Prerequisites of Isopeptide Bond Formation in Microcystin Biosynthesis

  • The biosynthesis of the potent cyanobacterial hepatotoxin microcystin involves isopeptide bond formation through the carboxylic acid side chains of d-glutamate and -methyl d-aspartate. Analysis of the in vitro activation profiles of the two corresponding adenylation domains, McyE-A and McyB-A(2), either in a didomain or a tridomain context with the cognate thiolation domain and the upstream condensation domain revealed that substrate activation of both domains strictly depended on the presence of the condensation domains. We further identified two key amino acids in the binding pockets of both adenylation domains that could serve as a bioinformatic signature of isopeptide bond-forming modules incorporating d-glutamate or d-aspartate. Our findings further contribute to the understanding of the multifaceted role of condensation domains in nonribosomal peptide synthetase assembly lines.

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Author:Sabine Meyer, Andi Mainz, Jan-Christoph KehrGND, Roderich Suessmuth, Elke DittmannORCiDGND
Pubmed Id:
Parent Title (English):ChemBioChem : a European journal of chemical biology
Place of publication:Weinheim
Document Type:Article
Year of first Publication:2017
Year of Completion:2017
Release Date:2020/05/15
Tag:amino acids; biosynthesis; cyanobacteria; nonribosomal peptide; substrate specificity
First Page:2376
Last Page:2379
Funder:Cluster of Excellence, Unifying Concepts in Catalysis (UniCAT); German Research Foundation (DFG)
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer Review:Referiert
Licence (German):License LogoKeine Nutzungslizenz vergeben - es gilt das deutsche Urheberrecht