Mutational analysis and chemical modification of Cys24 of lactococcin B, a bacteriocin produced by Lactococcus lactis
Venema, Koen and Dost, Michiel H. R. and Venema, Gerard and Kok, Jan,, 142, 2825-2830 (1996),
doi = https://doi.org/10.1099/13500872-142-10-2825,
publicationName = Microbiology Society,
issn = 1350-0872,
abstract= Using site-directed mutagenesis the single cysteine residue at position 24 of lactococcin B was replaced by all other possible amino acids. Most of these mutant molecules retained bacteriocin activity, with the exception of those in which cysteine was replaced by a positively charged amino acid. This would seem to be in agreement with the authors’ earlier observation that treatment of the wild-type molecule with HgCI2 resulted in its inactivation. The factor that causes inactivation of lactococcin B seems to be the introduction of a positive charge at position 24 by HgCI2 rather than oxidation of this residue, as treatment of the bacteriocin with other oxidative chemicals did not interfere with the ability of lactococcin B to dissipate the membrane potential of sensitive cells. Results are also reported which imply that inactive lactococcin B can still bind to its receptor. It can be replaced by an active bacteriocin molecule, resulting in dissipation of the membrane potential.,
language=,
type=