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

Authors :: Christian Thiel
Thomas Fleming
Markus Hecker
Andreas H. Wagner
Vittorio Calabrese
Verena Peters
Peter P. Nawroth
Claus Peter Schmitt
Elisabete Forsberg
Tim Weigand
Antje van den Berg
Giulio Vistoli
Kristina Klingbeil
Source :: Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 32, Iss 1, Pp 1102-1110 (2017), Journal of Enzyme Inhibition and Medicinal Chemistry
Publication Year :: 2017
Publisher :: Informa UK Limited, 2017.
Abstract: 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