Localisation of the aminoglycoside-(3)-N-acetyltransferase isoenzyme II in Escherichia coli.
For the location of the aminoglycoside-(3)-N-acetyltransferase isoenzyme II (AAC(3)-II) in the bacterial cell, two strains were studied: Escherichia coli HB101(pJV03), producing the 31-kDa AAC (3)-II enzyme, and E. coli HB101, which served as a control. From each strain five protein fractions were prepared: culture supernatant, and proteins occurring in the periplasm, cytoplasm, inner membrane and outer membrane. All fractions were tested for enzymatic activity of AAC(3)-II. Most of the acetylating activity was found in the cytoplasmic fraction. The distribution of marker enzymes showed a good separation between the periplasmic and the cytoplasmic fraction.
Vliegenthart
J S
JS
Department of Medical Microbiology, University Hospital, Leiden, The Netherlands.
Ketelaar-van Gaalen
P A
PA
Eelhart
J
J
van de Klundert
J A
JA
D000123:Acetyltransferases / Q000032:analysis*; D004926:Escherichia coli / Q000201:enzymology*; D007527:Isoenzymes / Q000032:analysis*; D014357:Trypsin / Q000494:pharmacology
D007527:Isoenzymes; D000123:Acetyltransferases; C045539:aminoglycoside N(3')-acetyltransferase; D014357:Trypsin