| First Author | De Miranda J | Year | 2000 |
| Journal | Gene | Volume | 256 |
| Issue | 1-2 | Pages | 183-8 |
| PubMed ID | 11054547 | Mgi Jnum | J:65488 |
| Mgi Id | MGI:1926659 | Doi | 10.1016/s0378-1119(00)00356-5 |
| Citation | De Miranda J, et al. (2000) Human serine racemase: moleular cloning, genomic organization and functional analysis. Gene 256(1-2):183-8 |
| abstractText | High levels of D-serine are found in mammalian brain, where it is an endogenous agonist of the strichinine-insensitive site of N-methyl D-aspartate type of glutamate receptors. D-serine is enriched in protoplasmic astrocytes that occur in gray matter areas of the brain and was shown to be synthesized from L-serine. We now report cloning and expression of human serine racemase, an enzyme that catalyses the synthesis of D-serine from L-serine. The enzyme displays a high homology to the murine serine racemase. It contains a pyridoxal 5'-phosphate attachment sequence similar to bacterial biosynthetic threonine dehydratase. Northern-blot analysis show high levels of human serine racemase in areas known to contain large amounts of endogenous D-serine, such as hippocampus and corpus callosum. Robust synthesis of D-serine was detected in cells transfected with human serine racemase, demonstrating the conservation of D-amino acid metabolism in humans. Serine racemase may be a therapeutic target in psychiatric diseases as supplementation of D-serine greatly improves schizophrenia symptoms. We identify the human serine racemase genomic structure and show that the gene encompasses seven exons and localizes to chromosome 17q13.3. Identification of the intron-exon boundaries of the human serine racemase gene will be useful to search for mutations in neuropsychiatric disorders. |
