Post-translational modifications of lantibiotics
✍ Scribed by Thomas Kupke; Friedrich Götz
- Publisher
- Springer Netherlands
- Year
- 1996
- Tongue
- English
- Weight
- 1003 KB
- Volume
- 69
- Category
- Article
- ISSN
- 0003-6072
No coin nor oath required. For personal study only.
✦ Synopsis
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 l antibiotic biosynthesis is given. The oxidative decarboxylation of the epidermin precursor peptide EpiA is described in detail. The b'MN-containing oxidoreductase EpiD is involved in the formation of the C-terminal S-[(Z)-2-aminovinyl]-Dcysteine 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 [VIIILI(M)/FIY/W]-[AISNITICI(IIL)]-C.
📜 SIMILAR VOLUMES
Alterations in amino acid sequence can generate neo-epitopes from self proteins, causing autoaggressive immune attack. There is a range of possible post-translational modifications (PTMs) of mammalian proteins that can allow immune recognition of neo-self epitopes. These effects can vary from overt
A variety of different post-translational modifications of peptides displayed by class I and II MHC molecules have now been described. Some modifications promote the binding of peptides to MHC molecules, and might also influence the ability of the peptide to be produced by antigen processing pathway