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The ability of the pathogenMycobacterium tuberculosis to metabolize steroids like cholesterol and the roles that these compounds play in the virulence and pathogenesis of this organism are increasingly evident. Here, we demonstrate through experiments and bioinformatic analysis the existence of an architecturally distinct subfamily of acyl coenzyme A (acyl-CoA) dehydrogenase (ACAD) enzymes that are α2 β2 heterotetramers with two active sites. These enzymes are encoded by two adjacent ACAD (fadE ) genes that are regulated by cholesterol. FadE26-FadE27 catalyzes the dehydrogenation of 3β-hydroxy-chol-5-en-24-oyl-CoA, an analog of the 5-carbon side chain cholesterol degradation intermediate. Genes encoding the α2 β2 heterotetrameric ACAD structures are present in multiple regions of theM. tuberculosis genome, and subsets of these genes are regulated by four different transcriptional repressors or activators: KstR1 (also known as KstR), KstR2, Mce3R, and SigE. Homologous ACAD gene pairs are found in otherActinobacteria , as well asProteobacteria . Their structures and genomic locations suggest that the α2 β2 heterotetrameric structural motif has evolved to enable catalysis of dehydrogenation of steroid- or polycyclic-CoA substrates and that they function in four subpathways of cholesterol metabolism.

journal of bacteriology

Shrinking the FadE Proteome of Mycobacterium tuberculosis: Insights into Cholesterol Metabolism through Identification of an α <sub>2</sub> β <sub>2</sub> Heterotetrameric Acyl Coenzyme A Dehydrogenase Family

Shrinking the FadE Proteome of Mycobacterium tuberculosis: Insights into Cholesterol Metabolism through Identification of an α 2 β 2 Heterotetrameric Acyl Coenzyme A Dehydrogenase Family

Shrinking the FadE Proteome of Mycobacterium tuberculosis: Insights into Cholesterol Metabolism through Identification of an α ₂ β ₂ Heterotetrameric Acyl Coenzyme A Dehydrogenase Family