Creation of a functional S-nitrosylation site in vitro by single point mutation
Keywords: 
Methionine adenosyltransferase
S-Nitrosylation
Issue Date: 
1999
Publisher: 
Elsevier
ISSN: 
1873-3468
Citation: 
Castro C, Ruiz FA, Perez-Mato I, Sanchez del Pino MM, LeGros L, Geller AM, et al. Creation of a functional S-nitrosylation site in vitro by single point mutation. FEBS Lett 1999 Oct 15;459(3):319-322.
Abstract
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

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