
Noureseothricin (streptothricin) inactivated by a plasmid pIE636 encoded acetyl transferase of Escherichia coli : Location of the acetyl group
Author(s) -
Zähringer Ulrich,
Voigt Wolfgang,
Seltmann Guntram
Publication year - 1993
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.1574-6968.1993.tb06344.x
Subject(s) - escherichia coli , transferase , plasmid , enterobacteriaceae , biology , genetics , chemistry , microbiology and biotechnology , biochemistry , enzyme , gene
Escherichia coli strains harbouring the plasmid pIE636 are able to synthesize acetylcoenzyme A: streptothricin acetyltransferase (ACSAT). The (enzymatic) N ‐acetylation of streptothricin F is known to contribute significantly towards the loss of antibacterial activity. 13 C‐NMR analysis of [ 14 C]N‐acetyl‐labelled streptothricin F, produced by ACSAT‐catalysed acetylation of streptothricin F and subsequent purification by various chromatographical steps, unequivocally revealed streptothricin F to be acetylated at the β‐amino group (C16) (and not at the ε‐amino group (C19)).