Biosynthesis, immunity, regulation, mode of action and engineering of the model lantibiotic nisinLubelski, J., Rink, R., Khusainov, R., Moll, G. N. & Kuipers, O. P., Feb-2008, In : Cellular and molecular life sciences. 65, 3, p. 455-476 22 p.
Research output: Contribution to journal › Review article › Academic › peer-review
This review discusses the state-of-the-art in molecular research on the most prominent and widely applied lantibiotic, i.e., nisin. The developments in understanding its complex biosynthesis and mode of action are highlighted. Moreover, novel applications arising from engineering either nisin itself, or from the construction of totally novel dehydrated and/or lanthionine-containing peptides with desired bioactivities are described. Several challenges still exist in understanding the immunity system and the unique multiple reactions occurring on a single substrate molecule, carried out by the dehydratase NisB and the cyclization enzyme NisC. The recent elucidation of the 3-D structure of NisC forms the exciting beginning of further 3-D-structure determinations of the other biosynthetic enzymes, transporters and immunity proteins. Advances in achieving in vitro activities of lanthionine-forming enzymes will greatly enhance our understanding of the molecular characteristics of the biosynthesis process, opening up new avenues for developing unique and novel biocatalytic processes.
|Number of pages||22|
|Journal||Cellular and molecular life sciences|
|Publication status||Published - Feb-2008|
- nisin, biosynthesis, dehydration, cyclization, thioether-containing peptides, protein engineering, mode of action, therapeutical peptides, PEPTIDE ANTIBIOTIC NISIN, LACTOCOCCUS-LACTIS N8, SODIUM DODECYL-SULFATE, PRECURSOR LIPID II, LEADER PEPTIDE, POSTTRANSLATIONAL MODIFICATION, BACILLUS-SUBTILIS, PORE FORMATION, ACID BACTERIA, GENE-CLUSTER