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• W2143064821 endingPage "964" @default.
• W2143064821 startingPage "943" @default.
• W2143064821 abstract "The N –methyl D–aspartate (NMDA) type of glutamate receptor requires two distinct agonists to operate. Glycine is assumed to be the endogenous ligand for the NMDA receptor glycine site, but this notion has been challenged by the discovery of high levels of endogenous D–serine in the mammalian forebrain. I have outlined an evolutionary framework for the appearance of a glycine site in animals and the metabolic events leading to high levels of D–serine in brain. Sequence alignments of the glycine–binding regions, along with the scant experimental data available, suggest that the properties of invertebrate NMDA receptor glycine sites are probably different from those in vertebrates. The synthesis of D–serine in brain is due to a pyridoxal–5'–phosphate (B 6 )–requiring serine racemase in glia. Although it remains unknown when serine racemase first evolved, data concerning the evolution of B 6 enzymes, along with the known occurrences of serine racemases in animals, point to D–serine synthesis arising around the divergence time of arthropods. D–Serine catabolism occurs via the ancient peroxisomal enzyme D–amino acid oxidase (DAO), whose ontogenetic expression in the hindbrain of mammals is delayed until the postnatal period and absent from the forebrain. The phylogeny of D–serine metabolism has relevance to our understanding of brain ontogeny, schizophrenia and neurotransmitter dynamics." @default.
• W2143064821 created "2016-06-24" @default.
• W2143064821 creator A5061312918 @default.
• W2143064821 date "2004-06-29" @default.
• W2143064821 modified "2023-10-14" @default.
• W2143064821 title "The<i>N</i>–methyl D–aspartate receptor glycine site and D–serine metabolism: an evolutionary perspective" @default.
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