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Dipeptide synthesis by an isolated adenylate‐forming domain of non‐ribosomal peptide synthetases (NRPS)
Author(s) -
Dieckmann Ralf,
Neuhof Torsten,
Pavela-Vrancic Maja,
von Döhren Hans
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02471-1
Subject(s) - adenylylation , adenylate kinase , dipeptide , peptide , ribosomal rna , biochemistry , peptide bond , amino acid , peptide biosynthesis , stereochemistry , biology , chemistry , enzyme , biosynthesis , rna , ribosome , gene
A deletion mutant of tyrocidine synthetase 1 (ΔΔTY1), comprising the adenylation domain of TY1 as an independent functional adenylate‐forming unit, was used to investigate the ability of the adenylation domain in non‐ribosomal peptide synthetases to catalyse peptide bond formation from the aminoacyl adenylate intermediate. The results demonstrate that only one substrate amino acid needs to be activated as an aminoacyl adenylate. In view of the potential exploitation of peptide synthetases for enzymatic synthesis of dipeptides of choice, it is important to note that this does not necessarily require a dimodular construct or an intermediate acyl transfer step.