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Carbonyl reductase family member 4 (CBR4) is a mitochondrial enzyme of the short-chain dehydrogenase/reductase superfamily. CBR4 forms a tetrameric structure, where it acts as a NADPH-dependent quinone reductase, preferring ortho- and para-quinones as substrates rather than other aldehydes or ketones. This reduction can generate reactive oxygen species through redox cycling, contributing to apoptosis under cytotoxic stress. Functionally, CBR4 also serves as the beta subunit in the mitochondrial 3-ketoacyl-[acyl-carrier-protein] reductase complex, where, alongside the alpha subunit HSD17B8, it is essential for mitochondrial fatty acid synthesis. CBR4 plays key roles in redox homeostasis, cellular defense against toxicants, and metabolic processes, with potential implications in cancer biology and other disease contexts.
NADPH-dependent reduction of ortho- and para-quinones Contribution to superoxide generation via redox cycling Reductive conversion of 3-oxoacyl-ACP intermediates in mitochondrial fatty acid synthesis
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