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However, total output from heterologous production pathways can suffer from low flux, enzyme promiscuity, formation of toxic intermediates, or intermediate loss to competing reactions, which ultimately hinder their full potential. The self-assembling, easy-to-modify, protein-based bacterial microcompartments (BMCs) offer a sophisticated way to overcome these obstacles by acting as an autonomous catalytic module decoupled from the cell's regulatory and metabolic networks. More than a decade of fundamental research on various types of BMCs, particularly structural studies of shells and their self-assembly, the recruitment of enzymes to BMC shell scaffolds, and the involvement of ancillary proteins such as transporters, regulators, and activating enzymes in the integration of BMCs into the cell's metabolism, has significantly moved the field forward. These advances have enabled bioengineers to design synthetic multi-enzyme BMCs to promote ethanol or hydrogen production, increase cellular polyphosphate levels, and convert glycerol to propanediol or formate to pyruvate. These pioneering efforts demonstrate the enormous potential of synthetic BMCs to encapsulate non-native multi-enzyme biochemical pathways for the synthesis of high-value products.<\/jats:p>","DOI":"10.1042\/bst20230229","type":"journal-article","created":{"date-parts":[[2024,5,30]],"date-time":"2024-05-30T10:43:05Z","timestamp":1717065785000},"page":"997-1010","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":29,"title":["Bacterial microcompartments as a next-generation metabolic engineering tool: utilizing nature's solution for confining challenging catabolic pathways"],"prefix":"10.1042","volume":"52","author":[{"given":"Lior","family":"Doron","sequence":"first","affiliation":[{"name":"1MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9977-8482","authenticated-orcid":false,"given":"Cheryl A.","family":"Kerfeld","sequence":"additional","affiliation":[{"name":"1MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI, U.S.A."},{"name":"2Environmental Genomics and Systems Biology and Molecular Biophysics and Integrative Bioimaging Divisions, Lawrence Berkeley National Laboratory, Berkeley, CA, U.S.A."},{"name":"3Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, U.S.A."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2024,5,30]]},"reference":[{"key":"2024062609213611000_BST-2023-0229CC1","doi-asserted-by":"publisher","first-page":"98","DOI":"10.1111\/1751-7915.13292","article-title":"Chasing bacterial chassis for metabolic engineering: a perspective review from classical to non-traditional microorganisms","volume":"12","year":"2018","journal-title":"Microb. 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