Cloning and sequence analysis of adrenodoxin reductase cDNA from bovine adrenal cortex.
cDNA clones for bovine adrenodoxin reductase were isolated, and the primary structure of the enzyme precursor was deduced from their nucleotide sequences. The precursor consists of 492 amino acids including an extrapeptide of 32 amino acids at the amino terminus. The extrapeptide is hydrophilic [corrected] and rich in arginine. The amino terminal sequence of the precursor is homologous with that of the adrenodoxin precursor. A possible FAD- or NADPH-binding site is present near the amino terminus of the mature enzyme.
Sagara
Y
Y
Laboratory of Microbiology, Faculty of Pharmaceutical Sciences, Kyushu University, Fukuoka.
Takata
Y
Y
Miyata
T
T
Hara
T
T
Horiuchi
T
T
D000302:Adrenal Cortex / Q000201:enzymology*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002417:Cattle; D004247:DNA / Q000235:genetics*; D004274:DNA, Recombinant; D004792:Enzyme Precursors / Q000235:genetics*; D005287:Ferredoxin-NADP Reductase / Q000235:genetics* / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D008969:Molecular Sequence Data; D009247:NADH, NADPH Oxidoreductases / Q000235:genetics*; D009249:NADP / Q000378:metabolism; D010446:Peptide Fragments / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics
D004274:DNA, Recombinant; D004792:Enzyme Precursors; D010446:Peptide Fragments; D012333:RNA, Messenger; D005182:Flavin-Adenine Dinucleotide; D009249:NADP; D004247:DNA; D005287:Ferredoxin-NADP Reductase; D009247:NADH, NADPH Oxidoreductases