ORGN 662 |
| Lacticin 481 is a lanthionine-containing bacteriocin (lantibiotic) produced by the Gram-positive bacteria Lactococcus lactis subsp. lactis. The final steps of lacticin 481 biosynthesis are cleavage of an N-terminal leader sequence from the prepeptide LctA followed by export of the mature lantibiotic. Both cleavage and export are performed by the dedicated ATP-binding cassette (ABC) transporter LctT. LctT belongs to the recently described family of AMS (ABC transporter maturation and secretion) proteins whose prepeptide substrates share a conserved double-glycine type cleavage site. While the in vitro activity of a non-lantibiotic bacteriocin protease, LagD, has been previously described by Håvarstein and co-workers, the activity of a lantibiotic protease has not yet been characterized. We report the purification and in vitro activity of the protease domain of LctT, which exhibited a permissive substrate scope. |
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Asymmetric Reactions, Combinatorial Chemistry, Molecular Recognition and Self-Assembly, Proteins, Peptides, Amino Acids and Enzyme Inhibitors
8:00 PM-10:00 PM, Wednesday, March 28, 2007 Hyatt Regency Chicago -- Riverside Center, Poster
Division of Organic Chemistry |