Mutational analysis of active-site residues of the enterococcal d-Ala-d-Ala dipeptidase VanX and comparison with Escherichia colid-Ala-d-Ala ligase and d-Ala-d-Ala carboxypeptidase VanY
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چکیده
منابع مشابه
Mutational analysis of active-site residues of the enterococcal D-ala-D-Ala dipeptidase VanX and comparison with Escherichia coli D-ala-D-Ala ligase and D-ala-D-Ala carboxypeptidase VanY.
BACKGROUND Vancomycin-resistant enterococci are pathogenic bacteria that attenuate antibiotic sensitivity by producing peptidoglycan precursors that terminate in D-Ala-D-lactate rather than D-Ala-D-Ala. A key enzyme in effecting antibiotic resistance is the metallodipeptidase VanX, which reduces the cellular pool of the D-Ala-D-Ala dipeptide. RESULTS We constructed eleven mutants, using the r...
متن کاملChapter 771 Actinomadura R39 d-Ala d Ala Carboxypeptidase
bacterial penicillin-binding proteins and beta-lactamases. Antimicrob. Agents Chemother. 42(1), 1 17. [41] Davies, C., White, S.W., Nicholas, R.A. (2001). Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-Å resolution. J. Biol. Chem. 276(1), 616 623. [42] Nicola, G., Tomberg, J., Pratt, R.F., Nicholas, R.A., Davies, C. (2010). Crystal structures of coval...
متن کاملDeterminants for differential effects on D-Ala-D-lactate vs D-Ala-D-Ala formation by the VanA ligase from vancomycin-resistant enterococci.
Bacteria with either intrinsic or inducible resistance to vancomycin make peptidoglycan (PG) precursors of lowered affinity for the antibiotic by switching the PG-D-Ala-D-Ala termini that are the antibiotic-binding target to either PG-D-Ala-D-lactate or PG-D-Ala-D-Ser as a consequence of altered specificity of the D-Ala-D-X ligases in the cell wall biosynthetic pathway. The VanA ligase of vanco...
متن کاملSimilar active sites in lysostaphins and D-Ala-D-Ala metallopeptidases.
Specific peptidases exist for nearly every amide linkage in peptidoglycan. In several cases, families of peptidoglycan hydrolases with different specificities turned out to be related. Here we show that lysostaphin-type peptidases and D-Ala-D-Ala metallopeptidases have similar active sites and share a core folding motif in otherwise highly divergent folds. The central Zn(2+) is tetrahedrally co...
متن کاملALA-D and ALA-D reactivated as biomarkers of lead contamination in the fish Prochilodus lineatus.
ALA-D activity and lead concentrations were measured in blood and liver tissues of the fish Prochilodus lineatus, collected from three locations along the coast of the La Plata River, Argentina. Two of them, Berazategui and Berisso, were located nearby the main ducts that discharge the urban and domestic waste disposal from Buenos Aires and La Plata cities, respectively, while the third station...
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ژورنال
عنوان ژورنال: Chemistry & Biology
سال: 1999
ISSN: 1074-5521
DOI: 10.1016/s1074-5521(99)89009-7