ArticleProtein science : a publication of the Protein Society2010
Effect of ligand binding on human D-amino acid oxidase: implications for the development of new drugs for schizophrenia treatment.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 55 citations in OpenAlex.
- Blood levels of D-aspartate oxidase, D-amino acid oxidase, serine racemase, and pLG72 are influenced by diagnoses of schizophrenia and autism spectrum disorder.Schizophrenia (Heidelberg, Germany) · 2026Article
- Post-translational regulation of human D-3-phosphoglycerate dehydrogenase in Alzheimer's disease.Protein science : a publication of the Protein Society · 2026Article
- Impact of D-Amino Acids in Schizophrenia.Biomolecules · 2025Review
- Prenatal Exposure to Lipopolysaccharide or Valproate Leads to Abnormal Accumulation of the NMDA Receptor Agonist D-Aspartate in the Adolescent Rat Brain.Journal of neurochemistry · 2025Article
- On the quaternary structure of human D-3-phosphoglycerate dehydrogenase.Protein science : a publication of the Protein Society · 2024Article
- Unveiling the Bio-corona Fingerprinting of Potential Anticancer Carbon Nanotubes Coupled with D-Amino Acid Oxidase.Molecular biotechnology · 2022Article
- Biochemical Properties and Physiological Functions of pLG72: Twenty Years of Investigations.Biomolecules · 2022Review
- Sodium Benzoate-Harmfulness and Potential Use in Therapies for Disorders Related to the Nervous System: A Review.Nutrients · 2022Review
- An Efficient Protein Evolution Workflow for the Improvement of Bacterial PET Hydrolyzing Enzymes.International journal of molecular sciences · 2021Article
- d-Amino Acids and pLG72 in Alzheimer's Disease and Schizophrenia.International journal of molecular sciences · 2021Review
- Biochemical and Biophysical Characterization of Recombinant Human 3-Phosphoglycerate Dehydrogenase.International journal of molecular sciences · 2021Article
- Yin and Yang in Post-Translational Modifications of Human D-Amino Acid Oxidase.Frontiers in molecular biosciences · 2021Article
- Human D-aspartate Oxidase: A Key Player in D-aspartate Metabolism.Frontiers in molecular biosciences · 2021Article
- Directly and Indirectly Targeting the Glycine Modulatory Site to Modulate NMDA Receptor Function to Address Unmet Medical Needs of Patients With Schizophrenia.Frontiers in psychiatry · 2021Review
- Substitution of Arginine 120 in Human D-Amino Acid Oxidase Favors FAD-Binding and Nuclear Mistargeting.Frontiers in molecular biosciences · 2019Article
- D-Serine: Potential Therapeutic Agent and/or Biomarker in Schizophrenia and Depression?Frontiers in psychiatry · 2019Review
- D-Amino Acid Oxidase-pLG72 Interaction and D-Serine Modulation.Frontiers in molecular biosciences · 2018Review
- Human D-Amino Acid Oxidase: Structure, Function, and Regulation.Frontiers in molecular biosciences · 2018Review
- Biochemical Properties of Human D-amino Acid Oxidase Variants and Their Potential Significance in Pathologies.Frontiers in molecular biosciences · 2018Review
- Competitive Inhibitors Unveil Structure/Function Relationships in Human D-Amino Acid Oxidase.Frontiers in molecular biosciences · 2017Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In human brain the flavoprotein D-amino acid oxidase (hDAAO) is responsible for the degradation of the neuromodulator D-serine, an important effector of NMDA-receptor mediated neurotransmission. Experimental evidence supports the concept that D-serine concentration increase by hDAAO inhibition may represent a valuable therapeutic approach to improve the symptoms in schizophrenia patients. This study investigated the effects on hDAAO conformation and stability of the substrate D-serine (or of the pseudo-substrate trifluoro-D-alanine), the FAD cofactor, and two inhibitors (benzoate, a classical substrate-competitive inhibitor and the drug chlorpromazine (CPZ), which competes with the cofactor). We demonstrated that all these compounds do not alter the interaction of hDAAO with its physiological partner pLG72. The ligands used affect the tertiary structure of hDAAO differently: benzoate or trifluoro-D-alanine binding increases the amount of the holoenzyme form in solution and stabilizes the flavoprotein, while CPZ binding favors a protein conformation resembling that of the apoprotein, which is more sensitive to degradation. Interestingly, the apoprotein form of hDAAO binds the substrate D-serine: this interaction increases FAD binding thus increasing the amount of active holoenzyme in solution. Benzoate and CPZ similarly modify the short-term cellular D-serine concentration but affect the cellular concentration of hDAAO differently. In conclusion, the different alteration of hDAAO conformation and stability by the ligands used represents a further parameter to take into consideration during the development of new drugs to cope schizophrenia.
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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.