| First Author | Mustafa AK | Year | 2007 |
| Journal | Proc Natl Acad Sci U S A | Volume | 104 |
| Issue | 8 | Pages | 2950-5 |
| PubMed ID | 17293453 | Mgi Jnum | J:125938 |
| Mgi Id | MGI:3760217 | Doi | 10.1073/pnas.0611620104 |
| Citation | Mustafa AK, et al. (2007) Nitric oxide S-nitrosylates serine racemase, mediating feedback inhibition of D-serine formation. Proc Natl Acad Sci U S A 104(8):2950-5 |
| abstractText | 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. |
