Title : Mechanism of Sirt1 NAD+-dependent Protein Deacetylase Inhibition by Cysteine S-Nitrosation.

Pub. Date : 2016 Dec 2

PMID : 27756843






2 Functional Relationships(s)
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1 Steady-state kinetic analyses and binding assays were consistent with Sirt1 S-nitrosation inhibiting binding of both the NAD+ and acetyl-lysine substrates. N(alpha)-acetyllysine sirtuin 1 Homo sapiens
2 Molecular dynamics simulations suggested that Zn2+ loss due to Sirt1 S-nitrosation results in repositioning of the tetrathiolate subdomain away from the rest of the catalytic domain, thereby disrupting the NAD+ and acetyl-lysine-binding sites. N(alpha)-acetyllysine sirtuin 1 Homo sapiens