TY  - JOUR
  - Book Reviews
  - McAuliffe, O,Ross, RP,Hill, C
  - 2001
  - January
  - Lantibiotics: structure, biosynthesis and mode of action
  - Validated
  - 1
  - ()
  - bacteriocin lantibiotic nisin lacticin 3147 mode of action PEPTIDE ANTIBIOTIC NISIN LACTIC-ACID BACTERIA GRAM-POSITIVE BACTERIA ENTEROCOCCUS-FAECALIS CYTOLYSIN PROTON MOTIVE FORCE VOLTAGE-DEPENDENT DEPOLARIZATION PEDIOCOCCUS-ACIDILACTICI PAC1.0 EPIDERMIN PRECURSOR PEPTIDE STAPHYLOCOCCUS-AUREUS C55 PYOGENES STRAIN FF22
  - The lantibiotics are a group of ribosomally synthesised, post-translationally modified peptides containing unusual amino acids, such as dehydrated and lanthionine residues. This group of bacteriocins has attracted much attention in recent years due to the success of the well characterised lantibiotic, nisin, as a Food preservative. Numerous other lantibiotics have since been identified and can be divided into two groups on the basis of their structures, designated type-A and type-B. To date, many of these lantibiotics have undergone extensive characterisation resulting in an advanced understanding of them at both the structural and mechanistic level. This review outlines some of the more recent developments in the biochemistry, genetics and mechanism of action of these peptides. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
  - 285
  - 308
DA  - 2001/01
ER  - 

@review{V160957841,
   = {Book Reviews},
   = {McAuliffe,  O and Ross,  RP and Hill,  C },
   = {2001},
   = {January},
   = {Lantibiotics: structure, biosynthesis and mode of action},
   = {Validated},
   = {1},
   = {()},
   = {bacteriocin lantibiotic nisin lacticin 3147 mode of action PEPTIDE ANTIBIOTIC NISIN LACTIC-ACID BACTERIA GRAM-POSITIVE BACTERIA ENTEROCOCCUS-FAECALIS CYTOLYSIN PROTON MOTIVE FORCE VOLTAGE-DEPENDENT DEPOLARIZATION PEDIOCOCCUS-ACIDILACTICI PAC1.0 EPIDERMIN PRECURSOR PEPTIDE STAPHYLOCOCCUS-AUREUS C55 PYOGENES STRAIN FF22},
   = {{The lantibiotics are a group of ribosomally synthesised, post-translationally modified peptides containing unusual amino acids, such as dehydrated and lanthionine residues. This group of bacteriocins has attracted much attention in recent years due to the success of the well characterised lantibiotic, nisin, as a Food preservative. Numerous other lantibiotics have since been identified and can be divided into two groups on the basis of their structures, designated type-A and type-B. To date, many of these lantibiotics have undergone extensive characterisation resulting in an advanced understanding of them at both the structural and mechanistic level. This review outlines some of the more recent developments in the biochemistry, genetics and mechanism of action of these peptides. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.}},
  pages = {285--308},
  source = {IRIS}
}