Enhancing Expression of 3-Ketosteroid-9α-Hydroxylase Oxygenase, an Enzyme with Broad Substrate Range and High Hydroxylation Ability, in Mycobacterium sp. LY-1

The effect of 3-ketosteroid-Δ1-dehydrogenase isoenzymes on the transformation of AD to 9α-OH-AD by Rhodococcus rhodochrous DSM43269

(2016) Yang Liu et al.   JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY

Blocking follistatin-like 1 attenuates bleomycin-induced pulmonary fibrosis in mice

(2015) Yingying Dong et al.   JOURNAL OF EXPERIMENTAL MEDICINE

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) Kang Yao et al.   METABOLIC ENGINEERING

Bioconversion of 4-androstene-3,17-dione to androst-1,4-diene-3,17-dione by recombinant Bacillus subtilis expressing ksdd gene encoding 3-ketosteroid-Δ1-dehydrogenase from Mycobacterium neoaurum JC-12

(2013) Wenqing Zhang et al.   JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY

Microbial steroid transformations: current state and prospects

(2012) Marina V. Donova et al.   APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

Gene Cluster Encoding Cholate Catabolism in Rhodococcus spp.

(2012) W. W. Mohn et al.   JOURNAL OF BACTERIOLOGY

Identification and engineering of cholesterol oxidases involved in the initial step of sterols catabolism in Mycobacterium neoaurum

(2012) Kang Yao et al.   METABOLIC ENGINEERING

Cholesterol metabolism in Mycobacterium smegmatis

(2012) Iria Uhía et al.   Environmental Microbiology Reports

Catabolism and biotechnological applications of cholesterol degrading bacteria

(2012) J. L. García et al.   Microbial Biotechnology

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

Structural Features in the KshA Terminal Oxygenase Protein That Determine Substrate Preference of 3-Ketosteroid 9 -Hydroxylase Enzymes

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

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

(2011) Jenna K. Capyk et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A comparative view of metabolite and substrate stress and tolerance in microbial bioprocessing: From biofuels and chemicals, to biocatalysis and bioremediation

(2010) Sergios A. Nicolaou et al.   METABOLIC ENGINEERING

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

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

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

(2009) Yanmin Hu et al.   MOLECULAR MICROBIOLOGY

Androstenedione production by biotransformation of phytosterols

(2008) Alok Malaviya et al.   BIORESOURCE TECHNOLOGY

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

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