Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/34484
Title: CRYSTALLISATION AND PRELIMINARY STRUCTURAL ANALYSIS OF ECM18 WHICH CATALYSES DISULFIDE TO THIOACETAL CONVERSION IN ECHINOMYCIN BIOSYNTHESIS
Authors: SOUMYA RANGANATHAN
Keywords: Crystallisation, Structure, enzyme, catalytic mechanism, antitumor, non-ribosomal
Issue Date: 5-Apr-2012
Source: SOUMYA RANGANATHAN (2012-04-05). CRYSTALLISATION AND PRELIMINARY STRUCTURAL ANALYSIS OF ECM18 WHICH CATALYSES DISULFIDE TO THIOACETAL CONVERSION IN ECHINOMYCIN BIOSYNTHESIS. ScholarBank@NUS Repository.
Abstract: Echinomycin, produced by the soil bacterium Streptomyces lasaliensis, is a non-ribosomal peptide natural product with both antibiotic and antitumor activity. In the first step of echinomycin biosynthesis, two non-ribosomal peptide synthetases produce the eight-residue cyclic peptide scaffold. In the next step, a disulfide bridge is formed across the peptide scaffold which is then converted to a thioacetal group by the enzyme Ecm18. This thioacetal group confers extra structural rigidity and chemical stability to echinomycin which is important for maintaining its biological activity. We report a preliminary X-ray crystal structure of the Ecm18¿echinomycin¿S-adenosylhomocysteine ternary complex and provide a plausible catalytic mechanism.
URI: http://scholarbank.nus.edu.sg/handle/10635/34484
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