Reference : The ybxI gene of Bacillus subtilis 168 encodes a class D beta-lactamase of low activity
Scientific journals : Article
Human health sciences : Pharmacy, pharmacology & toxicology
Life sciences : Microbiology
http://hdl.handle.net/2268/22699
The ybxI gene of Bacillus subtilis 168 encodes a class D beta-lactamase of low activity
English
Colombo, Maria-Luigi [> > > >]
Hanique, Sophie [> > > >]
Baurin, Stéphane L. [> > > >]
Bauvois, Cédric [> > > >]
De Vriendt, Kris [> > > >]
Van Beeumen, Jozef J. [> > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Département des sciences de la vie > Département des sciences de la vie >]
Joris, Bernard mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Feb-2004
Antimicrobial Agents and Chemotherapy
Amer Soc Microbiology
48
2
484-490
Yes (verified by ORBi)
0066-4804
Washington
[en] The ybxI gene of Bacillus subtilis 168 encodes a preprotein of 267 amino acid residues, including a putative signal peptide of 23 residues. The YbxI primary structure exhibits high similarity scores with two members of the superfamily of the serine penicillin-recognizing enzymes: the class D beta-lactamases and the hydrophilic carboxy-terminal domains of the BlaR and MecR penicillin receptors. To determine the function and the activity of this putative penicillin-recognizing enzyme, we have subcloned the ybxI gene in the pET-26b expression vector. Transformation of Escherichia coli BL21(DE3) by the recombinant plasmid pCIP51 resulted in the export of the mature YbxI in the periplasm as a water-soluble protein. The recombinant protein was purified to 95% homogeneity. YbxI interacts with several beta-lactam antibiotics and can hydrolyze some of them. YbxI is not inactivated by clavulanic acid. The YbxI function and its enzymatic activity in B. subtilis remain unknown. The acyl-enzyme obtained after incubation of YbxI with a fluorescent derivative of ampicillin can be detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, confirming that YbxI can be acylated by beta-lactam antibiotics. YbxI does not hydrolyze some of the standard substrates of D-alanyl-D-alanine peptidases, the targets of penicillin. YbxI belongs to the penicillin-recognizing enzyme family but has an activity intermediate between those of a penicillin-binding protein and a beta-lactamase.
http://hdl.handle.net/2268/22699

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