Structure of nisin

Gross, Erhard; Morell, John L.

doi:10.1021/ja00747a073

Cited by 573 publications

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“…The loss of activity in basic pH might be due to the degradation of the molecule. Similar type of observation was reported for Pediocin PA-1 [28] and Nisin [29,30] where probably the secondary structure is distorted at alkaline pH. It also retained its antimicrobial activity in autoclaving temperature, 121°C for 20 min [17].…”

Section: Partial Purification and Characterization Of The Antimicrobisupporting

confidence: 79%

Isolation and Characterization of Pediocin NV 5 Producing Pediococcus acidilactici LAB 5 from Vacuum-Packed Fermented Meat Product

Mandal¹,

Sen

Mandal

2011

Indian J Microbiol

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A potentially novel antimicrobial compound producing Pediococcus acidilactici LAB 5 was isolated from vacuum-packed fermented meat product. This compound was found active against some species of Enterococcus, Leuconostoc, Staphylococcus and Listeria, many of which are associated with food spoilage and food related health hazards. The strain was found to be a paired cocci which can utilize a broad range of carbohydrates and produce acid identical to the P. acidilactici and P. pentoseus. Since the antimicrobial agent was sensitive to proteolytic enzymes but quite resistant to heat, it was identified as a bacteriocin and was designated as Pediocin NV 5. The molecular weight of the bacteriocin was 10.3 kDa and the bacterium possessed a 5 kbp plasmid responsible for bacteriocin production and also for vancomycin resistance phenotype.

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Section: Partial Purification and Characterization Of The Antimicrobisupporting

confidence: 79%

Isolation and Characterization of Pediocin NV 5 Producing Pediococcus acidilactici LAB 5 from Vacuum-Packed Fermented Meat Product

Mandal¹,

Sen

Mandal

2011

Indian J Microbiol

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“…The structure of nisin [14,22] is shown in Fig. 1 ; it can be seen to contain five rings formed by lanthionine or methyllanthionine residues.…”

Section: Production and Characterisation Of Nandand Fragmentsmentioning

confidence: 99%

Structure‐activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin

Chan¹,

Leyland²,

Clark³

et al. 1996

FEBS Letters

123

160

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The post-translationally modified peptide antibiotic nisin has been cleaved by a number of proteases and the fragments produced purified, characterised chemically, and assayed for activity in inhibiting the growth of Lactococcus lactis MG1614 and Micrococcus luteus NCDO8166. These results provide information on the importance of different parts of the nisin molecule for its growth-inhibition activity. Removal of the C-terminal five residues leads to approximately a 10-fold decrease in potency, while removal of a further nine residues, encompassing two of the lanthionine rings, leads to a 100-fold decrease. There are some differences between analogous fragments of nisin and subtilin, suggesting possible subtle differences in mode of action. Cleavage within, or removal of, lanthionine ring C essentially abolishes the activity of nisin. The fragment ulsin t-12 is inactive itself, and specifically antagonises the growth-inhibitory action of nisin. These results are discussed in lerms of current models for the mechanism of action of nisin.Key words: Nisin; Lantibiotic; Peptide antibiotic; I'roteolysis; Structure-activity relationships mation of voltage-dependent pores in biological membranes [8][9][10], although recent evidence indicates that the inhibition of the outgrowth of spores by nisin and subtilin takes place by a different mechanism [11,12]. We have been studying the structure-activity relationships in nisin and subtilin, by both genetic and chemical modification of the structure [12][13][14][15][16][17][18][19][20], with a view to understanding their mechanism of action and to developing new derivatives with desirable properties. We now report the preparation, characterisation and anti-bacterial activity of a number of proteolytic fragments of nisin and subtilin, which allow us to define the parts of the molecule most important for biological activity. Materials and methodsNisin and subtilin were prepared as previously described [14,15]; [Ser33]-nisin, in which the serine residue at position 33 has escaped processing to a dehydroalanine residue, was isolated as a minor component of commercial nisin. All proteases were obtained from Sigma Chemical Co., Poole, Dorset, UK. ~. IntroductionThe post-translationally modified peptide antibiotics known :ts 'lantibiotics' contain cyclic structures formed by lanthioaine or 3-methyl-lanthionine residues, and often also dehydroalanine and/or dehydrobutyrine residues [1]. The first lan-!ibiotic to be characterised was nisin, produced by strains of Lactococcus lactis carrying a transposon containing genes coding for the nisin precursor and for proteins involved in aisin biosynthesis and resistance [2][3][4][5]. Nisin has been quite videly used as a food preservative, notably in cheese and ,~ther dairy products and in canned vegetables, for some 30 .,ears [6,7]. It inhibits the growth of a wide range of Gram~ositive organisms, and also inhibits the germination and/or mtgrowth of spores of Bacillus and Clostridium species [6]. Fhe growth-inhibitory activity of nisi...

