Allosteric inhibition of carnosinase (CN1) by inducing a conformational shift

In humans, low serum carnosinase (CN1) activity protects patients with type 2 diabetes from diabetic nephropathy. We now characterized the interaction of thiol-containing compounds with CN1 cysteine residue at position 102, which is important for CN1 activity. Reduced glutathione (GSH), N-acetylcyst...

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Veröffentlicht in:	Journal of enzyme inhibition and medicinal chemistry 2017-01, Vol.32 (1), p.1102-1110
Hauptverfasser:	Peters, Verena, Schmitt, Claus P., Weigand, Tim, Klingbeil, Kristina, Thiel, Christian, van den Berg, Antje, Calabrese, Vittorio, Nawroth, Peter, Fleming, Thomas, Forsberg, Elisabete, Wagner, Andreas H., Hecker, Markus, Vistoli, Giulio
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylcysteine allosteric inhibition Allosteric properties Allosteric Regulation - drug effects Ammonium Carnosinase 1 activity Carnosine CN1 Cysteine Diabetes Diabetes mellitus (non-insulin dependent) Diabetic nephropathy Dipeptidases - antagonists & inhibitors Dipeptidases - metabolism Enzyme Inhibitors - chemistry Enzyme Inhibitors - pharmacology Glutathione Humans Medicin och hälsovetenskap Molecular Conformation Molecular Dynamics Simulation N-acetylcysteine Nephropathy Research Paper Sulfhydryl Compounds - chemistry Sulfhydryl Compounds - pharmacology
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Zusammenfassung:	In humans, low serum carnosinase (CN1) activity protects patients with type 2 diabetes from diabetic nephropathy. We now characterized the interaction of thiol-containing compounds with CN1 cysteine residue at position 102, which is important for CN1 activity. Reduced glutathione (GSH), N-acetylcysteine and cysteine (3.2 ± 0.4, 2.0 ± 0.3, 1.6 ± 0.2 µmol/mg/h/mM; p
ISSN:	1475-6366 1475-6374 1475-6374
DOI:	10.1080/14756366.2017.1355793