Reference : The Active-Site-Serine Penicillin-Recognizing Enzymes as Members of the Streptomyces R61...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/34125
The Active-Site-Serine Penicillin-Recognizing Enzymes as Members of the Streptomyces R61 Dd-Peptidase Family
English
Joris, Bernard mailto [Université de Liège - ULg > Institut de Chimie > Service de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Chimie > Service de Microbiologie > >]
Dive, Georges mailto [Université de Liège - ULg > Institut de Chimie > Service de Microbiologie > >]
Renard, André [Eurogentec > > > >]
Dideberg, Otto [Université de Liège - ULg > Institut de Physique > Service de Cristallographie > >]
Charlier, Paulette mailto [Université de Liège - ULg > Institut de Physique > Service de Cristallographie > >]
Frère, Jean-Marie [Université de Liège - ULg > Département des sciences de la vie > Département des sciences de la vie >]
Kelly, Judith A. [University of Connecticut - UCONN > Institute of Materials Science > Department of Molecular and Cell Biology > >]
Boyington, Jeffrey [University of Connecticut - UCONN > Institute of Materials Science > Department of Molecular and Cell Biology > >]
Moews, Paul C. [University of Connecticut - UCONN > Institute of Materials Science > Department of Molecular and Cell Biology > >]
Knox, James [University of Connecticut - UCONN > Institute of Materials Science > Department of Molecular and Cell Biology > >]
1-Mar-1988
Biochemical Journal
Portland Press
250
2
313-324
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] Binding Sites ; Chymotrypsin ; Electricity ; Models, Chemical ; Quantum Theory ; Subtilisins
[en] Homology searches and amino acid alignments, using the Streptomyces R61 DD-peptidase/penicillin-binding protein as reference, have been applied to the beta-lactamases of classes A and C, the Oxa-2 beta-lactamase (considered as the first known member of an additional class D), the low-Mr DD-peptidases/penicillin-binding proteins (protein no. 5 of Escherichia coli and Bacillus subtilis) and penicillin-binding domains of the high-Mr penicillin-binding proteins (PBP1A, PBP1B, PBP2 and PBP3 of E. coli). Though the evolutionary distance may vary considerably, all these penicillin-interactive proteins and domains appear to be members of a single superfamily of active-site-serine enzymes distinct from the classical trypsin or subtilisin families. The amino acid alignments reveal several conserved boxes that consist of strict identities or homologous amino acids. The significance of these boxes is highlighted by the known results of X-ray crystallography, chemical derivatization and site-directed-mutagenesis experiments.
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; Fonds de la Recherche Scientifique Médicale - FRSM ; National Institutes of Health - NIH
Researchers ; Professionals
http://hdl.handle.net/2268/34125
http://www.biochemj.org/bj/default.htm

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