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

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

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

7-Ketocholesterol Catabolism by Rhodococcus jostii RHA1

(2009) J. M. Mathieu et al.   APPLIED AND ENVIRONMENTAL MICROBIOLOGY

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

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

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

MEGA: A biologist-centric software for evolutionary analysis of DNA and protein sequences

(2008) S. Kumar et al.   BRIEFINGS IN BIOINFORMATICS