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  4. Inhibition studies of porphobilinogen synthase from Escherichia coli differentiating between the two recognition sites
 
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Inhibition studies of porphobilinogen synthase from Escherichia coli differentiating between the two recognition sites

Auteur(s)
Stauffer, Frédéric
Zizzari, Eleonor
Jarret, Caroline
Faurite, Jean-Philippe
Bobalova, Janette
Neier, Reinhard 
Institut de chimie 
Date de parution
2001
In
Chembiochem
Vol.
5
No
2
De la page
343
A la page
354
Mots-clés
  • biosynthesis
  • inhibitors
  • intermediates
  • lyases
  • porphobilinogen
  • synthase
  • 5-AMINOLEVULINIC ACID DEHYDRATASE
  • X-RAY STRUCTURE
  • 280000-DALTON
  • PROTEIN
  • PYRROLE CHEMISTRY
  • ACTIVE-SITE
  • BIOSYNTHESIS
  • ANALOGS
  • RESOLUTION
  • MECHANISM
  • SUBSTRATE
  • biosynthesis

  • inhibitors

  • intermediates

  • lyases

  • porphobilinogen

  • synthase

  • 5-AMINOLEVULINIC ACID...

  • X-RAY STRUCTURE

  • 280000-DALTON

  • PROTEIN

  • PYRROLE CHEMISTRY

  • ACTIVE-SITE

  • BIOSYNTHESIS

  • ANALOGS

  • RESOLUTION

  • MECHANISM

  • SUBSTRATE

Résumé
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.
Identifiants
https://libra.unine.ch/handle/123456789/6413
Type de publication
journal article
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