NADPH CYTOCHROME-P-450 OXIDOREDUCTASE - FLAVIN MONONUCLEOTIDE AND FLAVIN ADENINE-DINUCLEOTIDE DOMAINS EVOLVED FROM DIFFERENT FLAVOPROTEINS
NADPH CYTOCHROME-P-450 OXIDOREDUCTASE - FLAVIN MONONUCLEOTIDE AND FLAVIN ADENINE-DINUCLEOTIDE DOMAINS EVOLVED FROM DIFFERENT FLAVOPROTEINS
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DOI：
10.1021/bi00355a036
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发表时间：
1986-04-08
期刊：
影响因子：
2.9
通讯作者：
KASPER, CB
中科院分区：
文献类型：
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作者：
PORTER, TD;KASPER, CB
NADPH-细胞色素P-450氧化还原酶的FMN结合区(残基77-228)与细菌黄毒素同源，而FAD结合区(残基267-678)与两种含有FAD的蛋白质(铁还蛋白-NADP+还原酶和NADH-细胞色素b5还原酶)高度相似。将这些蛋白质与谷胱甘肽还原酶进行比较，可以初步鉴定这些蛋白质中的FAD和辅因子结合残基。谷胱甘肽还原酶是一种已知的三维结构的黄素蛋白。NADPH-细胞色素P-450氧化还原酶和铁氧还蛋白-NADP+还原酶序列的显著保守性，以及氧化还原酶的FMN结合域与细菌黄素的同源性，表明NADPH-细胞色素P-450氧化还原酶是这两个功能连锁的黄素蛋白的祖先基因融合的结果。
The FMN-binding domain of NADPH-cytochrome P-450 oxidoreductase, residues 77-228, is homologous with bacterial flavodoxins, while the FAD-binding domain, residues 267-678, shows a high degree of similarity to two FAD-containing proteins, ferredoxin-NADP+ reductase and NADH-cytochrome b5 reductase. Comparison of these proteins to glutathione reductase, a flavoprotein whose three-dimensional structure is known, has permitted tentative identification of FAD- and cofactor-binding residues in these proteins. The remarkable conservation of sequence between NADPH-cytochrome P-450 oxidoreductase and ferredoxin-NADP+ reductase, coupled with the homology of the FMN-binding domain of the oxidoreductase with the bacterial flavodoxins, implies that NADPH-cytochrome P-450 oxidoreductase arose as a result of fusion of the ancestral genes for these two functionally linked flavoproteins.