{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Sutter M"],"funding":["NIGMS NIH HHS"],"pubmed_abstract":["Bacterial microcompartments (BMCs) are prokaryotic organelles that consist of a protein shell which sequesters metabolic reactions in its interior. While most of the substrates and products are relatively small and can permeate the shell, many of the encapsulated enzymes require cofactors that must be regenerated inside. We have analyzed the occurrence of an enzyme previously assigned as a cobalamin (vitamin B<sub>12</sub>) reductase and, curiously, found it in many unrelated BMC types that do not employ B<sub>12</sub> cofactors. We propose NAD+ regeneration as a new function of this enzyme and name it MNdh, for Metabolosome NADH dehydrogenase. Its partner shell protein BMC-T<sup>SE</sup> assists in passing the generated electrons to the outside. We support this hypothesis with bioinformat"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2024.07.15.603600"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11275729"],"repository":["biostudies-literature"],"pubmed_title":["Electrochemical cofactor recycling of bacterial microcompartments."],"pmcid":["PMC11275729"],"funding_grant_id":["R01 GM126218","P30 GM124169"],"pubmed_authors":["Sutter M","Gupta S","Tefft NM","TerAvest MA","Utschig LM","Vermaas JV","Paul S","Poluektov OG","Hickey DP","Kerfeld CA","Niklas J","Ralston CY","Kahan DN","Ferlez BH"],"additional_accession":[]},"is_claimable":false,"name":"Electrochemical cofactor recycling of bacterial microcompartments.","description":"Bacterial microcompartments (BMCs) are prokaryotic organelles that consist of a protein shell which sequesters metabolic reactions in its interior. While most of the substrates and products are relatively small and can permeate the shell, many of the encapsulated enzymes require cofactors that must be regenerated inside. We have analyzed the occurrence of an enzyme previously assigned as a cobalamin (vitamin B<sub>12</sub>) reductase and, curiously, found it in many unrelated BMC types that do not employ B<sub>12</sub> cofactors. We propose NAD+ regeneration as a new function of this enzyme and name it MNdh, for Metabolosome NADH dehydrogenase. Its partner shell protein BMC-T<sup>SE</sup> assists in passing the generated electrons to the outside. We support this hypothesis with bioinformat","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-04-07T21:13:25.025Z","creation":"2025-04-19T14:38:49.663Z"},"accession":"S-EPMC11275729","cross_references":{"pubmed":["39071365"],"doi":["10.1101/2024.07.15.603600"]}}