Nisin biosynthesis and its properties.
The antimicrobial peptide, nisin, produced by several strains of Lactococcus lactis, which belongs to the Class I bacteriocins called lantibiotics, is a small (3.4 kDa), 34-amino acid, cationic, hydrophobic peptide and has the five characteristic (beta-methyl)lanthionine rings formed by significant post-translational modification. A cluster of 11 genes has been involved in the biosynthesis of nisin and are proposed to be transcriptionally arranged as nisA(Z)BTCIP, nisRK, and nisFEG. The biosynthesis of nisin is regulated in a growth-phase-dependent manner including nisin-mediated induction which occurs via NisRK two-component regulatory system. This review outlines some of the more recent developments in the properties, regulation and applications of nisin biosynthesis.
Cheigh
Chan-Ick
CI
Department of Biotechnology, Yonsei University, 120-749, Seoul, Korea.
Pyun
Yu-Ryang
YR
D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000737:chemistry; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000737:chemistry; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D013294:Lactococcus lactis / Q000737:chemistry / Q000378:metabolism*; D009561:Nisin / Q000096:biosynthesis* / Q000737:chemistry; D011499:Protein Processing, Post-Translational / Q000502:physiology*
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D009561:Nisin