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

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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Bibliographic Details
Main Authors: Verena Peters, Claus P. Schmitt, Tim Weigand, Kristina Klingbeil, Christian Thiel, Antje van den Berg, Vittorio Calabrese, Peter Nawroth, Thomas Fleming, Elisabete Forsberg, Andreas H. Wagner, Markus Hecker, Giulio Vistoli
Format: Article
Language:English
Published: Taylor & Francis Group 2017-01-01
Series:Journal of Enzyme Inhibition and Medicinal Chemistry
Subjects:
Carnosinase 1 activity
CN1
allosteric inhibition
glutathione
N-acetylcysteine
diabetes
Online Access:http://dx.doi.org/10.1080/14756366.2017.1355793

Internet

http://dx.doi.org/10.1080/14756366.2017.1355793

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