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The gene encoding the putative reductase component (KshB) of 3-ketosteroid 9α-hydroxylase was cloned from  Rhodococcus equi  USA-18, a cholesterol oxidase-producing strain formerly named  Arthrobacter simplex  USA-18, by PCR according to consensus amino acid motifs of several bacterial KshB subunits. Deletion of the gene in  R. equi  USA-18 by a PCR-targeted gene disruption method resulted in a mutant strain that could accumulate up to 0.58 mg/ml 1,4-androstadiene-3,17-dione (ADD) in the culture medium when 0.2% cholesterol was used as the carbon source, indicating the involvement of the deleted enzyme in 9α-hydroxylation of steroids. In addition, this mutant also accumulated 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid (Δ 1,4 -BNC). Because both ADD and Δ 1,4 -BNC are important intermediates for the synthesis of steroid drugs, this mutant derived from  R. equi  USA-18 may deserve further investigation for its application potential.

microbial cell factories

Deletion of the gene encoding the reductase component of 3-ketosteroid 9α-hydroxylase in Rhodococcus equi USA-18 disrupts sterol catabolism, leading to the accumulation of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid and 1,4-androstadiene-3,17-dione