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Aminoglycoside acetyltransferases AACs

Figure 18 Enzymatic inactivation of ciprofloxacin by N-acetylation catalyzed by the aminoglycoside acetyltransferase AAC(6 )-lb enzyme. Figure 18 Enzymatic inactivation of ciprofloxacin by N-acetylation catalyzed by the aminoglycoside acetyltransferase AAC(6 )-lb enzyme.
Unit, [tg/mL Kan, kanamycin S. aureus, Staphylococcus aureus P. aeruginosa, Pseudomonas aeruginosa AAC, aminoglycoside acetyltransferase ANT, aminoglycoside nucleotidyltransferase Perm, mutant, mutant strain impermeable to kanamycin A and B. [Pg.151]

Acetylation of antibiotics is a common mechanism of modification. The acyltransferases generally use the metabolically abundant acetyl-CoA as the preferred acyl-donor. The aminoglycoside antibiotic acetyltransferases (AACs), for example, modify important amines that make contact with the target 16 S rRNA (Fig. 9), which results in a loss of positive charge and increased steric bulk that contribute to lowering the affinity of the antibiotics for the rRNA target by 600-fold (26). The AACs are members of the GCN5 superfamily of acyltransferases that include such members as the eukaryotic histone acetyltransferases and serotonin acetyltransferase (27). [Pg.90]

Fig. 13.5 Structure of kanamycin B showing system of ring numbering and sites of action of some aminoglycosidemodifying enzymes. AAC, aminoglycoside acetyltransferase ANT, aminoglycoside nucleotidyltransferase and APH, aminoglycoside phosphotransferase. Fig. 13.5 Structure of kanamycin B showing system of ring numbering and sites of action of some aminoglycosidemodifying enzymes. AAC, aminoglycoside acetyltransferase ANT, aminoglycoside nucleotidyltransferase and APH, aminoglycoside phosphotransferase.
More recently, the Auclair group has reported a more extensive investigation of bisubstrate analog inhibitors toward aminoglycoside 6 -A-acetyltransferase (AAC(6 )-Ii) from Enterococcus faecium. AAC(6 )-Ii is chromoso-mally encoded in E. faecium and has been shown to use an ordered kinetic mechanism with acetyl-CoA binding... [Pg.691]

S. Magnet, T. Lambert, P. Courvalin, J.S. Blanchard, Kinetic and mutagenic characterization of chromosomally encoded salmonella enterica AAC(6 )-ly aminoglycoside N-acetyltransferase, Biochemistry 2001, 40, 3700-3709. [Pg.690]


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