publication . Article . 2011

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

Petrusma, Mirjan; Hessels, Gerda; Dijkhuizen, Lubbert; van der Geize, Robert;
Open Access English
  • Published: 01 Aug 2011
Abstract
The well-known large catabolic potential of rhodococci is greatly facilitated by an impressive gene multiplicity. This study reports on the multiplicity of kshA, encoding the oxygenase component of 3-ketosteroid 9 alpha-hydroxylase, a key enzyme in steroid catabolism. Five kshA homologues (kshA1 to kshA5) were previously identified in Rhodococcus rhodochrous DSM43269. These KshA(DSM43269) homologues are distributed over several phylogenetic groups. The involvement of these KshA homologues in the catabolism of different classes of steroids, i.e., sterols, pregnanes, androstenes, and bile acids, was investigated. Enzyme activity assays showed that all KSH enzymes ...
Subjects
free text keywords: SP STRAIN RHA1, 3-KETOSTEROID 9-ALPHA-HYDROXYLASE, MYCOBACTERIUM-TUBERCULOSIS, ERYTHROPOLIS SQ1, CHOLESTEROL CATABOLISM, BIPHENYL, PATHWAY, GENES, MONOOXYGENASE, MACROPHAGES
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