2019Article
- Distant Non-Obvious Mutations Influence the Activity of a HyperthermophilicBiomolecules · 2019Article
- ExploringBiomolecules · 2018Article
- Human D-Amino Acid Oxidase: Structure, Function, and Regulation.Frontiers in molecular biosciences · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
D-amino acid oxidase (DAAO) degrades D-amino acids to produce α-ketoacids, hydrogen peroxide and ammonia. DAAO has often been investigated and engineered for industrial and clinical applications. We combined information from literature with a detailed analysis of the structure to engineer mammalian DAAOs. The structural analysis was complemented with molecular dynamics simulations to characterize solvent accessibility and product release mechanisms. We identified non-obvious residues located on the loops on the border between the active site and the secondary binding pocket essential for pig and human DAAO substrate specificity and activity. We engineered DAAOs by mutating such critical residues and characterised the biochemical activity of the resulting variants. The results highlight the importance of the selected residues in modulating substrate specificity, product egress and enzyme activity, suggesting further steps of DAAO re-engineering towards desired clinical and industrial applications.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.