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Biosynthesis of the lantibiotic mersacidin: organization of a type B lantibiotic gene cluster

Article Abstract:

Research has been conducted on the biosynthetic gene cluster of mersacidin. The complete sequence of the type B lantibiotic gene cluster is described.

Author: Altena, Karsten, Guder, Andre, Cramer, Claudia, Bierbaum, Gabriele
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
Germany, Statistical Data Included, Biosynthesis, Chromosomes, Microbiological research, Tetracycline, Tetracyclines

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The lantibiotic mersacidin is an autoinducing peptide

Article Abstract:

A SigH knockout is constructed to investigate the influence of the alternative sigma factor H on mersacidin biosynthesis. The knockout mutant is asporogenous and a comparison to the wild-type strain indicated no significant differences concerning mersacidin production and immunity.

Author: Bierbaum, Gabriele, Szekat, Christiane, Hoffmann, Anja, Schmitz, Stephanie, Rudd, Brian
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2006
United Kingdom, Science & research, Drugs, In-Vitro Diagnostic Substance Manufacturing, Bacterial Culture Products, Physiological aspects, Growth, Polymerase chain reaction, Bacillus (Bacteria), Bacillus, Peptide synthesis, Bacteriology, Oligopeptides, Bacterial cultures, Company growth, Chemical properties

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Engineering of a novel thioether bridge and role of modified residues in the lantibiotic Pep5

Article Abstract:

The insertion of a new methyllanthionine and a didehydroalanine into the flexible portion of the peptide Pep5 decreases the peptide's antimicrobial activity. The Pep5, produced by Staphylococcus epidermis 5, contains the thioether amino acids, lanthionine and methyllanthionine, in three ring structures. Peptides without the ring structures are susceptible to proteolysis, indicating that the rings are necessary for proteolytic stability. The introduction of a thioether in Pep5 increases proteolytic stability, but decreases antimicrobial activity.

Author: Jung, Gunther, Bierbaum, Gabriele, Szekat, Christiane, Sahl, Hans-Georg, Josten, Michaele, Heidrich, Christoph, Kempter, Christoph
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
Observations, Protein engineering, Staphylococcus

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Subjects list: Research, Analysis, Peptides
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