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The Antimicrobial peptide databases may be divided into two categories on the basis of the source of peptides it contains, as specific databases and general databases. These databases have various tools for antimicrobial peptides analysis and prediction. For example, the APD has a widely used calculation interface.
Pages in category "Antimicrobial peptides" The following 54 pages are in this category, out of 54 total. This list may not reflect recent changes. ...
Bacitracin is a polypeptide antibiotic derived from a bacterium, Bacillus subtilis, and acts against bacteria through the inhibition of cell wall synthesis. [6] It does this by inhibiting the removal of phosphate from lipid compounds, thus deactivating its function to transport peptidoglycan; the main component of bacterial cell membranes, to the microbial cell wall.
Bacillus amyloliquefaciens is a species of bacterium in the genus Bacillus that is the source of the BamHI restriction enzyme. It also synthesizes a natural antibiotic protein barnase, a widely studied ribonuclease that forms a famously tight complex with its intracellular inhibitor barstar, and plantazolicin, an antibiotic with selective activity against Bacillus anthracis.
Class IIa bacteriocins have a large potential for use in food preservation as well medical applications due to their strong anti-Listeria activity and broad range of activity. One example of Class IIa bacteriocin is pediocin PA-1. [13] The class IIb bacteriocins (two-peptide bacteriocins) require two different peptides for activity.
The antimicrobial resistance crisis also extends to the food industry, specifically with food producing animals. With an ever-increasing human population, there is constant pressure to intensify productivity in many agricultural sectors, including the production of meat as a source of protein. [ 57 ]
The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (involved in formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (involved in cross-linking of the peptide subunits) and the serine at the active site is conserved in all members of the PBP family.
This peptide consists of a core peptide segment which is typically preceded (and occasionally followed) by a leader peptide segment and is typically ~20-110 residues long. The leader peptide is usually important for enabling enzymatic processing of the precursor peptide via aiding in recognition of the core peptide by biosynthetic enzymes and ...