Abstract
Various 17β-hydroxysteroid oxido-reductases (from Pseudomonas testosteroni, and from guinea pig liver supernatant and microsomes) catalyse the “direct” oxidation of androsta-5-ene-3β,17β-diol 3-sulfate and 3β-glucuroniside. Kinetic studies indicate that the affinity, estimated from Km or Ki values, of enzymes for steroid conjugates is inferior to that for the corresponding free steroids, whereas oxidation rates are greater in some cases. Inhibition of testosterone oxidation by androsta-4-ene-3,17-dione and 17-oxosteroid conjugates (one of which is dehydroisoandrosterone sulfate) suggests that “adrenal androgens” may play a regulatory role on the male hormone inactivating oxidation.
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