Ontology highlight
ABSTRACT:
SUBMITTER: Mustafa AK
PROVIDER: S-EPMC1815287 | biostudies-literature | 2007 Feb
REPOSITORIES: biostudies-literature
Mustafa Asif K AK Kumar Manish M Selvakumar Balakrishnan B Ho Gary P H GP Ehmsen Jeffrey T JT Barrow Roxanne K RK Amzel L Mario LM Snyder Solomon H SH
Proceedings of the National Academy of Sciences of the United States of America 20070209 8
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 ...[more]