ArticleJournal of bacteriology2012
Homologues and bioengineered derivatives of LtnJ vary in ability to form D-alanine in the lantibiotic lacticin 3147.
Article in Journal of bacteriology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.
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Who cites it
11 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.
- Roles of d-Amino Acids on the Bioactivity of Host Defense Peptides.International journal of molecular sciences · 2016Pooled it
- Discovery, Biosynthesis, and Characterization of Rodencin, a Two-Component Lanthipeptide, Harboring d-Amino Acids Introduced by the Unusual Dehydrogenase RodJJournal of natural products · 2024Article
- Antimicrobial Peptides as Immunomodulators and Antimycobacterial Agents to Combat Mycobacterium tuberculosis: a Critical Review.Probiotics and antimicrobial proteins · 2023Review
- Towards creating an extended metabolic model (EMM) for E. coli using enzyme promiscuity prediction and metabolomics data.Microbial cell factories · 2019Article
- Dehydroamino acids: chemical multi-tools for late-stage diversification.Organic & biomolecular chemistry · 2019Review
- Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.Chemical reviews · 2017Review
- Post-translational Introduction of D-Alanine into Ribosomally Synthesized Peptides by the Dehydroalanine Reductase NpnJ.Journal of the American Chemical Society · 2015Article
- Expanded natural product diversity revealed by analysis of lanthipeptide-like gene clusters in actinobacteria.Applied and environmental microbiology · 2015Article
- Lantibiotic Reductase LtnJ Substrate Selectivity Assessed with a Collection of Nisin Derivatives as Substrates.Applied and environmental microbiology · 2015Article
- High divergence of the precursor peptides in combinatorial lanthipeptide biosynthesis.ACS chemical biology · 2014Article
- Saturation mutagenesis of selected residues of the α-peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity.Microbial biotechnology · 2013Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ltnα and Ltnβ are individual components of the two-peptide lantibiotic lacticin 3147 and are unusual in that, although ribosomally synthesized, they contain d-amino acids. These result from the dehydration of l-serine to dehydroalanine by LtnM and subsequent stereospecific hydrogenation to d-alanine by LtnJ. Homologues of LtnJ are rare but have been identified in silico in Staphylococcus aureus C55 (SacJ), Pediococcus pentosaceus FBB61 (PenN), and Nostoc punctiforme PCC73102 (NpnJ, previously called NpunJ [P. D. Cotter et al., Proc. Natl. Acad. Sci. U. S. A. 102:18584-18589, 2005]). Here, the ability of these enzymes to catalyze d-alanine formation in the lacticin 3147 system was assessed through heterologous enzyme production in a ΔltnJ mutant. PenN successfully incorporated d-alanines in both peptides, and SacJ modified Ltnα only, while NpnJ was unable to modify either peptide. Site-directed mutagenesis was also employed to identify residues of key importance in LtnJ. The most surprising outcome from these investigations was the generation of peptides by specific LtnJ mutants which exhibited less bioactivity than those generated by the ΔltnJ strain. We have established that the reduced activity of these peptides is due to the inability of the associated LtnJ enzymes to generate d-alanine residues in a stereospecific manner, resulting in the presence of both d- and l-alanines at the relevant locations in the lacticin 3147 peptides.
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