Dipeptide synthesis by an isolated adenylate-forming domain of non-ribosomal peptide synthetases (NRPS).
A deletion mutant of tyrocidine synthetase 1 (DeltaDeltaTY1), 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.
Dieckmann
R
R
Max-Volmer-Institut für Biophysikalische Chemie und Biochemie, Technische Universität Berlin, Germany.
Neuhof
T
T
Pavela-Vrancic
M
M
von Döhren
H
H
D000225:Adenine / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D004151:Dipeptides / Q000096:biosynthesis*; D004926:Escherichia coli; D010453:Peptide Synthases / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary
D004151:Dipeptides; D010453:Peptide Synthases; C104385:non-ribosomal peptide synthase; D000225:Adenine