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Reversibility of Steroid -Isomerase

III. THE SOLUBLE ENZYME OF PSEUDOMONAS TESTOSTERONI

From the ¹ From the John Collins Warren Laboratories of the Huntington Memorial Hospital of Harvard University, at the Massachusetts General Hospital, and the Department of Biological Chemistry, Harvard Medical School, Boston Massachusetts 02114

The purified ß-hydroxysteroid dehydrogenase and steroid -isomerase of Pseudomonas testosteroni have been incubated, both separately and together, with testosterone-4-¹⁴C and reduced diphosphopyridine nucleotide. Substantial yields of androst-4-ene-3ß,17ß-diol were obtained whenever the dehydrogenase was present, while androst-5-ene-3ß, 17ß-diol was formed only when both the dehydrogenase and the isomerase were incubated. No radioactive products were detected when only the isomerase was incubated or in the absence of either enzyme.

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