|
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 |
Family |
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 |
2016/10/06 17:12 |
|