Structural, biochemical and bioinformatic analyses of nonribosomal peptide synthetase adenylation domains.

Jaclyn M Winter, Stephanie C Heard

Journal: Natural product reports 2024;41(7):1180-1205

PMID: 38488017

Abstract

Covering: 1997 to July 2023The adenylation reaction has been a subject of scientific intrigue since it was first recognized as essential to many biological processes, including the homeostasis and pathogenicity of some bacteria and the activation of amino acids for protein synthesis in mammals. Several foundational studies on adenylation (A) domains have facilitated an improved understanding of their molecular structures and biochemical properties, in particular work on nonribosomal peptide synthetases (NRPSs). In NRPS pathways, A domains activate their respective acyl substrates for incorporation into a growing peptidyl chain, and many nonribosomal peptides are bioactive. From a natural product drug discovery perspective, improving existing bioinformatics platforms to predict unique NRPS products more accurately from genomic data is desirable. Here, we summarize characterization efforts of A domains primarily from NRPS pathways from July 1997 up to July 2023, covering protein structure elucidation, assay development, and tools for improved predictions.

Address: Department of Pharmacology and Toxicology, University of Utah, Salt Lake City, UT 84112, USA. [email protected].

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