ORGN 661 |
| Lantibiotics are a unique class of ribosomally synthesized peptide antibiotics produced by Gram-positive bacteria. These compounds are termed lantibiotics because they contain the thioether amino acids lanthionine and/or methyllanthionine, in addition to 2,3-didehydroalanine and (Z)-2,3-didehydrobutyrine, which arise from enzyme catalyzed post-translational modifications. These non-proteinogenic amino acids are introduced by the dehydration of serine and threonine residues followed by stereoselective intramolecular Michael addition of cysteines onto the unsaturated amino acids. Lacticin 481 synthetase (LctM) catalyzes the post-translational modifications required for the generation of the lantibiotic lacticin 481. Recent studies of this protein responsible for the creation of the intricate polycyclic antimicrobial agent have revealed relaxed substrate specificity. In an effort to utilize this bifunctional enzyme for the engineering of novel therapeutic peptides, further substrate specificity is examined. |
|
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 |