<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Zhan T</submitter><funding>Deutsche Forschungsgemeinschaft</funding><pagination>107243</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11061730</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>300(5)</volume><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</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Bacterial stigmasterol degradation involving radical flavin delta-24 desaturase and molybdenum-dependent C26 hydroxylase.</pubmed_title><pmcid>PMC11061730</pmcid><funding_grant_id>235777276</funding_grant_id><funding_grant_id>SFB 1381</funding_grant_id><pubmed_authors>Jacoby C</pubmed_authors><pubmed_authors>Gunter A</pubmed_authors><pubmed_authors>Muller M</pubmed_authors><pubmed_authors>Knapp B</pubmed_authors><pubmed_authors>Zhan T</pubmed_authors><pubmed_authors>Boll M</pubmed_authors><pubmed_authors>Ferlaino S</pubmed_authors><pubmed_authors>Weber S</pubmed_authors><pubmed_authors>Drepper F</pubmed_authors><pubmed_authors>Jede M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Bacterial stigmasterol degradation involving radical flavin delta-24 desaturase and molybdenum-dependent C26 hydroxylase.</name><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</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 May</publication><modification>2026-06-01T09:24:47.308Z</modification><creation>2026-04-08T11:14:04.232Z</creation></dates><accession>S-EPMC11061730</accession><cross_references><pubmed>38556086</pubmed><doi>10.1016/j.jbc.2024.107243</doi></cross_references></HashMap>