Nitric oxide S-nitrosylates serine racemase, mediating feedback inhibition of D-serine formation.
basic_science · Level V
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- Record sourced from PubMed, PMID 17293453.
- Also identified by PMC identifier 1815287.
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Abstract
Serine racemase (SR) generates D-serine, a coagonist with glutamate at NMDA receptors. We show that SR is physiologically S-nitrosylated leading to marked inhibition of enzyme activity. Inhibition involves interactions with the cofactor ATP reflecting juxtaposition of the ATP-binding site and cysteine-113 (C113), the site for physiological S-nitrosylation. NMDA receptor physiologically enhances SR S-nitrosylation by activating neuronal nitric-oxide synthase (nNOS). These findings support a model whereby postsynaptic stimulation of nitric-oxide (NO) formation feeds back to presynaptic cells to S-nitrosylate SR and decrease D-serine availability to postsynaptic NMDA receptors.
Medical subject headings
- Feedback, Physiological
- Nitric Oxide
- Racemases and Epimerases
- S-Nitrosoglutathione
- Serine