{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Del Rio Flores A"],"funding":["National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["824-834"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9905339"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["62(3)"],"pubmed_abstract":["Isonitrile lipopeptides (INLPs) are known to be related to the virulence of pathogenic mycobacteria by mediating metal transport, but their biosynthesis remains obscure. In this work, we use in vitro biochemical assays, site-directed mutagenesis, chemical synthesis, and spectroscopy techniques to scrutinize the activity of core enzymes required for INLP biosynthesis in mycobacteria. Compared to environmental <i>Streptomyces</i>, pathogenic <i>Mycobacterium</i> employ a similar chemical logic and enzymatic machinery in INLP biosynthesis, differing mainly in the fatty-acyl chain length, which is controlled by multiple enzymes in the pathway. Our in-depth study on the non-heme iron(II) and α-ketoglutarate-dependent dioxygenase for isonitrile generation, including Rv0097 from <i>Mycobacterium "],"journal":["Biochemistry"],"pubmed_title":["Biosynthesis of Isonitrile Lipopeptide Metallophores from Pathogenic Mycobacteria."],"pmcid":["PMC9905339"],"funding_grant_id":["R01 GM136758","R01GM136758"],"pubmed_authors":["De Matias K","Zhang W","Narayanamoorthy M","Zhai R","Seshadri K","Del Rio Flores A","Shen Y","Xue Z","Yang S","Cai W"],"additional_accession":[]},"is_claimable":false,"name":"Biosynthesis of Isonitrile Lipopeptide Metallophores from Pathogenic Mycobacteria.","description":"Isonitrile lipopeptides (INLPs) are known to be related to the virulence of pathogenic mycobacteria by mediating metal transport, but their biosynthesis remains obscure. In this work, we use in vitro biochemical assays, site-directed mutagenesis, chemical synthesis, and spectroscopy techniques to scrutinize the activity of core enzymes required for INLP biosynthesis in mycobacteria. Compared to environmental <i>Streptomyces</i>, pathogenic <i>Mycobacterium</i> employ a similar chemical logic and enzymatic machinery in INLP biosynthesis, differing mainly in the fatty-acyl chain length, which is controlled by multiple enzymes in the pathway. Our in-depth study on the non-heme iron(II) and α-ketoglutarate-dependent dioxygenase for isonitrile generation, including Rv0097 from <i>Mycobacterium ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2026-05-29T05:35:54.459Z","creation":"2025-04-04T11:50:02.707Z"},"accession":"S-EPMC9905339","cross_references":{"pubmed":["36638317"],"doi":["10.1021/acs.biochem.2c00611"]}}