| Literature DB >> 17293453 |
Asif K Mustafa1, Manish Kumar, Balakrishnan Selvakumar, Gary P H Ho, Jeffrey T Ehmsen, Roxanne K Barrow, L Mario Amzel, Solomon H Snyder.
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.Entities:
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Year: 2007 PMID: 17293453 PMCID: PMC1815287 DOI: 10.1073/pnas.0611620104
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205