ArticleThe Journal of biological chemistry2026
Temperature-dependent conformational dynamics govern regioselectivity in a CYP152 decarboxylase.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Peroxygenases from the CYP152 family catalyze oxidative transformations of fatty acids using hydrogen peroxide and bypass the canonical redox partners. A subset of these enzymes performs fatty acid decarboxylation to generate terminal alkenes, which serve as key intermediates for renewable fuels and petrochemicals. A central unanswered question is how CYP152 enzymes orchestrate the branching between decarboxylation and hydroxylation, a balance that ultimately defines their utility as selective biocatalysts. Here, we uncover a temperature-dependent switch in the peroxygenase from Nosocomiicoccus massiliensis (OleT
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