Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase
Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase
复制标题
大鼠线粒体烯酰辅酶A水合酶cDNA的分子克隆和序列分析
DOI:
10.1111/j.1432-1033.1989.tb15083.x
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发表时间:
1989
期刊:
影响因子:
5.4
通讯作者:
T. Hashimoto
中科院分区:
文献类型:
--
作者:
N. Minami;S. Taketani;T. Osumi;T. Hashimoto
To elucidate structural relationships between the mitochondrial and peroxisomal isozymes of β-oxidation systems, cDNA of the mitochondrial enoyl-CoA hydratase was cloned and sequenced. The 1454-bp cDNA sequence contained a 870 bp of open reading frame, encoding a polypeptide of 290 amino acid residues. When compared with the amino-terminal sequence of the mature enzyme, the predicted sequence contained a 29-residue presequence at the amino terminus. This presequence had characteristics typical of a mitochondrial signal peptide. The primary structure of this enzyme showed significant similarity with the amino-terminal portion of sequence of the peroxisomal enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme. The carboxy-terminal part of the latter enzyme has sequence similarity with mitochondrial 3-hydroxyacyl-CoA dehydrogenase [Ishii, N., Hijikata, M., Osumi, T. & Hashimoto, T. (1987) J. Biol. Chem. 262, 8144–8150]. These findings suggest that the peroxisomal bifunctional enzyme has the hydratase and dehydrogenase functions on the amino- and carboxy-terminal sides, respectively. The mitochondrial β-oxidation enzymes and the peroxisomal bifunctional enzyme may have common evolutionary origins.
DOI:
10.1073/pnas.80.5.1194
发表时间:
1983-01-01
期刊:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子:
--
作者:
YOUNG, RA;DAVIS, RW
通讯作者:
DAVIS, RW