| The ybxI gene of Bacillus subtilis 168 encodes a class D beta-lactamase of low activity. | |
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MedLine Citation:
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PMID: 14742199 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Maria-Luigi Colombo; Sophie Hanique; Stéphane L Baurin; Cédric Bauvois; Kris De Vriendt; Jozef J Van Beeumen; Jean-Marie Frère; Bernard Joris |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Antimicrobial agents and chemotherapy Volume: 48 ISSN: 0066-4804 ISO Abbreviation: Antimicrob. Agents Chemother. Publication Date: 2004 Feb |
Date Detail:
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Created Date: 2004-01-26 Completed Date: 2004-03-11 Revised Date: 2013-04-18 |
Medline Journal Info:
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Nlm Unique ID: 0315061 Medline TA: Antimicrob Agents Chemother Country: United States |
Other Details:
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Languages: eng Pagination: 484-90 Citation Subset: IM |
Affiliation:
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Centre d'Ingénierie des Protéines, Institut de Chimie B6a, Université de Liège, Sart Tilman, B-4000 Liège 1, Belgium. |
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Bacillus subtilis / drug effects, enzymology*, genetics* Bacterial Proteins Bicarbonates / pharmacology Carrier Proteins Cephalosporins / metabolism Electrophoresis, Polyacrylamide Gel Genes, Bacterial / genetics* Hexosyltransferases Hydrolysis Kinetics Molecular Sequence Data Muramoylpentapeptide Carboxypeptidase Penicillin-Binding Proteins Peptidoglycan / metabolism Peptidyl Transferases Plasmids / genetics RNA, Bacterial / biosynthesis RNA, Messenger / biosynthesis Reverse Transcriptase Polymerase Chain Reaction beta-Lactamases / biosynthesis*, genetics* |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Bicarbonates; 0/Carrier Proteins; 0/Cephalosporins; 0/Penicillin-Binding Proteins; 0/Peptidoglycan; 0/RNA, Bacterial; 0/RNA, Messenger; EC 2.3.2.12/Peptidyl Transferases; EC 2.4.1.-/Hexosyltransferases; EC 3.4.17.8/Muramoylpentapeptide Carboxypeptidase; EC 3.5.2.6/beta-Lactamases; EWP54G0J8F/nitrocefin |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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