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“…The highly modified mature peptide of 34 amino acid residues contains several uncommon features, such as lanthionine and β-methyllanthionine residues forming five intramolecular thioether bridges, and the dehydrated residues dehydro-alanine and dehydro-butyrine, derived from Ser and Thr residues, respectively (Gross and Morell, 1971;Hurst, 1981). It has been shown that removal of the highly charged leader peptide of 23 residues is the last step in the maturation of nisin, and that this step requires a specific, extracellular leader peptidase (Van der Meer et aI., 1993.…”

Section: Introductionmentioning

confidence: 99%

Homology modelling of the Lactococcus lactis leader peptidase NisP and its interaction with the precursor of the lantibiotic nisin

Siezen¹,

Rollema²,

Kuipers³

et al. 1995

Protein Eng Des Sel

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Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 12-05-2018Protein Engineering vol.8 no.2 pp. [117][118][119][120][121][122][123][124][125] 1995 Homology modelling of the Lactococcus lactis leader peptidase NisP and its interaction with the precursor of the lantibiotic nisin ITo whom correspondence should be addressed A model is presented for the 3-D structure of the catalytic domain of the putative leader peptidase NisP of Lactococcus lactis, and the interaction with its specific substrate, the precursor of the lantibiotic nisin. This homology model is based on the crystal structures of subtilisin BPN' and thermitase in complex with the inhibitor eglin. Predictions are made of the general protein fold, inserted loops, Ca2+ binding sites, aromatic interactions and electrostatic interactions of NisP. Cleavage of the leader peptide from precursor nisin by NisP is the last step in maturation of nisin. A detailed prediction of the substrate binding site attempts to explain the basis of specificity of NisP for precursor nisin. Specific acidic residues in the SI sub site of the substrate binding region of NisP appear to be of particular importance for electrostatic interaction with the PI Arg residue of precursor nisin after which cleavage occurs. The hydrophobic S4 subsite of NisP may also contribute to substrate binding as it does in subtilisins. Predictions of enzyme-substrate interaction were tested by protein engineering of precursor nisin and determining susceptibility of mutant precursors to cleavage by NisP. An unusual property of NisP predicted from this catalytic domain model is a surface patch near the substrate binding region which is extremely rich in aromatic residues. It may be involved in binding to the cell membrane or to hydrophobic membrane proteins, or it may serve as the recognition and binding region for the modified, hydrophobic C-terminal segment of precursor nisin. Similar predictions for the tertiary structure and substrate binding are made for the highly homologous protein EpiP, the putative leader peptidase for the lantibiotic epidermin from Staphylococcus epidermidis, but EpiP lacks the aromatic patch. Based on these models, protein engineering can be employed not only to test the predicted enzyme-substrate interactions, but also to design lantibiotic leader peptidases with a desired specificity.

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Structure of nisin

Cited by 573 publications

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Isolation and Characterization of Pediocin NV 5 Producing Pediococcus acidilactici LAB 5 from Vacuum-Packed Fermented Meat Product

Isolation and Characterization of Pediocin NV 5 Producing Pediococcus acidilactici LAB 5 from Vacuum-Packed Fermented Meat Product

Structure‐activity relationships in the peptide antibiotic nisin: antibacterial activity of fragments of nisin

Homology modelling of the Lactococcus lactis leader peptidase NisP and its interaction with the precursor of the lantibiotic nisin

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