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Delineation of key amino acid chains and peptide domains for antimicrobial properties of divercin V41, a pediocin-like bacteriocin secreted by Canobacterium divergens V41

Article Abstract:

A study has revealed that antilisterial peptide Divercin V41, produced by Carnobacterium divergens V41, is homologous to pediocin PA-1 and contains two disulfide bonds. Such compounds have been found to useful in human applications and may provide new approaches for dealing with antibiotic-resistant bacteria. Membrane-active peptide cationicity is important for membrane insertions since these substance interact strongly with anionic membrane phospholipids.

Author: Molle, Daniel, Boyaval, Patrick, Marion, Didier, Dousset, Xavier, Bhugaloo-vial, Parwin, Douliez, Jean-Paul
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
Antibiotics, Antibacterial agents, Microorganisms, Listeria

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(Omega)-amino acid:pyruvate transaminase from alcaligenes denitrificans Y2k-2: a new catalyst for kinetic resolution of (beta)-amino acids and amines

Article Abstract:

Selective enrichment and screening of soil samples containing (omega)-amino acid:pyruvate transaminase activity was undertaken for obtaining alcaligenes denitrificans Y2k-2 and kinetically resolve aliphatic (beta)-amino acid and form the clone of the corresponding structural gene (aptA). The study resulted in the characterization of the basic properties of a new L-stereospecific (omega)-APT.

Author: Yun, Hyungdon, Lim, Seongyop, Cho, Byung-Kwan, Kim, Byung-Gee
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2004
Pyruvates

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Binding of pediocin PA-1 with anionic lipid induces model membrane destabilization

Article Abstract:

A study on the effects of pediocin PA-1 on model membranes is reported. The findings show that the association with the membrane interface of dimyristoylphosphatidylcholine (DMPG) does not affect the conformation of the peptide, the adsorption inducing a more folded structure.

Author: Gaussier, Helene, Lefevre, Thierry, Subirade, Muriel
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2003
Usage, Fourier transform infrared spectroscopy, Structure

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Subjects list: Research, Peptides, Amino acids
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