Regulation of rat hepatic 3beta-hydroxysterol delta7-reductase: substrate specificity, competitive and non-competitive inhibition, and phosphorylation/dephosphorylation.

@article{Shefer1998RegulationOR,
  title={Regulation of rat hepatic 3beta-hydroxysterol delta7-reductase: substrate specificity, competitive and non-competitive inhibition, and phosphorylation/dephosphorylation.},
  author={Sarah Shefer and Gerald Salen and Akira Honda and Ashok Kumir Batta and L. B. Nguyen and G. Stephen Tint and Yiannis A. Ioannou and Robert J Desnick},
  journal={Journal of lipid research},
  year={1998},
  volume={39 12},
  pages={2471-6}
}
The mechanism for the catalytic reduction of the double bond at C-7, 8 in 7-dehydrocholesterol by 3beta-hydroxysterol Delta7-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 addition of either an ethyl substituent at C-24 (7-dehydrositosterol), a double bond at… CONTINUE READING

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Ergosterol , 7-dehydrositosterol , and 7-dehydroepicholesterol were reduced at C-7 , 8 to form brassicasterol , sitosterol , and epicholesterol , respectively , but 75% less efficiently than 7-dehydrocholesterol .
Ergosterol , 7-dehydrositosterol , and 7-dehydroepicholesterol were reduced at C-7 , 8 to form brassicasterol , sitosterol , and epicholesterol , respectively , but 75% less efficiently than 7-dehydrocholesterol .
Ergosterol , 7-dehydrositosterol , and 7-dehydroepicholesterol were reduced at C-7 , 8 to form brassicasterol , sitosterol , and epicholesterol , respectively , but 75% less efficiently than 7-dehydrocholesterol .
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