Format

Send to:

Choose Destination
See comment in PubMed Commons below
Antonie Van Leeuwenhoek. 2010 May;97(4):319-33. doi: 10.1007/s10482-010-9418-4. Epub 2010 Feb 6.

Microbial engineering of dehydro-amino acids and lanthionines in non-lantibiotic peptides.

Author information

  • 1BiOMaDe Technology Foundation, Nijenborgh 4, Groningen, The Netherlands. Moll@biomade.nl

Abstract

This minireview focuses on the use of bacteria to introduce dehydroresidues and (methyl)lanthionines in (poly)peptides. It mainly describes the broad exploitation of bacteria containing lantibiotic enzymes for the engineering of these residues in a wide variety of peptides in particular in peptides unrelated to lantibiotics. Lantibiotic dehydratases dehydrate serines and threonines present in peptides preceded by a lantibiotic leader peptide thus forming dehydroalanine and dehydrobutyrine, respectively. These dehydroresidues can be coupled to cysteines thus forming (methyl)lanthionines. This coupling is catalysed by lantibiotic cyclases. The design, synthesis, and export of microbially engineered dehydroresidue and or lanthionine-containing peptides in non-lantibiotic peptides are reviewed, illustrated by some examples which demonstrate the high relevance of these special residues. This minireview is the first with special focus on the microbial engineering of nonlantibiotic peptides by exploiting lantibiotic enzymes.

PMID:
20140513
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer
    Loading ...
    Write to the Help Desk