ArticleBiochemistry2013
Mycobacterium tuberculosis utilizes a unique heterotetrameric structure for dehydrogenation of the cholesterol side chain.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 67 citations in OpenAlex.
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- Identification of dehydrogenase, hydratase, and aldolase responsible for the propionyl residue removal in degradation of cholic acid C-17 side chain inMicrobiology spectrum · 2025Article
- Efficient Synthesis of Steroidal Intermediates with a C17 Side Chain from Phytosterols by Genetically Modified Mycolicibacterium neoaurum NRRL B-3805 Strain.ChemistryOpen · 2025Article
- Structural basis for expanded substrate specificities of human long chain acyl-CoA dehydrogenase and related acyl-CoA dehydrogenases.Scientific reports · 2024Article
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- Structural Basis for Expanded Substrate SpeciResearch square · 2024Article
- Functional analysis of acyl-CoA dehydrogenases and their application to C22 steroid production.Applied microbiology and biotechnology · 2023Article
- Targeted Mutagenesis of Mycobacterium Strains by Homologous Recombination.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Bioconversion of Phytosterols to 9-Hydroxy-3-Oxo-4,17-Pregadiene-20-Carboxylic Acid Methyl Ester by Enoyl-CoA Deficiency and Modifying Multiple Genes in Mycolicibacterium neoaurum.Applied and environmental microbiology · 2022Article
- The unusual convergence of steroid catabolic pathways inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Multiple acyl-CoA dehydrogenase deficiency kills Mycobacterium tuberculosis in vitro and during infection.Nature communications · 2021Article
- Rv0180c contributes to Mycobacterium tuberculosis cell shape and to infectivity in mice and macrophages.PLoS pathogens · 2021Article
- Comparative Analysis of Bile-Salt Degradation inApplied and environmental microbiology · 2021Article
- Proteome, Bioinformatic, and Functional Analyses Reveal a Distinct and Conserved Metabolic Pathway for Bile Salt Degradation in theApplied and environmental microbiology · 2021Article
- Degradation of Bile Acids by Soil and Water Bacteria.Microorganisms · 2021Review
- Enzymatic β-Oxidation of the Cholesterol Side Chain inACS infectious diseases · 2021Article
- Different genome-wide transcriptome responses of Nocardioides simplex VKM Ac-2033D to phytosterol and cortisone 21-acetate.BMC biotechnology · 2021Article
- Structural basis for the broad substrate specificity of two acyl-CoA dehydrogenases FadE5 from mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- IpdE1-IpdE2 Is a Heterotetrameric Acyl Coenzyme A Dehydrogenase That Is Widely Distributed in Steroid-Degrading Bacteria.Biochemistry · 2020Article
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2 authors at 1 institution in 1 country.
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Abstract
Compounding evidence supports the important role in pathogenesis that the metabolism of cholesterol by Mycobacterium tuberculosis plays. Elucidating the pathway by which cholesterol is catabolized is necessary to understand the molecular mechanism by which this pathway contributes to infection. On the basis of early metabolite identification studies in multiple actinomycetes, it has been proposed that cholesterol side chain metabolism requires one or more acyl-CoA dehydrogenases (ACADs). There are 35 genes annotated as encoding ACADs in the M. tuberculosis genome. Here we characterize a heteromeric ACAD encoded by Rv3544c and Rv3543c, formerly named fadE28 and fadE29, respectively. We now refer to genes Rv3544c and Rv3543c as chsE1 and chsE2, respectively, in recognition of their validated activity in cholesterol side chain dehydrogenation. Analytical ultracentrifugation and liquid chromatography-ultraviolet experiments establish that ChsE1-ChsE2 forms an α(2)β(2) heterotetramer, a new architecture for an ACAD. Our bioinformatic analysis and mutagenesis studies reveal that heterotetrameric ChsE1-ChsE2 has only two active sites. E241 in ChsE2 is required for catalysis of dehydrogenation by ChsE1-ChsE2. Steady state kinetic analysis establishes the enzyme is specific for an intact steroid ring system versus hexahydroindanone substrates with specificity constants (k(cat)/K(M)) of (2.5 ± 0.5) × 10(5) s(-1) M(-1) versus 9.8 × 10(2) s(-1) M(-1), respectively, at pH 8.5. The characterization of a unique ACAD quaternary structure involved in sterol metabolism that is encoded by two distinct cistronic ACAD genes opens the way to identification of additional sterol-metabolizing ACADs in M. tuberculosis and other actinomycetes through bioinformatic analysis.
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