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B6db references: 11054547

type Journal Article
authors De Miranda, J.; Santoro, A.; Engelender, S.; Wolosker, H.
title Human serine racemase: moleular cloning, genomic organization and functional analysis
journal Gene
Activity 5.1.1.18
sel selected
ui 11054547
year (2000)
volume 256
number 1-2
pages 183-8
 
keywords Amino Acid Sequence
abstract 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.
last changed 2009/07/03 14:48

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