Allosteric inhibition of carnosinase (CN1) by inducing a conformational shift.
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ABSTRACT:
SUBMITTER: Peters V
PROVIDER: S-EPMC6009930 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
Publications
Allosteric inhibition of carnosinase (CN1) by inducing a conformational shift.
Peters Verena V Schmitt Claus P CP Weigand Tim T Klingbeil Kristina K Thiel Christian C van den Berg Antje A Calabrese Vittorio V Nawroth Peter P Fleming Thomas T Forsberg Elisabete E Wagner Andreas H AH Hecker Markus M Vistoli Giulio G
Journal of enzyme inhibition and medicinal chemistry 20171201 1
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 < .05) lowered dose-dependently recombinant CN1 (rCN1) efficiency (5.2 ± 0.2 µmol/mg/h/mM) and normalized increased CN1 activity rena ...[more]
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