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Structural studies in the biosynthesis of the glycopeptide antibiotic teicoplanin
Author(s) -
Li Zhi,
Nair Satish K.
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.lb211
Subject(s) - teicoplanin , glycopeptide , glycopeptide antibiotic , antibiotics , vancomycin , microbiology and biotechnology , biochemistry , chemistry , biology , bacteria , staphylococcus aureus , genetics
Teicoplanin is a glycopeptide antibiotic that has proven efficacy against Gram‐positive bacteria and is in clinical trials. It is distinguished from vancomycin‐type glycopeptides antibiotics by side chain modifications, which have been shown to contribute to its improved efficacy and superior pharmacokinetic profile. Our research aims to study the biosynthetic mechanisms of teicoplanin, which will likely lead to the development of new glycopeptide derivatives. Here we present high resolution crystal structures of several enzymes that modify teicoplanin side chains during its biosynthesis. The structures provide insights into the active residues of these enzymes and suggest possible mechanisms of modifying glycopeptides antibiotics.