Bioinformatic, structural, and biochemical analysis leads to the discovery of novel isonitrilases and decodes their substrate selectivity.

ABSTRACT: Bacterial species, such as Mycobacterium tuberculosis, utilize isonitrile-containing peptides (INPs) for trace metal trafficking, e.g., copper or zinc. Despite their importance, very few INP structures have been characterized to date. Reported INPs consist of a peptide backbone and β-isonitrile amide moieties. While the peptide backbone can be annotated using an adenylation domain predictor of non-ribosomal peptide synthetase (NRPS), determining the alkyl chain of β-isonitrile amide moieties remains challenging via conventional analytical techniques. In this study, we focus on non-heme iron and 2-oxoglutarate (Fe/2OG) dependent isonitrilases that exhibit inherent selectivity toward the alkyl chain length of the substrate, thus enabling the structural elucidation of INP

SUBMITTER: Hostetler T 

PROVIDER: S-EPMC11811631 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature