TitleDatePubMed ID
Functional characterization of 3-ketosteroid 9α-hydroxylases in Rhodococcus ruber strain chol-4.2017 Sep28642093
Efficient 9α-hydroxy-4-androstene-3,17-dione production by engineered Bacillus subtilis co-expressing Mycobacterium neoaurum 3-ketosteroid 9α-hydroxylase and B. subtilis glucose 1-dehydrogenase with NADH regeneration.201627516945
Substrate specificities and conformational flexibility of 3-ketosteroid 9α-hydroxylases.2014 Sep 1225049233
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.2014 Sep 925201011
Characterization and engineering of 3-ketosteroid-△1-dehydrogenase and 3-ketosteroid-9α-hydroxylase in Mycobacterium neoaurum ATCC 25795 to produce 9α-hydroxy-4-androstene-3,17-dione through the catabolism of sterols.2014 Jul24831710
3-Ketosteroid 9α-hydroxylase enzymes: Rieske non-heme monooxygenases essential for bacterial steroid degradation.2014 Jul24846050
Structural features in the KshA terminal oxygenase protein that determine substrate preference of 3-ketosteroid 9α-hydroxylase enzymes.2012 Jan22020644
Activity of 3-ketosteroid 9α-hydroxylase (KshAB) indicates cholesterol side chain and ring degradation occur simultaneously in Mycobacterium tuberculosis.2011 Nov 2521987574
Multiplicity of 3-Ketosteroid-9α-Hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids.2011 Aug21642460
A new steroid-transforming strain of Mycobacterium neoaurum and cloning of 3-ketosteroid 9alpha-hydroxylase in NwIB-01.2010 Nov20204712