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大鼠NADPH-细胞色素P-450氧化还原酶cDNA的编码核苷酸序列及黄素结合结构域的鉴定。

Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains.

作者信息

Porter T D, Kasper C B

出版信息

Proc Natl Acad Sci U S A. 1985 Feb;82(4):973-7. doi: 10.1073/pnas.82.4.973.

DOI:10.1073/pnas.82.4.973
PMID:3919392
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC397175/
Abstract

The coding nucleotide sequence of the mRNA for NADPH-cytochrome P-450 oxidoreductase (NADPH:ferricytochrome oxidoreductase, EC 1.6.2.4) from rat liver was determined from two overlapping cDNA clones, pOR-7 and pOR-8, which together contain 2401 nucleotides complementary to rat liver oxidoreductase mRNA. The single open reading frame of 2034 nucleotides spanning these cDNAs codes for a 678 amino acid polypeptide with a molecular weight of 76,962. The deduced amino acid composition is in excellent agreement with that determined by direct amino acid analysis of purified rat liver P-450 oxidoreductase, and the amino-terminal region (residues 1-80) largely coincides with the amino-terminal sequence of the oxidoreductase isolated from rabbit liver. Comparison of the amino acid sequence to those of other flavoproteins revealed two separate domains that are likely to be involved in flavin binding: a long segment (residues 77-228) homologous with Desulfovibrio vulgaris flavodoxin, an FMN-containing protein, and a shorter segment (residues 452-477) homologous with the FAD-binding segment of fumarate reductase from Escherichia coli.

摘要

从大鼠肝脏中分离出两个重叠的cDNA克隆pOR - 7和pOR - 8，由此确定了NADPH - 细胞色素P - 450氧化还原酶（NADPH：铁细胞色素氧化还原酶，EC 1.6.2.4）mRNA的编码核苷酸序列。这两个克隆共包含2401个与大鼠肝脏氧化还原酶mRNA互补的核苷酸。跨越这些cDNA的2034个核苷酸的单一开放阅读框编码一个678个氨基酸的多肽，分子量为76,962。推导的氨基酸组成与通过对纯化的大鼠肝脏P - 450氧化还原酶进行直接氨基酸分析所确定的结果高度一致，并且氨基末端区域（第1 - 80位氨基酸残基）与从兔肝脏中分离的氧化还原酶的氨基末端序列基本一致。将该氨基酸序列与其他黄素蛋白的序列进行比较，发现了两个可能参与黄素结合的不同结构域：一个长片段（第77 - 228位氨基酸残基）与含有FMN的普通脱硫弧菌黄素氧还蛋白同源，另一个较短片段（第452 - 477位氨基酸残基）与大肠杆菌延胡索酸还原酶的FAD结合片段同源。

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