猪NADPH-细胞色素P-450还原酶亲水结构域的完整结构

Complete structure of the hydrophilic domain in the porcine NADPH-cytochrome P-450 reductase.

作者信息

Vogel F, Lumper L

出版信息

Biochem J. 1986 Jun 15;236(3):871-8. doi: 10.1042/bj2360871.

DOI:10.1042/bj2360871

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1146921/

Abstract

The 622-residue amino acid sequence of the hydrophilic domain in the porcine NADPH-cytochrome P-450 reductase (EC 1.6.2.4) is reported. The structural data required to complete the sequences published previously [Vogel, Kaiser, Witt & Lumper (1985) Biol. Chem. Hoppe-Seyler 366, 577-587] and to establish the primary structure of the porcine hydrophilic domain have been obtained by sequencing proteolytic subfragments derived from CNBr fragments and by characterizing the overlapping S-[14C]methylmethionine-containing peptides isolated from tryptic digests of the [14C]methyl-labelled hydrophilic domain. The hydrophilic domain displays 91.8% positional identity with that of the corresponding domain in the rat NADPH-cytochrome P-450 reductase. The region Val528-Ser678 in the NADPH-cytochrome P-450 reductase shows a significant homology to the sequence Ile165-Tyr314 in the spinach ferredoxin-NADP+ oxidoreductase. A model for the secondary structure of the hydrophilic domain has been derived by computer-assisted analysis of the amino acid sequence. Cys472 and Cys566 are protected against chemical modification in the NADP+ complex of the NADPH-cytochrome P-450 reductase.

摘要

本文报道了猪NADPH-细胞色素P-450还原酶（EC 1.6.2.4）亲水结构域的622个氨基酸残基序列。通过对源自CNBr片段的蛋白水解亚片段进行测序，以及对从[14C]甲基标记的亲水结构域的胰蛋白酶消化物中分离出的重叠含S-[14C]甲基甲硫氨酸的肽段进行表征，获得了完成先前发表的序列[Vogel, Kaiser, Witt & Lumper (1985) Biol. Chem. Hoppe-Seyler 366, 577 - 587]并确定猪亲水结构域一级结构所需的结构数据。该亲水结构域与大鼠NADPH-细胞色素P-450还原酶相应结构域的位置一致性为91.8%。NADPH-细胞色素P-450还原酶中Val528 - Ser678区域与菠菜铁氧化还原蛋白-NADP+氧化还原酶中的Ile165 - Tyr314序列具有显著同源性。通过对氨基酸序列进行计算机辅助分析，得出了亲水结构域的二级结构模型。在NADPH-细胞色素P-450还原酶的NADP+复合物中，Cys472和Cys566免受化学修饰。

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本文引用的文献

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