nisin

Nisin is a polycyclic antibacterial peptide produced by the bacterium Lactococcus lactis that is used as a food preservative. It has 34 amino acid residues, including the uncommon amino acids lanthionine (Lan), methyllanthionine (MeLan), didehydroalanine (Dha), and didehydroaminobutyric acid (Dhb). These unusual amino acids are introduced by posttranslational modification of the precursor peptide. In these reactions a ribosomally synthesized 57-mer is converted to the final peptide. The unsaturated amino acids originate from serine and threonine, and the enzyme-catalysed addition of cysteine r

Chemical data

Formula: C143H230N42O37S7
Molecular weight: 3354.1 g/mol
IUPAC name: (2S)-6-amino-2-[2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(1R,4S,7R,11R,14S,17R)-7-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-4-amino-2-[[(3R,9S,12S,15S,21S)-21-[[(2R)-6-amino-2-[[(3R,7R,13S)-3-[[(3R,6S,12S,15R)-15-[[(E)-2-[[(2S,3S)-2-amino-3-methylpentanoyl]amino]but-2-enoyl]amino]-12-[(2S)-butan-2-yl]-9-methylidene-6-(2-methylpropyl)-5,8,11,14-tetraoxo-1-thia-4,7,10,13-tetrazacyclohexadecane-3-carbonyl]amino]-4-methyl-2,9,12-trioxo-5-thia-1,8,11-triazabicyclo[11.3.0]hexadecane-7-carbonyl]amino]hexanoyl]amino]-15,22-dimethyl-12-(2-methylpropyl)-9-(2-methylsulfanylethyl)-5,8,11,14,17,20-hexaoxo-1-thia-4,7,10,13,16,19-hexazacyclodocosane-3-carbonyl]amino]-4-oxobutanoyl]amino]-4-methylsulfanylbutanoyl]amino]hexanoyl]amino]-14-(1H-imidazol-5-ylmethyl)-4,8,20-trimethyl-3,6,12,15,21-pentaoxo-9,19-dithia-2,5,13,16,22-pentazabicyclo[9.9.2]docosane-17-carbonyl]amino]-3-hydroxypropanoyl]amino]-3-methylpentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-methylbutanoyl]amino]prop-2-enoylamino]hexanoic acid
SMILES: CC[C@H](C)[C@H]1C(=O)NC(=C)C(=O)N[C@H](C(=O)N[C@@H](CSC[C@@H](C(=O)N1)NC(=O)/C(=C\C)/NC(=O)[C@H]([C@@H](C)CC)N)C(=O)N[C@H]2C(SC[C@H](NC(=O)CNC(=O)[C@@H]3CCCN3C2=O)C(=O)N[C@H](CCCCN)C(=O)N[C@@H]4C(SC[C@H](NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)CNC4=O)C)CC(C)C)CCSC)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@H]5C(SC[C@H]6C(=O)N[C@H](C(=O)N[C@@H](CSC([C@@H](C(=O)N6)NC(=O)[C@@H](NC5=O)C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC7=CN=CN7)C(=O)N[C@@H](C(C)C)C(=O)NC(=C)C(=O)N[C@@H](CCCCN)C(=O)O)CC8=CN=CN8)C)C)C)CC(C)C
InChIKey: NVNLLIYOARQCIX-ILAIHEEGSA-N
XLogP: -6.1
Polar surface area: 1390 Å²
H-bond donors: 41
H-bond acceptors: 50
Formal charge: 0

via PubChem

Research

3,168 papers

After a century of nisin research - where are we now?FEMS microbiology reviews · 2023
Nisin-relevant antimicrobial peptides: synthesis strategies and applications.Food & function · 2024
Nisin variants: What makes them different and unique?Peptides · 2024
Nisin: From a structural and meat preservation perspective.Food microbiology · 2023
Nisin-A lantibiotic with immunomodulatory properties: A review.Peptides · 2021

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Wikidata facts

Show 2 more facts

chemical formula: C₁₄₃H₂₃₀N₄₂O₃₇S₇
Commons category: Nisin

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Article

7 sections

Contents

Properties
Applications
Food production
Other
Further reading
References
External links

Subtilin and epidermin are related to nisin. All are members of a class of molecules known as lantibiotics. A recent study has highlighted that the genetic capacity to produce nisin is more widespread than previously thought with over 100 species predicted to encode the genes to produce the peptide.