Geller, A.M. (Arthur M.)
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- Creation of a functional S-nitrosylation site in vitro by single point mutation(Elsevier, 1999) Corrales, F.J. (Fernando José); Perez-Mato, I. (Isabel); Sanchez-del-Pino, M.M. (Manuel M.); Ruiz, F.A. (Félix A.); Kotb, M. (Malak); Castro, C. (Carmen); LeGros, L. (Leighton); Mato, J.M. (José María); Geller, A.M. (Arthur M.)Here we show that in extrahepatic methionine adenosyltransferase replacement of a single amino acid (glycine 120) by cysteine is sufficient to create a functional nitric oxide binding site without affecting the kinetic properties of the enzyme. When wild-type and mutant methionine adenosyltransferase were incubated with S-nitrosoglutathione the activity of the wild-type remained unchanged whereas the activity of the mutant enzyme decreased markedly. The mutant enzyme was found to be S-nitrosylated upon incubation with the nitric oxide donor. Treatment of the S-nitrosylated mutant enzyme with glutathione removed most of the S-nitrosothiol groups and restored the activity to control values. In conclusion, our results suggest that functional S-nitrosylation sites can develop from existing structures without drastic or large-scale amino acid replacements