Steroidumwandelnde Enzyme aus Mikroorganismen XI. Reversibilität der Dehydrierungsreaktion der Steroid‐1‐Dehydrogenase aus Nocardia opaca

Abstract

Highly purified preparations of the 4‐en‐3‐oxosteroid: (acceptor)‐1‐en‐oxidoreductase from Nocardia opaca have been investigated in both types of reactions: 1.2‐dehydrogenation of the 4‐en‐3‐oxo‐derivative and 1.2‐hydrogenation of the 1.4‐dien‐3‐oxo‐derivative. It was not possible to separate the hydrogenating activity from the dehydrogenating activity by affinity chromatography, disc electrophoresis, SDS‐electrophoresis, and isoelectric focusing techniques. The pure enzyme preparation is discussed as only one FAD depending protein acting in response to the system as a dehydrogenase as well as a reductase.

Biotransformations of Steroids

“…erythropolis IMET 7 185, and M. smegmatis IMET SG 99, dehydrogenation and hydrogenation were shown to be performed by only a single enzyme. [119][120][121] Although significant amounts of the unwanted products were described to be formed during fermentation in unfavorable media and in conditions of inadequate aeration,",' I 2 . ' l 4 side-product formation in commercial 1-dehydrogenation is not as important a problem as in 11 Por 16a-hydroxylations, and in properly controlled fermentations, a product of 90% yield is not uncommon.…”