Full metadata record
DC Field | Value | Language |
---|---|---|
dc.creator | Castro, C. (Carmen) | - |
dc.creator | Ruiz, F.A. (Félix A.) | - |
dc.creator | Perez-Mato, I. (Isabel) | - |
dc.creator | Sanchez-del-Pino, M.M. (Manuel M.) | - |
dc.creator | LeGros, L. (Leighton) | - |
dc.creator | Geller, A.M. (Arthur M.) | - |
dc.creator | Kotb, M. (Malak) | - |
dc.creator | Corrales, F.J. (Fernando José) | - |
dc.creator | Mato, J.M. (José María) | - |
dc.date.accessioned | 2012-03-28T13:48:22Z | - |
dc.date.available | 2012-03-28T13:48:22Z | - |
dc.date.issued | 1999 | - |
dc.identifier.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. | es_ES |
dc.identifier.issn | 1873-3468 | - |
dc.identifier.uri | https://hdl.handle.net/10171/21385 | - |
dc.description.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 | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Elsevier | es_ES |
dc.rights | info:eu-repo/semantics/openAccess | es_ES |
dc.subject | Methionine adenosyltransferase | es_ES |
dc.subject | S-Nitrosylation | es_ES |
dc.title | Creation of a functional S-nitrosylation site in vitro by single point mutation | es_ES |
dc.type | info:eu-repo/semantics/article | es_ES |
dc.relation.publisherversion | http://www.sciencedirect.com/science/article/pii/S0014579399012673 | es_ES |
dc.type.driver | info:eu-repo/semantics/article | es_ES |
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