|
type |
Journal Article |
authors |
Wolosker, H.; Blackshaw, S.; Snyder, S. H. |
title |
Serine racemase: a glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission |
journal |
Proc Natl Acad Sci U S A |
Activity |
5.1.1.18 |
sel |
selected |
ui |
10557334 |
year |
(1999) |
volume |
96 |
number |
23 |
pages |
13409-14 |
| |
keywords |
Amino Acid Sequence |
abstract |
Although D amino acids are prominent in bacteria, they generally are thought not to occur in mammals. Recently, high levels of D-serine have been found in mammalian brain where it activates glutamate/N-methyl-D- aspartate receptors by interacting with the "glycine site" of the receptor. Because amino acid racemases are thought to be restricted to bacteria and insects, the origin of D-serine in mammals has been puzzling. We now report cloning and expression of serine racemase, an enzyme catalyzing the formation of D-serine from L-serine. Serine racemase is a protein representing an additional family of pyridoxal-5' phosphate-dependent enzymes in eukaryotes. The enzyme is enriched in rat brain where it occurs in glial cells that possess high levels of D- serine in vivo. Occurrence of serine racemase in the brain demonstrates the conservation of D-amino acid metabolism in mammals with implications for the regulation of N-methyl-D-aspartate neurotransmission through glia-neuronal interactions. |
last changed |
2009/07/03 14:46 |
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