Complete amino acid sequence of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes.
Complete amino acid sequence of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes.
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来自猪肝微粒体的 NADPH-细胞色素 P-450 还原酶的完整氨基酸序列。
DOI：
10.1021/bi00372a018
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发表时间：
1986
期刊：
影响因子：
2.9
通讯作者：
Shively,JE
中科院分区：
文献类型：
--
作者：
Haniu,M;Iyanagi,T;Miller,P;Lee,TD;Shively,JE
91010加州杜阿尔特希望城贝克曼研究所免疫学教研室和日本筑波大学基础医学研究所生化室1986年4月24日收到修订稿件1986年7月10日收到摘要：通过对几组蛋白水解性片段的微序列分析，测定了猪肝微粒体NADPH-细胞色素P-450还原酶的完整氨基酸序列。首先对20kDa的片段进行了序列研究，然后对80 kDa的片段进行了序列研究。成熟蛋白的氨基末端被乙酰基封堵，其次是676个氨基酸残基。结果表明，COOH末端的20 kDa片段是通过ASN-Gly(残基502-503)链上的裂解而产生的，其机制未知。NADPH保护的半胱氨酸残基位于第565位，靠近与铁还蛋白-NADP+还原酶高度同源的区域。FMN和FAD结合区可能分别位于蛋白质分子的氨基末端和中部，正如Porter和Kasper[Porter，T.D.，&Kasper，C.B.(1985)Proc]所提出的那样。娜塔莉。阿卡德。SCI。美国82,973-977]，当该序列与大鼠酶的序列比较时，有60个氨基酸残基被取代，这可能是由于物种的差异。然而，这些酶之间的总序列同源性为90%。疏水图分析表明，残基27-43和残基523-544的两个区域表现出高度的疏水性，表明细胞色素P-450与膜结合或相互作用。
Division of Immunology, Beckman Research Institute of the City of Hope, Duarte, California 91010, and Division of Biochemistry, Institute of Basic Medical Sciences, The University of Tsukuba, Ibaraki 305, Japan Received April 24, 1986; Revised Manuscript Received July 10, 1986 abstract: The complete amino acid sequence of porcine hepatic microsomal NADPH-cytochrome P-450 reductase has been determined by microsequence analysis on several sets of proteolytic fragments. Sequence studies were performed initially on a 20-kilodalton (kDa) fragment and then on 80-kDa fragment. The amino-terminal end of the mature protein was blocked with an acetyl group, followed by 676 amino acid residues. It has been revealed that the COOH-terminal 20-kDa fragment has been derived fromoriginal enzyme by cleavage at the Asn-Gly (residues 502-503) linkage by an unknown mechanism. An NADPH-protected cysteine residue is located at residue 565, near a region exhibiting high sequence homology with ferredoxin-NADP+ reductase. The FMN and FAD binding regions are possibly located in the amino-terminal regionand the middle part of the protein molecule, respectively, as suggested by Porter and Kasper [Porter, T. D., & Kasper, C. B.(1985) Proc. Natl. Acad. Sci. USA 82, 973-977], When this sequence is compared with that of rat enzyme, 60 amino acid residues are substituted, probably due to species differences. However, total sequence homology between these enzymes is 90%. Hydropathy plot analysis reveals that two regions from residues 27-43 and from residues 523-544 exhibit a high degree of hydrophobicity, suggesting membrane binding or interaction with cytochrome P-450.
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DOI：
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DOI：
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发表时间：
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期刊：
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影响因子：
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DOI：
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发表时间：
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期刊：
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