Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver.
Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver.
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来自成人肝脏的含黄素单加氧酶（II 型）cDNA 的分子克隆。
DOI：
10.1073/pnas.89.5.1685
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发表时间：
1992
影响因子：
11.1
通讯作者：
Cashman,JR
中科院分区：
文献类型：
--
作者：
Lomri,N;Gu,Q;Cashman,JR
从lambda gt10和lambda gt11文库中分离到编码成人肝脏含黄素单加氧酶（FMO; dimethylaniline N-oxidase, EC 1.14.13.8）的cDNA克隆。利用猪肝FMO cDNA核酸序列合成的3个36-mer寡核苷酸探针对cDNA文库进行筛选。推导出的成人肝脏FMO氨基酸序列与猪肝FMO有较大差异，并将其命名为II型（HLFMO II）。HLFMO II全长cDNA序列[2119碱基对（bp）]有1599个核苷酸的开放阅读框，编码533个氨基酸的Mr 59,179蛋白，5'-非编码区136个核苷酸，3'-非编码区369个核苷酸（不包括聚(a)尾）。所得HLFMOⅱ的氨基酸序列与兔肝FMOⅱ的相似度为80%，与兔肝（I型）、猪肝（I型）和胎人肝（I型）FMOs的氨基酸相似性分别为52%、55%和53%。对成人肝脏RNA进行分析，发现HLFMOⅱmRNA有1种。基因组DNA分析表明，HLFMO II为单基因产物。这些结果表明，推导出的HLFMO II的氨基酸序列含有高度保守的残基，表明FMO酶具有密切的亲缘关系，并且无疑来自同一祖先基因。
Complementary DNA (cDNA) clones encoding the adult human liver flavin-containing monooxygenase (FMO; dimethylaniline N-oxidase, EC 1.14.13.8) were isolated from lambda gt10 and lambda gt11 libraries. The cDNA libraries were screened with three synthetic 36-mer oligonucleotide probes derived from the nucleic acid sequence of the pig liver FMO cDNA. The deduced amino acid sequence for the adult human liver FMO was quite distinct from the pig liver FMO, and adult human liver FMO was designated form II (HLFMO II). The full-length cDNA sequence of HLFMO II [2119 base pairs (bp)] had an open reading frame of 1599 nucleotides, which encoded a 533-amino acid protein of Mr 59,179, a 5'-noncoding region of 136 nucleotides and a 3'-noncoding region of 369 nucleotides excluding the poly(A) tail. The deduced amino acid sequence of HLFMO II had 80% similarity with the rabbit liver FMO II but only a 52%, 55%, and 53% amino acid similarity with the rabbit liver (form I), the pig liver (form I), and fetal human liver (form I) FMOs, respectively. RNA analysis of adult human liver RNA showed that there was one HLFMO II mRNA species. Analysis of genomic DNA indicated that HLFMO II was the product of a single gene. These results indicated that the deduced amino acid sequence for HLFMO II contained highly conserved residues and suggested that FMO enzymes were closely related and, undoubtedly, derived from the same ancestral gene.