{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhan T"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["107243"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11061730"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["300(5)"],"pubmed_abstract":["Sterols are ubiquitous membrane constituents that persist to a large extent in the environment due to their water insolubility and chemical inertness. Recently, an oxygenase-independent sterol degradation pathway was discovered in a cholesterol-grown denitrifying bacterium Sterolibacterium (S.) denitrificans. It achieves hydroxylation of the unactivated primary C26 of the isoprenoid side chain to an allylic alcohol via a phosphorylated intermediate in a four-step ATP-dependent enzyme cascade. However, this pathway is incompatible with the degradation of widely distributed steroids containing a double bond at C22 in the isoprenoid side chain such as the plant sterol stigmasterol. Here, we have enriched a prototypical delta-24 desaturase from S. denitrificans, which catalyzes the electron ac"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Bacterial stigmasterol degradation involving radical flavin delta-24 desaturase and molybdenum-dependent C26 hydroxylase."],"pmcid":["PMC11061730"],"funding_grant_id":["235777276","SFB 1381"],"pubmed_authors":["Jacoby C","Gunter A","Muller M","Knapp B","Zhan T","Boll M","Ferlaino S","Weber S","Drepper F","Jede M"],"additional_accession":[]},"is_claimable":false,"name":"Bacterial stigmasterol degradation involving radical flavin delta-24 desaturase and molybdenum-dependent C26 hydroxylase.","description":"Sterols are ubiquitous membrane constituents that persist to a large extent in the environment due to their water insolubility and chemical inertness. Recently, an oxygenase-independent sterol degradation pathway was discovered in a cholesterol-grown denitrifying bacterium Sterolibacterium (S.) denitrificans. It achieves hydroxylation of the unactivated primary C26 of the isoprenoid side chain to an allylic alcohol via a phosphorylated intermediate in a four-step ATP-dependent enzyme cascade. However, this pathway is incompatible with the degradation of widely distributed steroids containing a double bond at C22 in the isoprenoid side chain such as the plant sterol stigmasterol. Here, we have enriched a prototypical delta-24 desaturase from S. denitrificans, which catalyzes the electron ac","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-01T09:24:47.308Z","creation":"2026-04-08T11:14:04.232Z"},"accession":"S-EPMC11061730","cross_references":{"pubmed":["38556086"],"doi":["10.1016/j.jbc.2024.107243"]}}