Premium
Characterization of the stereochemical configuration of lanthionines formed by the lanthipeptide synthetase G eo M
Author(s) -
Garg Neha,
Goto Yuki,
Chen Ting,
van der Donk Wilfred A.
Publication year - 2016
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22876
Subject(s) - chemistry , dehydroalanine , lantibiotics , stereochemistry , lanthionine , peptide , escherichia coli , biosynthesis , pentapeptide repeat , enzyme , ring (chemistry) , biochemistry , organic chemistry , nisin , gene , antimicrobial
The biosynthesis of the class II lanthipeptide geobacillin II was reconstituted in vitro . The purified precursor peptide was modified by the lanthipeptide synthetase GeoM at temperatures ranging between 37 and 80°C demonstrating the thermostability of the enzyme. Geobacillin II shares with cytolysin, haloduracin, and carnolysin a DhxDhxXxxXxxCys motif (Dhx = dehydroalanine or dehydrobutyrine) as precursor to its N‐terminal A‐ring. Like in these other three lantibiotics, the lanthionine in the A‐ring of geobacillin II had the LL stereochemical configuration as shown by chiral gas chromatography/mass spectrometry. Various analogues of geobacillin II were produced using co‐expression of mutants of the precursor peptide GeoAII and the synthetase GeoM in Escherichia coli . The findings in this study suggest that the stereochemical outcome of the A‐ring in geobacillin II is not solely dependent on the peptide sequence as previously suggested for haloduracin © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 834–842, 2016.