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Cover Picture: Investigation of the Substrate Specificity of Lacticin 481 Synthetase by Using Nonproteinogenic Amino Acids (ChemBioChem 5/2009)
Author(s) -
Levengood Matthew R.,
Kerwood Christopher C.,
Chatterjee Champak,
van der Donk Wilfred A.
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200990014
Subject(s) - lantibiotics , peptide , chemistry , amino acid , stereochemistry , peptide bond , enzyme , thioether , biochemistry , bacteriocin , organic chemistry , antimicrobial
The cover picture shows the forgiveness of lacticin 481 synthetase with respect to its substrate specificity. This enzyme crosslinks Ser (red) and Cys (blue) residues in its precursor peptide through thioether bonds to generate the lantibiotic lacticin 481. Lantibiotics are currently used worldwide in the food industry, in particular in dairy products. Recent years have seen a growing interest in engineering of lantibiotics for potential use as human therapeutics. Towards this goal, the residues shown in green in the precursor peptide could be replaced by a variety of non‐proteinogenic amino acids, including peptoids and β‐amino acids, without affecting the enzymatic activity of lacticin 481 synthetase. The tolerance of lacticin 481 synthetase holds much promise for branching into lantibiotics with increased biostability. For further details, see the article by W. van der Donk et al. on p. 911 ff.