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EC Number	Posttranslational Modification	Commentary	Reference
1.1.1.284	nitrosylation	GSNO reductase activity is regulated by posttranslational modification through S-nitrosylation under in vitro conditions which can be reversed by dithiothreitol	739889
1.1.1.284	nitrosylation	regulation of GSNOR activity through S-nitrosation of conserved cysteines is observed in Arabidopsis thaliana plants. Mono-, di-, and trinitrosation, which are confirmed by mass spectrometry, lead to subtle changes in enzyme conformation. GSNOR enzymatic activity, but not gene expression, is inhibited by the nitrogen assimilatory pathway via post-transcriptional S-nitrosation, preventing any scavenging of GSNO	763605
1.1.1.284	S-nitrosylation	the not Zn2+ chelating cysteine residues Cys10, Cys271 and Cys370 of Arabidopsis are targets for S-nitrosylation. Whereas modification of Cys370 seems to promote Snitrosylation of Cys10 and Cys271 by inducing conformational changes that alters the solvent accessibility and electrostatic environment of these cysteine residues. In detail, Snitrosylation of GSNOR slightly changes the solvent accessibility of amino acids from the substrate binding site and/or the dimer interface. Mass spectrometric analysis confirms the presence of monomeric and dimeric S-nitrosylated GSNOR, while unmodified GSNOR exists as dimers	763054

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Release 2023.1 (January 2023)