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Testicular and adrenal 3β-hydroxy-5-ene-steroid dehydrogenase and 5-ene-4-ene isomerase

Authors
Journal
Journal of Steroid Biochemistry
0022-4731
Publisher
Elsevier
Publication Date
Volume
27
Identifiers
DOI: 10.1016/0022-4731(87)90149-x
Disciplines
  • Biology
  • Medicine

Abstract

Abstract The purified multifunctional enzyme, 3β-hydroxysteroid dehydrogenase with steroid 5-ene-4-ene isomerase from rat testes and adrenals showed similar catalytic properties. They exhibited the same molecular weight of 46,500. Either NAD + or NADH was required for steroid isomerizing activity, probably as an allosteric effector. It was clearly demonstrated by using the purified enzyme that without NAD(H) no isomerizing activity was detected. In the presence of NADH, or its analogue, 3β-hydroxysteroid dehydrogenase obtained from both tissues was inhibited; however, steroid isomerizing activity remained due to the allosteric effect. The results suggest that in these endocrine organs, both enzyme activities reside within the same protein.

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