Post-translational modifications of lantibiotics.
Several newly reported post-translational modification reactions are involved in lantibiotic biosynthesis. A short overview of the present knowledge on the post-translational modifications and on the enzymes involved in lantibiotic biosynthesis is given. The oxidative decarboxylation of the epidermin precursor peptide EpiA is described in detail. The FMN-containing oxidoreductase EpiD is involved in the formation of the C-terminal S-[(Z)-2-aminovinyl]-D-cysteine residue of epidermin: under reducing conditions the side chain of the C-terminal cysteine residue of EpiA is converted to an enethiol. EpiD has no absolute substrate specificity and can be used for modification of peptides having the C-terminal consensus motif [V/I/L/(M)/F/Y/W]-[A/S/V/T/C/(I/L)]-C.
Kupke
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Mikrobielle Genetik, Universität Tübingen, Germany.
Götz
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D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000378:metabolism*; D001430:Bacteriocins; D002262:Carboxy-Lyases; D003653:Decarboxylation; D005420:Flavoproteins / Q000378:metabolism; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism; D010443:Peptide Chain Termination, Translational; D010455:Peptides; D011499:Protein Processing, Post-Translational
D000900:Anti-Bacterial Agents; D001430:Bacteriocins; D005420:Flavoproteins; D010455:Peptides; C050558:epidermin; D010088:Oxidoreductases; C075971:epidermin decarboxylase; D002262:Carboxy-Lyases