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

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?

SUBMITTER: Peters V 

PROVIDER: S-EPMC6009930 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature

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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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