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The allosteric interplay between S‐nitrosylation and glycine binding controls the activity of human serine racemase
Author(s) -
Marchesani Francesco,
Gianquinto Eleonora,
Autiero Ida,
Michielon Annalisa,
Campanini Barbara,
Faggiano Serena,
Bettati Stefano,
Mozzarelli Andrea,
Spyrakis Francesca,
Bruno Stefano
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15645
Subject(s) - allosteric regulation , s nitrosylation , chemistry , serine , nitrosylation , stereochemistry , glycine , cysteine , biochemistry , enzyme , amino acid , nitric oxide , organic chemistry
Serine racemase is the enzyme responsible for the synthesis of the neuromodulator D‐serine in neurons. ATP allosterically activates the enzyme, whereas S‐nitrosylation at a specific cysteine residue inhibits it. Here, we show that S‐nitrosylation occurs only in the presence of ATP and produces a conformational rearrangement toward a more open and less active structure. Ligand binding at the active site prevents nitrosylation.