Expression of an active adenylate‐forming domain of peptide synthetases corresponding to acyl‐CoA‐synthetases

FEBS Letters

van Liempt, Henk¹  Dieckmann, Ralf¹  Kleinkauf, Horst¹  Lee, Yoen-Ok¹  von Döhren, Hans¹ 

[1] Institut für Biochemie und Molekulare Biologie, Technische Universität Berlin, Franklinstrasse 29, 10587 Berlin, Germany

关键词: Tyrocidine synthetase;    Multienzyme;    Peptide synthetase;    Acyl-CoA-synthetase;    Panthetheine;    CoA;   

DOI  :  10.1016/0014-5793(94)01342-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 1629 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.

【 授权许可】

Unknown