Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 86, Issue 3, Pages 891-899Publisher
SPRINGER
DOI: 10.1007/s00253-009-2334-8
Keywords
Lantibiotic; Unusual amino acids; Modification enzyme; Peptide engineering; Posttranslational modification
Categories
Funding
- Japan Society for the Promotion of Science
- Japan Science Society
- Novartis Foundation (Japan) for the Promotion of Science
- Novozymes Japan Research Fund
- Nagase Science and Technology Foundation
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The lantibiotic nukacin ISK-1 is an antimicrobial peptide containing unusual amino acids such as lanthionine and dehydrobutyrine. The nukacin ISK-1 prepeptide (NukA) undergoes posttranslational modifications, such as the dehydration and cyclization reactions required to form the unusual amino acids by the modification enzyme NukM. We have previously constructed a system for the introduction of unusual amino acids into NukA by coexpression of NukM in Escherichia coli. Using this system, we describe the substrate specificity of NukM by the coexpression of a series of NukA mutants. Our results revealed the following characteristics of NukM: (1) its dehydration activity is not coupled to its cyclization activity; (2) its dehydration activity is site-specific; (3) the length of the substrate is important for its dehydration activity. Furthermore, we succeeded in introducing a novel thioether bridge in NukA by replacing an unmodified Ser at position 27 with a Cys residue.
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