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Proc Natl Acad Sci U S A. 2007 Feb 20;104(8):2950-5. Epub 2007 Feb 9.

Nitric oxide S-nitrosylates serine racemase, mediating feedback inhibition of D-serine formation.

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1
Solomon H. Snyder Department of Neuroscience, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.

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.

PMID:
17293453
PMCID:
PMC1815287
DOI:
10.1073/pnas.0611620104
[Indexed for MEDLINE]
Free PMC Article
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