Abstract
Corynebacterium spec, mutant Chol 73 T 191 degrades cholesterol nearly quantitatively into 20-carboxy-pregna-1,4-diene-3-one (BNC) in the absence of inhibitors (1). From the presence of small amounts of 20-carboxy-pregn-4-ene-3-one (Δ4-BNC), androsta-1,4-diene-3,17-dione (AD) and androst-4-ene-3, 17-dione (ADD), the presence of a steroid Δ1-dehydrogenase (E.C. 1.3.99.4) can be inferred. This enzyme has recently been isolated and purified 160 fold from Nocardia opaca (2). In Mycobacterium in direct evidence for the presence of an isoenzyme system has been presented (3). We now report direct proof for steroid Δ1-dehydrogenase isoenzymes inCorynebacterium spec. Chol 73 T 191, based on the RB position of the specifically stained steroid Δ1-dehydrogenase band after PAA-electrophoresis with bromophenol blue having an RB value of 1.00. With AD and cholesterol as inducers, the RB values were 0.09 and 0.71, respectively.
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References
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© 1982 Plenum Press, New York
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Mueller, WR., Preuss, W., Schmid, R.D. (1982). SteroidΔ1-Dehydrogenase Isoenzymes in Corynebacterium Species Chol 73 T 191. In: Chibata, I., Fukui, S., Wingard, L.B. (eds) Enzyme Engineering. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9290-7_16
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DOI: https://doi.org/10.1007/978-1-4615-9290-7_16
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