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Ticlopidine as a selective mechanism-based inhibitor of human cytochrome P450 2C19.
Ticlopidine is the first selective mechanism-based inhibitor of human liver CYP2C19 and should be a new interesting tool for studying the topology of the active site of CYP 2C19.
Substrate specificity of NO synthases: detailed comparison of L-arginine, homo-L-arginine, their N omega-hydroxy derivatives, and N omega-hydroxynor-L-arginine.
Most of the above results could be interpreted by comparing the possible positionings of the various substrates relative to the two NOS active oxygen species which are believed to be responsible for the two steps of the reaction.
Interaction of sulfaphenazole derivatives with human liver cytochromes P450 2C: molecular origin of the specific inhibitory effects of sulfaphenazole on CYP 2C9 and consequences for the substrate
The effects of sulfaphenazole, 1, on typical activities catalyzed by human cytochromes P450 of the 1A, 3A, and 2C subfamilies expressed in yeast were studied and a model for the binding of 1 in the CYP 2C9 active site is proposed.
Cytochromes P450 catalyze both steps of the major pathway of clopidogrel bioactivation, whereas paraoxonase catalyzes the formation of a minor thiol metabolite isomer.
Chemical experiments on 2-oxo-clopidogrel showed that this thiolactone is in equilibrium with its tautomer having a double bond inside the piperidine ring and that nucleophiles such as CH(3)O(-) preferentially react on the thioester function of this tautomers.
N omega-hydroxyl-L-arginine, an intermediate in the L-arginine to nitric oxide pathway, is a strong inhibitor of liver and macrophage arginase.
L-NOHA is a potent inhibitor of the arginase activity of rat liver homogenates and of murine macrophages and could play a role in the modulation of the biosynthesis of the biological mediator NO by increasing local L-Arg concentrations.
The great diversity of reactions catalyzed by cytochromes P450.
  • D. Mansuy
  • Chemistry
    Comparative biochemistry and physiology. Part C…
  • 1 November 1998
Thiophene derivatives as new mechanism-based inhibitors of cytochromes P-450: inactivation of yeast-expressed human liver cytochrome P-450 2C9 by tienilic acid.
TA exhibited all of the characteristics of a mechanism-based inactivator for P 450 2C9 and 2C10 enzymes and could be a starting point for the appearance of anti-P450 2C antibodies detected in patients treated with TA and suffering from immunoallergic hepatitis.
Diclofenac and its derivatives as tools for studying human cytochromes P450 active sites: particular efficiency and regioselectivity of P450 2Cs.
Results show that diclofenac derivatives are interesting tools to compare the active site topologies of human P450 2Cs, and that oxidation ofdicl ofenac and its derivative 2, either with chemical model systems of cytochrome P450 or with recombinant human P 450s, generally occurs at position 5.