PMID:7805893

Citation	Dieckmann, R, Lee, YO, van Liempt, H, von Döhren, H and Kleinkauf, H (1995) Expression of an active adenylate-forming domain of peptide synthetases corresponding to acyl-CoA-synthetases. FEBS Lett. 357:212-6
Abstract	Peptide synthetases and acyl-CoA-synthetases form acyl adenylates which are transferred to CoA or enzyme-bound pantetheine. To verify the existence of an adenylate domain in peptide synthetases, a 60.8 kDa fragment of tyrocidine 1-synthetase was constructed by a 1,629 bp deletion, expressed in Escherichia coli, and characterized. The truncated multienzyme activated phenylalanine and substrate analogues with comparable kinetics as the over-expressed synthetase, as judged by ATP-[32P]PP(i) exchange reaction. Thus the N-terminal domain resembling an acyl-CoA-synthetase is an autonomous structural element. This N-terminal domain is followed by a cofactor binding domain, resembling acyl carrier proteins involved in polyketide formation.
Links	PubMed
Keywords	Adenosine Monophosphate/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Amino Acids/metabolism; Binding Sites; Coenzyme A Ligases/chemistry; Coenzyme A Ligases/metabolism; Escherichia coli; Molecular Sequence Data; Peptide Synthases/chemistry; Peptide Synthases/genetics; Peptide Synthases/metabolism; Phenylalanine/metabolism; Phosphates/metabolism; Recombinant Proteins; Sequence Deletion; Sequence Homology, Amino Acid
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