Reference : Importance of the His-298 Residue in the Catalytic Mechanism of the Streptomyces R61 ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/79709
Importance of the His-298 Residue in the Catalytic Mechanism of the Streptomyces R61 Extracellular Dd-Peptidase
English
Hadonou, Ayaovi M. [Université de Liège - ULiège > Institut de Chimie > Centre d'Ingenierie des Proteines > >]
Jamin, Marc [Université de Liège - ULiège > Institut de Chimie > Centre d'Ingenierie des Proteines > >]
Adam, Maggy [Université de Liège - ULiège > Institut de Chimie > Centre d'Ingenierie des Proteines > >]
Joris, Bernard mailto [Université de Liège - ULiège > > Centre d'ingénierie des protéines >]
Dusart, Jean [Université de Liège - ULiège > Institut de Chimie > Centre d'Ingenierie des Proteines > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > Institut de Chimie > Centre d'ingénieurie des protéines > > >]
Frère, Jean-Marie mailto [Université de Liège - ULiège > Institut de Chimie > Centre d'ingénierie des protéines > >]
1-Mar-1992
Biochemical Journal
Portland Press
282
Pt 2
495-500
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] Streptomyces ; Penicillin binding protein ; Peptidase ; Molecular orientation ; Histidine ; Site directed mutagenesis ; Streptomycetaceae ; Actinomycetales ; Actinomycetes ; Bacteria
[fr] Protéine liaison pénicilline ; Orientation moléculaire ; Mutagenèse dirigée ; Bactérie
[es] Proteína enlace penicilina ; Orientación molecular ; Histidina
[en] Mutagénesis dirigida
[en] Among the active-site-serine penicillin-recognizing proteins, the Streptomyces R61 extracellular DD-peptidase is the only one to have a His-Thr-Gly sequence [instead of Lys-Thr(Ser)-Gly] in 'box' VII. The His residue was replaced by Gln or Lys. Both mutations induced a marked decrease in the rates of both tripeptide substrate hydrolysis and acylation by benzylpenicillin and cephalosporin C. The rate of hydrolysis of the thioester hippuryl thioglycollate was less affected. The most striking result was the disproportionate loss of transpeptidation properties by both mutants, indicating an important role of His-298 in this reaction. We believe that this result represents the first modification of a DD-peptidase leading to a specific decrease of the transpeptidation-to-hydrolysis ratio.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/79709

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