Molecular cloning of cDNA for vitamin D3 25-hydroxylase from rat liver mitochondria.
A cDNA clone encoding mitochondrial vitamin D3 25-hydroxylase was isolated from a rat liver cDNA library by the use of specific antibodies to the enzyme. The isolated cDNA clone was 1.9 kbp long and contained a 1599 bp open reading frame encoding 533 amino acid residues. The deduced primary structure contained a presequence typical for mitochondrial enzymes in the N-terminal region. The N-terminal sequence of the mature enzyme was determined to be Ala-Ile-Pro-Ala-Ala, which agrees perfectly with a portion of the deduced sequence, establishing the cleavage point of the precursor.
Usui
E
E
Department of Biochemistry, Hiroshima University School of Dentistry, Japan.
Noshiro
M
M
Okuda
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D053493:Cholestanetriol 26-Monooxygenase; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis*; D005260:Female; D051379:Mice; D008807:Mice, Inbred BALB C; D008930:Mitochondria, Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D051381:Rats; D013250:Steroid Hydroxylases / Q000235:genetics*
D004247:DNA; D013250:Steroid Hydroxylases; D053493:Cholestanetriol 26-Monooxygenase; C506832:Cyp27a1 protein, mouse