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Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.
This review presents recommended nomenclature for the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), a rapidly growing class of natural products. The…
Specific Binding of Nisin to the Peptidoglycan Precursor Lipid II Combines Pore Formation and Inhibition of Cell Wall Biosynthesis for Potent Antibiotic Activity*
- I. Wiedemann, E. Breukink, +4 authors H. Sahl
- Biology, MedicineThe Journal of Biological Chemistry
- 19 January 2001
Genetically engineered nisin variants are used to identify the structural requirements for the interaction of the peptide with lipid II, and the remaining in vivo activity is found to result from the unaltered capacity of the mutated peptide to bind to lipid II and thus to inhibit its incorporation into the peptidoglycan network.
Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from gram-positive bacteria.
The fundamental aspects of the biosynthetic machinery, which include information for the antibiotic prepeptide, the modification enzymes and accessory functions such as dedicated proteases and ABC transporters as well as immunity factors and regulatory proteins, are discussed along with the biotechnological potential of the peptides and of the enzymes, which could be used for construction of novel, peptide-based biomedical effector molecules.
Lantibiotics: mode of action, biosynthesis and bioengineering.
In vitro modification systems have successfully been used to introduce thioether rings into other biologically active peptides and at least one promising new lantibiotic with strong activity against multiresistant pathogens has been described.
Biosynthesis and biological activities of lantibiotics with unique post-translational modifications.
Lantibiotics are biologically active peptides which contain the thioether amino acid lanthionine as well as several other modified amino acids which are synthesised on the ribosome as a prepeptide which undergoes several post-translational modification events, including dehydration of specific hydroxyl amino acids to form dehydroamino acids.
Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of PepP and PepC. Evidence for a role of PepC in thioether formation.
- C. Meyer, G. Bierbaum, +6 authors H. Sahl
- Biology, MedicineEuropean journal of biochemistry
- 1 September 1995
It is demonstrated that PepC is a thioether-forming protein and strongly suggest that PepB is responsible for dehydration of serine and threonine in the cells without excretion of processed peptide.
Matrix-Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry for Fast and Reliable Identification of Clinical Yeast Isolates
- G. Marklein, M. Josten, +8 authors H. Sahl
- Biology, MedicineJournal of Clinical Microbiology
- 1 July 2009
Overall, MALDI-TOF MS proved a most rapid and reliable tool for the identification of yeasts and yeast-like fungi, with the method providing a combination of the lowest expenditure of consumables, easy interpretation of results, and a fast turnaround time.
Biosynthesis of the Lantibiotic Mersacidin: Organization of a Type B Lantibiotic Gene Cluster
- K. Altena, A. Guder, C. Cramer, G. Bierbaum
- Medicine, BiologyApplied and Environmental Microbiology
- 1 June 2000
The biosynthetic gene cluster of mersacidin, a lanthionine-containing antimicrobial peptide, is located on the chromosome of the producer, Bacillus sp.
Role of lipid‐bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics
Results demonstrate that, in vitro and in vivo, lipid II serves as a docking molecule for nisin and epidermin, but not for Pep5 and epilancin K7, and thereby facilitates the formation of pores in the cytoplasmic membrane.
The Lantibiotic Mersacidin Inhibits Peptidoglycan Synthesis by Targeting Lipid II
- H. Brötz, G. Bierbaum, K. Leopold, P. Reynolds, H. Sahl
- Biology, MedicineAntimicrobial Agents and Chemotherapy
- 1 January 1998
The interaction of mersacidin with lipid II apparently occurs via a binding site which is not targeted by any antibiotic currently in use, and in contrast to the glycopeptide antibiotics, complex formation does not involve the C-terminald-alanyl–d-alanine moiety of the lipid intermediate.