Reference : Purification and Characterization of Pbp4a, a New Low-Molecular-Weight Penicillin-Bindin...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/1783
Purification and Characterization of Pbp4a, a New Low-Molecular-Weight Penicillin-Binding Protein from Bacillus subtilis
English
[fr] Purification et caractérisation du PBP4a, un nouveau PBP de faible poids moléculaire, de Bacillus subtilis
Duez, Colette mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Vanhove, Marc [Université de Liège > > Centre d'Ingénierie des Protéines > 2001 >]
Gallet, Xavier [Faculté Universitaire des Sciences Agronomiques de Gembloux - FUSAGx > > Laboratopire de Biophysique Moléculaire Numérique > 2001 >]
Bouillenne, Fabrice mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Docquier, Jean-Denis [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Brans, Alain mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Département des sciences de la vie > Enzymologie >]
Mar-2001
Journal of Bacteriology
183
5
1595-9
Yes (verified by ORBi)
International
0021-9193
[en] Penicillin-Binding Protein ; Bacillus subtilis
[en] Penicillin-binding protein 4a (PBP4a) from Bacillus subtilis was overproduced and purified to homogeneity. It clearly exhibits DD-carboxypeptidase and thiolesterase activities in vitro. Although highly isologous to the Actinomadura sp. strain R39 DD-peptidase (B. Granier, C. Duez, S. Lepage, S. Englebert, J. Dusart, O. Dideberg, J. van Beeumen, J. M. Frere, and J. M. Ghuysen, Biochem. J. 282:781-788, 1992), which is rapidly inactivated by many beta-lactams, PBP4a is only moderately sensitive to these compounds. The second-order rate constant (k(2)/K) for the acylation of the essential serine by benzylpenicillin is 300,000 M(-1) s(-1) for the Actinomadura sp. strain R39 peptidase, 1,400 M(-1) s(-1) for B. subtilis PBP4a, and 7,000 M(-1) s(-1) for Escherichia coli PBP4, the third member of this class of PBPs. Cephaloridine, however, efficiently inactivates PBP4a (k(2)/K = 46,000 M(-1) s(-1)). PBP4a is also much more thermostable than the R39 enzyme.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Scientifique (Communauté française de Belgique) - FNRS, Services Fédéraux des affaires scientifiques
Purification et caractérisation du PBP4a de Bacillus subtilis
Researchers
http://hdl.handle.net/2268/1783
also: http://hdl.handle.net/2268/64111
10.1128/JB.183.5.1595-1599.2001

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