![]() In vitro characterization of representatives from both families confirmed the ability of these enzymes to acetylate 5-ASA. This associated 12 previously uncharacterized microbial acetyltransferases with 5-ASA inactivation, belonging to two protein superfamilies: thiolases and acyl-CoA N-acyltransferases. To uncover the source of this metabolism, we developed a multi-omics workflow combining gut microbiome metagenomics, metatranscriptomics and metabolomics from the longitudinal IBDMDB cohort of 132 controls and patients with IBD. Identification of the responsible microbes and enzyme(s), however, has proved elusive. decades, variability in clinical efficacy of the widely used inflammatory bowel disease (IBD) drug 5-aminosalicylic acid (5-ASA) has been attributed, in part, to its acetylation and inactivation by gut microbes. Chan School of Public Health, Harvard University, Boston, MA, USA. 15 Department of Immunology & Infectious Disease, T. 14 Harvard Chan Microbiome in Public Health Center, T. 12 Broad Institute of MIT and Harvard, Cambridge, MA, USA.1 Division of Gastroenterology, Massachusetts General Hospital and Harvard Medical School, Boston, MA, USA. 11 Howard Hughes Medical Institute, Harvard University, Cambridge, MA, USA.10 Department of Cancer Biology, Dana-Farber Cancer Institute and Harvard Medical School, Boston, MA, USA.9 Department of Immunology & Infectious Disease, T.8 Resnick Sustainability Institute, California Institute of Technology, Pasadena, CA, USA. ![]() 7 Harvard Chan Microbiome in Public Health Center, T.5 Division of Pulmonary and Critical Care Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA, USA. ![]()
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