ArticleProtein science : a publication of the Protein Society2009
Relevance of weak flavin binding in human D-amino acid oxidase.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 46 citations in OpenAlex.
- Kynurenic Acid Synthesis from D-Kynurenine in the Cerebellum: A Distinct Role of D-Amino Acid Oxidase.Cells · 2025Article
- On the quaternary structure of human D-3-phosphoglycerate dehydrogenase.Protein science : a publication of the Protein Society · 2024Article
- Biochemical and Biophysical Characterization of Recombinant Human 3-Phosphoglycerate Dehydrogenase.International journal of molecular sciences · 2021Article
- Antimicrobial D-amino acid oxidase-derived peptides specify gut microbiota.Cellular and molecular life sciences : CMLS · 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
- Yin and Yang in Post-Translational Modifications of Human D-Amino Acid Oxidase.Frontiers in molecular biosciences · 2021Article
- Substitution of Arginine 120 in Human D-Amino Acid Oxidase Favors FAD-Binding and Nuclear Mistargeting.Frontiers in molecular biosciences · 2019Article
- Editorial: Bioscience of D-amino Acid Oxidase From Biochemistry to Pathophysiology.Frontiers in molecular biosciences · 2018Article
- Human D-Amino Acid Oxidase: Structure, Function, and Regulation.Frontiers in molecular biosciences · 2018Review
- Co-expression network analysis identified six hub genes in association with metastasis risk and prognosis in hepatocellular carcinoma.Oncotarget · 2017Article
- Biochemical Properties of Human D-Amino Acid Oxidase.Frontiers in molecular biosciences · 2017Article
- Competitive Inhibitors Unveil Structure/Function Relationships in Human D-Amino Acid Oxidase.Frontiers in molecular biosciences · 2017Review
- Controversial Effects of D-Amino Acid Oxidase Activator (DAOA)/G72 on D-Amino Acid Oxidase (DAO) Activity in Human Neuronal, Astrocyte and Kidney Cell Lines: The N-methyl D-aspartate (NMDA) Receptor Hypofunction Point of View.Frontiers in molecular neuroscience · 2017Article
- Expression of D-Amino Acid Oxidase (Frontiers in neuroanatomy · 2017Article
- Novel human D-amino acid oxidase inhibitors stabilize an active-site lid-open conformation.Bioscience reports · 2014Article
- Effect of ligand binding on human D-amino acid oxidase: implications for the development of new drugs for schizophrenia treatment.Protein science : a publication of the Protein Society · 2010Article
- Metabolism of the neuromodulator D-serine.Cellular and molecular life sciences : CMLS · 2010Review
- The neurobiology of D-amino acid oxidase and its involvement in schizophrenia.Molecular psychiatry · 2010Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the brain, the human flavoprotein D-amino acid oxidase (hDAAO) is involved in the degradation of the gliotransmitter D-serine, an important modulator of NMDA-receptor-mediated neurotransmission; an increase in hDAAO activity (that yields a decrease in D-serine concentration) was recently proposed to be among the molecular mechanisms leading to the onset of schizophrenia susceptibility. This human flavoenzyme is a stable homodimer (even in the apoprotein form) that distinguishes from known D-amino acid oxidases because it shows the weakest interaction with the flavin cofactor in the free form. Instead, cofactor binding is significantly tighter in the presence of an active site ligand. In order to understand how hDAAO activity is modulated, we investigated the FAD binding process to the apoprotein moiety and compared the folding and stability properties of the holoenzyme and the apoprotein forms. The apoprotein of hDAAO can be distinguished from the holoenzyme form by the more "open" tertiary structure, higher protein fluorescence, larger exposure of hydrophobic surfaces, and higher sensitivity to proteolysis. Interestingly, the FAD binding only slightly increases the stability of hDAAO to denaturation by urea or temperature. Taken together, these results indicate that the weak cofactor binding is not related to protein (de)stabilization or oligomerization (as instead observed for the homologous enzyme from yeast) but rather should represent a means of modulating the activity of hDAAO. We propose that the absence in vivo of an active site ligand/substrate weakens the cofactor binding, yielding the inactive apoprotein form and thus avoiding excessive D-serine degradation.
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