Microbial engineering of dehydro-amino acids and lanthionines in non-lantibiotic peptides.
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.
Moll
Gert N
GN
BiOMaDe Technology Foundation, Nijenborgh 4, Groningen, The Netherlands. Moll@biomade.nl
Kuipers
Anneke
A
Rink
Rick
R
D000409:Alanine / Q000031:analogs & derivatives* / Q000096:biosynthesis; D000596:Amino Acids / Q000096:biosynthesis*; D001419:Bacteria / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D053898:Biosynthetic Pathways / Q000235:genetics*; D005818:Genetic Engineering; D014176:Protein Biosynthesis; D013440:Sulfides
D000596:Amino Acids; D013440:Sulfides; C001520:lanthionine; D000409:Alanine