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A spontaneous point mutation i the aac(6′)‐lb′ gene results in altered substrate specificity of aminoglycoside 6′‐ N ‐acetyltransferase of a Pseudomonas fluorescens strain
Author(s) -
Lambert Thierry,
Ploy MarieCecile,
Courvalin Patrice
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06654.x
Subject(s) - aminoglycoside , acetyltransferase , amikacin , pseudomonas fluorescens , point mutation , gentamicin , pseudomonas aeruginosa , gene , microbiology and biotechnology , biology , pseudomonas , mutation , chemistry , biochemistry , genetics , bacteria , antibiotics , acetylation
The aac(6′)‐lb′ gene from Pseudomonas fluorescens BM2687, encoding an aminoglycoside 6′‐ N ‐acetyltransferase type II which confers resistance to gentamicin but not to amikacin, was characterized. Nucleotide sequence determination indicated total identity between aac6′)‐lb and the aac(6′)‐lb gene from Pseudomonas aeruginosa BM2656 [1] with the exception of a C‐to‐T transition that results in a serine to lecine substitution at position 83 of the deduced polypeptide. The aac(6′)‐lb gene specifies a type I enzyme which confers resistance to amikacin but not to gentamicin [2]. It thus appears that the point mutation detected is responsible for enzymic altered substrate specificity.

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