Activity of 3-Ketosteroid 9α-Hydroxylase (KshAB) Indicates Cholesterol Side Chain and Ring Degradation Occur Simultaneously inMycobacterium tuberculosis

FadD19 of Rhodococcus rhodochrous DSM43269, a Steroid-Coenzyme A Ligase Essential for Degradation of C-24 Branched Sterol Side Chains

(2011) M. H. Wilbrink et al.   APPLIED AND ENVIRONMENTAL MICROBIOLOGY

Multiplicity of 3-Ketosteroid-9 -Hydroxylase Enzymes in Rhodococcus rhodochrous DSM43269 for Specific Degradation of Different Classes of Steroids

(2011) M. Petrusma et al.   JOURNAL OF BACTERIOLOGY

Metabolic Regulation of Mycobacterial Growth and Antibiotic Sensitivity

(2011) Seung-Hun Baek et al.   PLOS BIOLOGY

Mycobacterium tuberculosis Wears What It Eats

(2010) David G. Russell et al.   Cell Host & Microbe

A Flavin-dependent Monooxygenase fromMycobacterium tuberculosisInvolved in Cholesterol Catabolism

(2010) Carola Dresen et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Mycobacterium tuberculosis CYP125A1, a steroid C27 monooxygenase that detoxifies intracellularly generated cholest-4-en-3-one

(2010) Hugues Ouellet et al.   MOLECULAR MICROBIOLOGY

Functional Genetic Diversity among Mycobacterium tuberculosis Complex Clinical Isolates: Delineation of Conserved Core and Lineage-Specific Transcriptomes during Intracellular Survival

(2010) Susanne Homolka et al.   PLoS Pathogens

Rhodococcus rhodochrous DSM 43269 3-Ketosteroid 9 -Hydroxylase, a Two-Component Iron-Sulfur-Containing Monooxygenase with Subtle Steroid Substrate Specificity

(2009) M. Petrusma et al.   APPLIED AND ENVIRONMENTAL MICROBIOLOGY

A Thiolase of Mycobacterium tuberculosis Is Required for Virulence and Production of Androstenedione and Androstadienedione from Cholesterol

(2009) N. M. Nesbitt et al.   INFECTION AND IMMUNITY

Mycobacterium tuberculosis Is Able To Accumulate and Utilize Cholesterol

(2009) A. Brzostek et al.   JOURNAL OF BACTERIOLOGY

Mycobacterial Cytochrome P450 125 (Cyp125) Catalyzes the Terminal Hydroxylation of C27 Steroids

(2009) Jenna K. Capyk et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Characterization of 3-Ketosteroid 9α-Hydroxylase, a Rieske Oxygenase in the Cholesterol Degradation Pathway ofMycobacterium tuberculosis

(2009) Jenna K. Capyk et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Characterization of a Carbon-Carbon Hydrolase from Mycobacterium tuberculosis Involved in Cholesterol Metabolism

(2009) Nathan A. Lack et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Cytochrome P450 125 (CYP125) catalyses C26-hydroxylation to initiate sterol side-chain degradation inRhodococcus jostiiRHA1

(2009) Kamila Z. Rosłoniec et al.   MOLECULAR MICROBIOLOGY

3-Ketosteroid 9α-hydroxylase is an essential factor in the pathogenesis ofMycobacterium tuberculosis

(2009) Yanmin Hu et al.   MOLECULAR MICROBIOLOGY

Studies of a Ring-Cleaving Dioxygenase Illuminate the Role of Cholesterol Metabolism in the Pathogenesis of Mycobacterium tuberculosis

(2009) Katherine C. Yam et al.   PLoS Pathogens

Characterization of a Second Rhodococcus erythropolis SQ1 3-Ketosteroid 9 -Hydroxylase Activity Comprising a Terminal Oxygenase Homologue, KshA2, Active with Oxygenase-Reductase Component KshB

(2008) R. van der Geize et al.   APPLIED AND ENVIRONMENTAL MICROBIOLOGY

3-Keto-5α-steroid Δ1-dehydrogenase fromRhodococcus erythropolisSQ1 and its orthologue inMycobacterium tuberculosisH37Rv are highly specific enzymes that function in cholesterol catabolism

(2008) Jan Knol et al.   BIOCHEMICAL JOURNAL

Tuberculous Granulomas Are Hypoxic in Guinea Pigs, Rabbits, and Nonhuman Primates

(2008) L. E. Via et al.   INFECTION AND IMMUNITY

Mycobacterial persistence requires the utilization of host cholesterol

(2008) A. K. Pandey et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA