PMID:9751644
| Citation |
Lessard, IA, Pratt, SD, McCafferty, DG, Bussiere, DE, Hutchins, C, Wanner, BL, Katz, L and Walsh, CT (1998) Homologs of the vancomycin resistance D-Ala-D-Ala dipeptidase VanX in Streptomyces toyocaensis, Escherichia coli and Synechocystis: attributes of catalytic efficiency, stereoselectivity and regulation with implications for function. Chem. Biol. 5:489-504 |
|---|---|
| Abstract |
Vancomycin-resistant enterococci are pathogenic bacteria that have altered cell-wall peptidoglycan termini (D-alanyl-D-lactate [D-Ala-D-lactate] instead of D-alanyl-D-alanine [D-Ala-D-Ala]), which results in a 1000-fold decreased affinity for binding vancomycin. The metallodipeptidase VanX (EntVanX) is key enzyme in antibiotic resistance as it reduces the cellular pool of the D-Ala-D-Ala dipeptide. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Base Sequence; Catalysis; Cell Wall/metabolism; Cyanobacteria/enzymology; Dipeptidases/chemistry; Dipeptidases/metabolism; Dipeptides/metabolism; Drug Resistance, Microbial; Escherichia coli/enzymology; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Alignment; Serine-Type D-Ala-D-Ala Carboxypeptidase; Stereoisomerism; Streptomyces/enzymology; Substrate Specificity; Vancomycin/pharmacology; Zinc/metabolism |
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