Sagara Y, Takata Y, Miyata T, Hara T, Horiuchi T
Laboratory of Microbiology, Faculty of Pharmaceutical Sciences, Kyushu University, Fukuoka.
J Biochem. 1987 Dec;102(6):1333-6. doi: 10.1093/oxfordjournals.jbchem.a122178.
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.
分离出了牛肾上腺皮质铁氧化还原蛋白还原酶的cDNA克隆，并根据其核苷酸序列推导了该酶前体的一级结构。前体由492个氨基酸组成，包括氨基末端32个氨基酸的额外肽段。该额外肽段具有亲水性且富含精氨酸。前体的氨基末端序列与肾上腺皮质铁氧化还原蛋白前体的序列同源。在成熟酶的氨基末端附近存在一个可能的FAD或NADPH结合位点。
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