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Thioredoxin Trx -related proteins, including Trx1 and 2 in mammals, catalyze the direct denitrosylation of S-nitrosoproteins [22] [23] [24]. The redox-based chemical mechanisms for S-nitrosylation in biological systems were also described concomitantly [13].

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Aberrant S-nitrosylation following stimulation of the NMDA receptor would come to serve as a prototypic example of the involvement of S-nitrosylation in disease [16]. Jump to navigation Jump to search S-Nitrosylation, the covalent attachment of NO to a cysteine residue to form an S-nitrosothiol SNOis a post-translational protein modification of broad purview across phylogeny and cell types.

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Important examples of proteins whose activities were subsequently shown to be regulated by S-nitrosylation include the NMDA-type glutamate receptor in the brain [14] [15]. Multiple enzymes have been described to date, which fall into two main classes mediating denitrosylation of protein and low molecular weight SNOs, respectively.

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Biology of Nitric Oxide. The enzyme is highly conserved from bacteria to humans. Aberrant S-nitrosylation and denitrosylation has been implicated in multiple diseases including heart disease, cancer and asthma [25] [26] [27] as well as neurological disorders, including stroke [28]chronic degenerative diseases e.

S-nitrosylation is precisely targeted, [2] reversible, [3] spatiotemporally restricted [4] [5] and necessary for a wide range of cellular responses, [6] including the prototypic example of red blood cell mediated autoregulation of blood flow that is essential for vertebrate life [7].

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It operates as a fundamental mechanism for cellular signaling and accounts for the large part of NO bioactivity. S-Nitrosylation is now established as ubiquitous in biology, having been demonstrated to occur in all phylogenetic kingdoms [17] [18] and has been described as the prototypic redox-based signalling mechanism, [19] hypothesized to have evolved on primordial Earth.

Although originally thought to involve multiple chemical routes in vivo, accumulating evidence suggests that S-nitrosylation depends on enzymatic activity, entailing three classes of enzymes S-nitrosylases that operate in concert to conjugate NO to proteins, drawing analogy to ubiquitinylation.

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