'NO-how' enzymatic S-nitrosylation controls insulin pathophysiology.

Trends Endocrinol Metab

Redox Biology, Danish Cancer Institute, Strandboulevarden 49, 2100, Copenhagen, Denmark; Department of Biology, Tor Vergata University, Via della Ricerca Scientifica, 00133, Rome, Italy. Electronic address:

Published: February 2024

Whether S-nitrosylation is the result of an unselective chemical process or enzymatically driven has been debated for years. A recent study by Zhou et al. identifies and characterizes the first S-nitroso-CoA (SNO-CoA)-assisted nitrosylase (SCAN) that catalyzes protein S-nitrosylation in mammals, including insulin receptor (INSR)/insulin receptor substrate 1 (IRS1), with implications for human metabolism.

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http://dx.doi.org/10.1016/j.tem.2024.02.010DOI Listing

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Similar Publications

'NO-how' enzymatic S-nitrosylation controls insulin pathophysiology.

Trends Endocrinol Metab

February 2024

Redox Biology, Danish Cancer Institute, Strandboulevarden 49, 2100, Copenhagen, Denmark; Department of Biology, Tor Vergata University, Via della Ricerca Scientifica, 00133, Rome, Italy. Electronic address:

Whether S-nitrosylation is the result of an unselective chemical process or enzymatically driven has been debated for years. A recent study by Zhou et al. identifies and characterizes the first S-nitroso-CoA (SNO-CoA)-assisted nitrosylase (SCAN) that catalyzes protein S-nitrosylation in mammals, including insulin receptor (INSR)/insulin receptor substrate 1 (IRS1), with implications for human metabolism.

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