Prerequisites of Isopeptide Bond Formation in Microcystin Biosynthesis.
Chembiochem
; 18(24): 2376-2379, 2017 12 14.
Article
em En
| MEDLINE
| ID: mdl-29024253
ABSTRACT
The biosynthesis of the potent cyanobacterial hepatotoxin microcystin involves isopeptide bond formation through the carboxylic acid side chains of d-glutamate and ß-methyl d-aspartate. Analysis of the in vitro activation profiles of the two corresponding adenylation domains, McyE-A and McyB-A2 , 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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Base de dados:
MEDLINE
Assunto principal:
Cianobactérias
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Biossíntese de Peptídeos Independentes de Ácido Nucleico
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Microcistinas
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article