Voici les éléments 1 - 3 sur 3
  • Publication
    Métadonnées seulement
    Inhibition studies of porphobilinogen synthase from Escherichia coli differentiating between the two recognition sites
    (2001)
    Stauffer, Frédéric
    ;
    Zizzari, Eleonor
    ;
    Jarret, Caroline
    ;
    Faurite, Jean-Philippe
    ;
    Bobalova, Janette
    ;
    Porphobilinogen synthase condenses two molecules of 5-amino-levulinate in an asymmetric way. This unusual transformation requires a selective recognition and differentiation between the :substrates ending up in the A site or in the P site of porphobilinogen synthase. Studies of inhibitors based on the key intermediate first postulated by Jordan allowed differentiation of the two recognition sites. The P site, whose structure is known from X-ray crystallographic studies, tolerates ester functions well. The A site interacts very strongly with nitro groups, but is not very tolerant to ester functions. This differentiation is a central factor in the asymmetric I handling of the two identical substrates. Finally, it could be shown nor the keto group of-the,Substrate bound at the A site is not Only essential for the recognition, but that an increase in electrophilicity of-the carbon atom also increases the inhibition potency considerably. This has important consequences for the recognition process at the A site, whose-exact structure is not yet known.
  • Publication
    Métadonnées seulement
    Inhibition Studies of Porphobilinogen Synthase from Escherichia coli Using Diacids
    (: Imperial College Press, 1998)
    Jarret, Caroline
    ;
    Bobalova, Janette
    ;
    Stauffer, Frédéric
    ;
    Henz, Matthias
    ;
    ;
    Rzepa, H.J.
    ;
    Kappe, O.
  • Publication
    Métadonnées seulement
    Inhibition of porphobilinogen synthase (PBG-synthase) by 4,6-dioxoheptanoic acid and related compounds
    (1998)
    Stauffer, Frederic
    ;
    Jarret, Caroline
    ;
    Engeloch, Thomas
    ;
    Henz, Matthias
    ;
    Bobalova, Janette
    ;
    We are investigating the mechanism of PBG-synthase by active site directed inhibition studies. The procedure for testing and the data obtained with compds. related to 4,6-dioxoheptanoic acid are reported and the results are discussed in the context of our kinetic model. [on SciFinder(R)]