1-Ene-steroid reductase of Mycobacterium SP. NRRL B-3805

T. Goren, M. Harni, S. Rimonk, Y. Aharonowitz*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


The microbial enzymatic reduction of 1,4-androstadiene-3,17-dione (ADD) to 4-androstene-3, 17-dione (AD), testosterone and 1-dehydrotestosterone (DHT) is described. Two reducing activities observed in washed cell suspensions and cell free extracts of Mycobacterium sp. NRRL B-3805 were found to account for these bioconversions. One was a 1-ene-steroid reductase and the other a 17-keto steroid reductase. The first reducing activity was found to appear in the soluble cell fraction whereas the latter could be precipitated by centrifugation. Maximum 1-ene-steroid reductase specific activity was achieved during the exponential growth phase of the organism and significantly increased upon induction with ADD. The 1-ene-steroid reductase was partially purified (30-fold) by ammonium sulfate fractionation, gel-filtration and ion-exchange chromatography, and was eluted from a Sephacryl S-300 column with an Mr = 115,000. The 1-ene-steroid reductase activity was NADPH-dependent and had specificity towards steroid compounds containing C-1,2 double bond with an apparent Km for ADD of 2.2 × 10-5 M. The reverse reaction catalyzing C-1,2 dehydrogenation could not be detected in our preparations. The results suggest that in Mycobacterium sp NRRL B-3805 and B-3683 the steroid C-1,2 dehydrogenation and 1-ene reduction are two separable activities.

Original languageEnglish
Pages (from-to)1789-1797
Number of pages9
JournalJournal of Steroid Biochemistry
Issue number6
StatePublished - Dec 1983


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