ArticleThe Journal of biological chemistry2011
Substrate recognition and specificity of the NisB protein, the lantibiotic dehydratase involved in nisin biosynthesis.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 64 citations in OpenAlex.
- Article
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Structural insights into the substrate binding mechanism of the class I dehydratase MadB.Communications biology · 2025Article
- α-N-Methyltransferase regiospecificity is mediated by proximal, redundant enzyme-substrate interactions.Protein science : a publication of the Protein Society · 2025Article
- Development of chemically defined media for3 Biotech · 2023Article
- Changes in community structures and functions of the gut microbiomes of deep-sea cold seep mussels during in situ transplantation experiment.Animal microbiome · 2023Article
- Bioinformatic prediction and experimental validation of RiPP recognition elements.Methods in enzymology · 2023Article
- Macrophage-targeting oligopeptides fromChemical science · 2022Article
- Substrate Recognition by the Peptidyl-(ACS chemical biology · 2022Article
- Analysis of Cross-Functionality within LanBTC Synthetase Complexes from Different Bacterial Sources with Respect to Production of Fully Modified Lanthipeptides.Applied and environmental microbiology · 2022Article
- The structure of MadC fromFrontiers in microbiology · 2022Article
- Article
- Article
- Structural Analysis of Class I Lanthipeptides fromACS chemical biology · 2021Article
- Microbiome-wide association studies reveal correlations between the structure and metabolism of the rhizosphere microbiome and disease resistance in cassava.Plant biotechnology journal · 2021Article
- Article
- Article
- Impact of the nisin modification machinery on the transport kinetics of NisT.Scientific reports · 2020Article
- Substrate Recognition by the Class II Lanthipeptide Synthetase HalM2.ACS chemical biology · 2020Article
- A Structural View on the Maturation of Lanthipeptides.Frontiers in microbiology · 2020Review
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nisin is a posttranslationally modified antimicrobial peptide containing the cyclic thioether amino acids lanthionine and methyllanthionine. Although much is known about its antimicrobial activity and mode of action, knowledge about the nisin modification process is still rather limited. The dehydratase NisB is believed to be the initial interaction partner in modification. NisB dehydrates specific serine and threonine residues in prenisin, whereas the cyclase NisC catalyzes the (methyl)lanthionine formation. The fully modified prenisin is exported and the leader peptide is cleaved off by the extracellular protease NisP. Light scattering analysis demonstrated that purified NisB is a dimer in solution. Using size exclusion chromatography and surface plasmon resonance, the interaction of NisB and prenisin, including several of its modified derivatives, was studied. Unmodified prenisin binds to NisB with an affinity of 1.05 ± 0.25 μm, whereas the dehydrated and the fully modified derivatives bind with respective affinities of 0.31 ± 0.07 and 10.5 ± 1.7 μm. The much lower affinity for the fully modified prenisin was related to a >20-fold higher off-rate. For all three peptides the stoichiometry of binding was 1:1. Active nisin, which is the equivalent of fully modified prenisin lacking the leader peptide did not bind to NisB, nor did prenisin in which the highly conserved FNLD box within the leader peptide was mutated to AAAA. Taken together our data indicate that the leader peptide is essential for initial recognition and binding of prenisin to NisB.
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