AUTHOR=Sacchi Silvia , Cappelletti Pamela , Murtas Giulia TITLE=Biochemical Properties of Human D-amino Acid Oxidase Variants and Their Potential Significance in Pathologies JOURNAL=Frontiers in Molecular Biosciences VOLUME=5 YEAR=2018 URL=https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2018.00055 DOI=10.3389/fmolb.2018.00055 ISSN=2296-889X ABSTRACT=
The stereoselective flavoenzyme D-amino acid oxidase (DAAO) catalyzes the oxidative deamination of neutral and polar D-amino acids producing the corresponding α-keto acids, ammonia, and hydrogen peroxide. Despite its peculiar and atypical substrates, DAAO is widespread expressed in most eukaryotic organisms. In mammals (and humans in particular), DAAO is involved in relevant physiological processes ranging from D-amino acid detoxification in kidney to neurotransmission in the central nervous system, where DAAO is responsible of the catabolism of D-serine, a key endogenous co-agonist of N-methyl-D-aspartate receptors. Recently, structural and functional studies have brought to the fore the distinctive biochemical properties of human DAAO (hDAAO). It appears to have evolved to allow a strict regulation of its activity, so that the enzyme can finely control the concentration of substrates (such as D-serine in the brain) without yielding to an excessive production of hydrogen peroxide, a potentially toxic reactive oxygen species (ROS). Indeed, dysregulation in D-serine metabolism, likely resulting from altered levels of hDAAO expression and activity, has been implicated in several pathologies, ranging from renal disease to neurological, neurodegenerative, and psychiatric disorders. Only one mutation in