Steroid specificity of human placental 5-ene-3 beta-hydroxysteroid oxidoreductase.

Abstract:

:The properties of 5-ene-3 beta hydroxysteroid oxidoreductase (3 beta-HSD) from human placental homogenates were studied in vitro. The apparent Michaelis constants for 3 beta-HSD with the substrates pregnenolone (delta 5P) and dehydroepiandrosterone (DHA) were 170 nM and nM respectively. The optimal pH for both these substrates was between 10 and 12. With NAD as the substrate, the Km for the pregnenolone was 20 microM and for DHA, 17 microM. The activity of 3 beta-HSD was inhibited by various steroids. Competitive inhibitors (pregnenolone substrate) included: ethynylestradiol (inhibition constant Ki=7.3 nM), DHA (Ki=46 nM), estradiol-17 beta (Ki=46 nM), cholesterol (Ki=0.68 microM) and 16 alpha-hydroxydehydroepiandrosterone (16 alphaOHDHA) (Ki=2.2 microM). When the substrate was DHA, competitive inhibition occurred with the following steroids: ethynylestradiol (Ki=6.4 nM), estradiol-17 beta (Ki=69 nM), pregnenolone (Ki=91 nM), cholesterol (Ki=1.3 microM) and 16 alphaOHDHA (Ki=1.9 microM). 4-Ene-3-ketosteroids such as androstenedione, progesterone (delta 4P), norethindrone and chlormadinone acetate acted as noncompetitive inhibitors towards both substrates.

journal_name

Steroids

journal_title

Steroids

authors

Yoshida N

doi

10.1016/s0039-128x(79)80002-1

subject

Has Abstract

pub_date

1979-01-01 00:00:00

pages

9-21

issue

1

eissn

0039-128X

issn

1878-5867

pii

S0039-128X(79)80002-1

journal_volume

33

pub_type

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