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• W2034379310 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." @default.
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• W2034379310 date "1995-01-03" @default.
• W2034379310 modified "2023-10-14" @default.
• W2034379310 title "Expression of an active adenylate-forming domain of peptide synthetases corresponding to acyl-CoA-synthetases" @default.
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• W2034379310 doi "https://doi.org/10.1016/0014-5793(94)01342-x" @default.
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