Vitamin D hydroxylases

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<jats:title>Abstract</jats:title><jats:p>There are three mixed function oxidases which catalyze hydroxylations of vitamin D and its derivatives. These include the hepatic mitochondrial or microsomal vitamin D<jats:sub>3</jats:sub>‐25‐hydroxylase and the two renal mitochondrial enzymes which further hydroxylate 25‐hydroxyvitamin‐D<jats:sub>3</jats:sub> (25‐OH‐D<jats:sub>3</jats:sub>) to form 24R,25‐dihydroxyvitamin D<jats:sub>3</jats:sub> (24,25(OH)<jats:sub>2</jats:sub>D<jats:sub>3</jats:sub>) and 1,25‐dihydroxyvitamin D<jats:sub>3</jats:sub> [1,25(OH)<jats:sub>2</jats:sub>D<jats:sub>3</jats:sub>], the primary steroid hormonal derivative of vitamin D<jats:sub>3</jats:sub>. All three enzymes are cytochrome P450 dependent. The two renal mitochondrial enzymes are regulated, usually in a reciprocal fashion. The intracellular signalling systems involved in this regulation include 1,25(OH)<jats:sub>2</jats:sub>D<jats:sub>3</jats:sub> itself and both protein kinases A and C. Recent progress has been made in the purification and cloning of the vitamin D<jats:sub>3</jats:sub>‐25‐hydroxylase and the 25‐OH‐D<jats:sub>3</jats:sub>‐24‐hydroxylase. When the 25‐OH‐D<jats:sub>3</jats:sub>‐1‐hydroxylase is purified and cloned, efforts which have thus far been frustrated by its low abundance, fertile new ground for the study of the regulation of vitamin D metabolism at the molecular level will be opened up.</jats:p>

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