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• W2187090702 abstract "The mechanism for the catalytic reduction of the double bond at C-7,8 in 7-dehydrocholesterol by 3 b -hydrox- ysterol D 7 -reductase was investigated by testing structurally related sterols as substrates and potential inhibitors. The hepatic smooth endoplasmic reticulum was identified as the site of enzyme activity. All putative substrates contained 27 carbons, but differed from 7-dehydrocholesterol by the ad- dition of either an ethyl substituent at C-24 (7-dehydrosito- sterol), a double bond at C-22 with a methyl substituent at C-24 (ergosterol), epimerization of the hydroxyl from the 3 b - to 3 a -configuration (7-dehydroepicholesterol), or a sat- urated double bond at C-5,6 (lathosterol). Two non-steroi- dal compounds that inhibit 3 b -hydroxysterol D 7 -reductase in vivo (AY 9944 and BM 15.766) were also tested. Ergos- terol, 7-dehydrositosterol, and 7-dehydroepicholesterol were reduced at C-7,8 to form brassicasterol, sitosterol, and epi- cholesterol, respectively, but 75% less efficiently than 7-de- hydrocholesterol. Increasing concentrations of these sterols competitively inhibited 3 b -hydroxysterol D 7 -reductase activ- ity. The double bond at C-7,8 in lathosterol was not re-" @default.
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• W2187090702 date "1998-01-01" @default.
• W2187090702 modified "2023-09-27" @default.
• W2187090702 title "substrate specificity, competitive and non-competitive inhibition, and phosphorylation/dephosphorylation" @default.
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