A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme.

A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme.
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DOI:
10.1073/pnas.88.17.7610
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发表时间:
1991-09
影响因子:
11.1
通讯作者:
M. Yasunami;Cheng-Sheng Chen;A. Yoshida
M. Yasunami;Cheng-Sheng Chen;A. Yoshida
中科院分区:
综合性期刊1区
文献类型:
--
作者:
M. Yasunami;Cheng-Sheng Chen;A. Yoshida

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人酒精脱氢酶(alcohol dehydrogenase, ADH; alcohol:NAD+ oxidoreductase, EC 1.1.1.1)基因家族由5个已知基因座(ADH1-ADH5)组成,它们在4号染色体(4q21-25)上被定位在一起。由这些基因编码的ADH同工酶根据其酶学性质分为三种不同的类别。在不同类的成员之间观察到适度的结构相似性。通过与ADH2 (class I) cDNA探针的交叉杂交,我们分离出了ADH基因家族的另一个成员。该基因对应的cDNA克隆也从pcr扩增文库中得到。全长368个氨基酸的开放阅读框的编码序列被内含子打断为8个外显子,在基因组上跨越约17000个碱基。该基因在5'区含有糖皮质激素反应元件。在胃和肝脏中检测到转录本。开放阅读框的氨基酸序列与已知人类ADHs的位置一致性约为60%。这种程度的同源性与人类ADH家族的类间相似性相当。因此,新发现的基因,被命名为ADH6,控制一种酶的合成,这种酶属于另一类adh,可能具有独特的生理作用。
The human alcohol dehydrogenase (ADH; alcohol:NAD+ oxidoreductase, EC 1.1.1.1) gene family consists of five known loci (ADH1-ADH5), which have been mapped close together on chromosome 4 (4q21-25). ADH isozymes encoded by these genes are grouped in three distinct classes in terms of their enzymological properties. A moderate structural similarity is observed between the members of different classes. We isolated an additional member of the ADH gene family by means of cross-hybridization with the ADH2 (class I) cDNA probe. cDNA clones corresponding to this gene were derived from PCR-amplified libraries as well. The coding sequence of a 368-amino-acid-long open reading frame was interrupted by introns into eight exons and spanned approximately 17 kilobases on the genome. The gene contains a glucocorticoid response element at the 5' region. The transcript was detected in the stomach and liver. The deduced amino acid sequence of the open reading frame showed about 60% positional identity with known human ADHs. This extent of homology is comparable to interclass similarity in the human ADH family. Thus, the newly identified gene, which is designated ADH6, governs the synthesis of an enzyme that belongs to another class of ADHs presumably with a distinct physiological role.