One-pot synthesis of 2,5-diketopiperazine with high titer and versatility using adenylation enzyme

Nonribosomal peptide synthetases, consisting of multiple catalytic domains, are involved in the biosynthesis of an important family of bioactive natural products in a coordinated manner. Among the functional domains, adenylation domains are specifically responsible for recognizing carboxylic acid building blocks and synthesizing aminoacyl adenylates. Given their critical roles in the biosynthesis of the growing peptide, A-domains are also referred to as the “gatekeeper”. In this review, very recent developments in the A-domains from NRPSs are reviewed to expand the fundamental knowledge of the A domain, including knowledge on the structures, functions, and molecular interactions. Several recent examples were also discussed to highlight the great .potential of A-domain engineering. This study should provide a framework for the combinatorial biosynthesis or synthetic biology-driven microbial production of novel nonribosomal peptides.

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One-pot synthesis of 2,5-diketopiperazine with high titer and versatility using adenylation enzyme

Cited by 2 publications

References 33 publications

Crosslinking intermodular condensation in non-ribosomal peptide biosynthesis

Crosslinking intermodular condensation in non-ribosomal peptide biosynthesis

Engineered Biosynthesis through the Adenylation Domains from Nonribosomal Peptide Synthetases

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