Abstract
3-Ketosteroid-1,2-dehydrogenase (KstD) is a promising enzyme for the synthesis of C1,2-dehydrogenized steroids. KstD specifically catalyzes the dehydrogenization of steroid in which an intermediate containing hydroxyl groups is formed before dehydrated to generate a double bond. However, KstDs from bacterial sources exhibit distinct specificity for a variety of steroids and their structural mechanisms have been fully understood. Recently we identified a novel KstD from Mycobacterium neoaurum HGMS2 (i.e., KstD211) that was involved in phytosterol degradation.
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