Structural and functional characterization of a plant S-nitrosoglutathione reductase from Solanum lycopersicum

S-Nitrosoglutathione Reductase: A Key Regulator of S-Nitrosylation in Plant Development and Stress Responses

“…Recent advances in detailed biochemical and structural characterization of plant GSNOR enzymes confirmed their similarities to mammalian homologues (Crotty 2009;Kubienová et al 2013;Xu et al 2013). In comparison to human GSNOR, plant GSNORs exhibit a difference in the composition of the anion-binding pocket, which negatively influences the affinity for the carboxyl group of ω-hydroxyfatty acids (Kubienová et al 2013).…”

“…S-Nitrosoglutathione reductase activity of the plant enzyme shows similar kinetic and molecular properties as mammalian GSNOR (Sakamoto et al 2002;Crotty 2009;Kubienová et al 2013). Arabidopsis and tomato GSNOR exhibit 10-fold higher velocity of NADH-dependent GSNO reduction compared to HMGSH oxidation (Crotty 2009;Kubienová et al 2013).…”

“…In comparison to human GSNOR, plant GSNORs exhibit a difference in the composition of the anion-binding pocket, which negatively influences the affinity for the carboxyl group of ω-hydroxyfatty acids (Kubienová et al 2013). Plant GSNORs are also unusually cysteine-rich proteins, which suggested their possible regulation by post-translational modifications of several conserved cysteine residues exposed at the protein dimer surface (Xu et al 2013).…”

“…Arabidopsis and tomato GSNOR exhibit 10-fold higher velocity of NADH-dependent GSNO reduction compared to HMGSH oxidation (Crotty 2009;Kubienová et al 2013). Similarly to human GSNOR, fatty acids as substrate analogues show weak non-competitive inhibition of plant GSNOR, whereas GSH and S-methylglutathione were reported to non-competitively inhibit GSNO reduction in the millimolar range (Kubienová et al 2013). Several new potent pyrrole-based GSNOR inhibitors including the compound N6022 have been described for the human enzyme (Sun et al 2011).…”

“…The binding of N6022 includes an interaction of the propionic acid side chain of the inhibitor with all three residues forming the GSNOR anionic pocket (Green et al 2012). N6022 was found to inhibit tomato GSNOR at concentrations of 10 À7 M and thus represents an attractive tool for GSNOR inhibition studies in plants (Kubienová et al 2013). …”