Premium
Purification and characterization of a plasmid‐encoded aminoglycoside‐(3)‐ N ‐acetyltransferase IV from Escherichia coli
Author(s) -
Bräu Barbara,
Piepersberg Wolfgang
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80737-7
Subject(s) - escherichia coli , plasmid , acetyltransferase , enzyme , peptide sequence , aminoglycoside , microbiology and biotechnology , biochemistry , nucleic acid sequence , chemistry , gene , biology , antibiotics , acetylation
Plasmid‐encoded aminoglycoside‐(3)‐ N ‐acetyltransferase IV, AAC(3)‐IV, was purified to homogeneity by affinity chromatography from E. coli The enzyme was shown to consist of a monomer, with the apparent M r being in agreement with that calculated from the nucleotide sequence of the aacC4 gene ( M r 28 500). Determination of the sequence of the N‐terminal 6 amino acids revealed that processing did not occur, indicating the cytoplasmic localization of the AAC(3)‐IV enzyme. A correlation of antibiotic resistance with K m values of the purified enzyme for a corresponding set of aminoglycoside substrates is discussed with respect to the mechanism of resistance in vivo.