On the substrate specificity of dehydration by lacticin 481 synthetase

Research output: Contribution to journalArticle

Abstract

Dehydroamino acids are valuable building blocks that are a challenge to incorporate synthetically into unprotected peptides. Lantibiotic synthetases possess dehydration activity that converts Ser and Thr residues in their peptide substrates into dehydroalanine and dehydrobutyrine residues, respectively. We show here that lacticin 481 synthetase can convert the Thr analogues (R)-3-EtSer, (R)-3-vinylSer, (R)-3-ethynylSer, (R)-3-[(E)-propenyl]Ser, and (R)-3-propynylSer into the corresponding dehydroamino acids when incorporated into its peptide substrate. This relaxed substrate specificity holds promise for using the enzyme for synthetic purposes and for lantibiotic engineering. On the other hand, (R)-3-PrSer, (R)-3-iPrSer, and allo-Thr are not substrates for the enzyme.

Original languageEnglish (US)
Pages (from-to)2212-2213
Number of pages2
JournalJournal of the American Chemical Society
Volume129
Issue number8
DOIs
StatePublished - Feb 28 2007

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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