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Unique property of liver mitochondrial P450 to catalyze the two physiologically important reactions involved in both cholesterol catabolism and vitamin D activation
Author(s) -
Emiko Usui,
Mitsuhide Noshiro,
Yoshihiko Ohyama,
Kyuichiro Okuda
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81357-t
Subject(s) - adrenodoxin , hydroxylation , enzyme , biochemistry , chemistry , mitochondrion , catabolism , reductase , vitamin d and neurology , biology , cytochrome p450 , endocrinology
The cDNA for vitamin D 25‐hydroxylase in rat liver mitochondria was transfected in COS cells in order to confirm our previous postulation that both 5β‐cholestane‐3α,7α,12α‐triol 27‐hydroxylation and vitamin D 25‐hydroxylation are catalyzed by a common enzyme. As a result it was found that both enzyme activities could be reconstituted from the solubilized extract of mitochondria of these cells. NADPH. NADPH‐adrenodoxin reductase and adrenodoxin, giving unequivocal evidence that the two enzyme activities are catalyzed by a common enzyme.