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KMID : 0903520060490040293
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology
2006 Volume.49 No. 4 p.293 ~ p.297
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Cloning of Pig Kidney cDNA Encoding an Angiotensin I Converting Enzyme
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Yoon Jang-Ho
Yoon Joo-Ok
Hong Kwang-Won
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Abstract
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Angiotensin converting enzyme (ACE) is a zinc-containing dipeptidase widely distributed in mammalian tissues and is thought to play a significant role in blood pressure regulation by hydrolyzing angiotensin I to the potent vasoconstrictor, angiotensin II. Recently, the presence of ACE in pig ovary was reported and the ACE from pig kidney was isolated and characterized. However no nucleotide sequence of the ACE gene from pig is yet known. We report here the cloning of the ACE cDNA from pig kidney by using the reverse transcriptase-polymerase chain reaction. The complete amino acid sequence deduced from the cDNA contains 1309 residues with a molecular mass of 150 kDa, beginning with a signal peptide of 33 amino acids. Amino acid sequence analysis showed that pig kidney ACE is also probably anchored by a short transmembrane domain located near the C-terminus. This protein contains a tandem duplication of the two homologous amino acid peptidase domain. Each of these two domains bears a putative metal-binding site (His-Glu- Met-Gly-His) identified in mammalian somatic ACE. The alignment of pig ACE amino acid sequence with human, rabbit, and mouse reveals that both two domains have been highly conserved during evolution.
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KEYWORD
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pig kidney, cDNA cloning, angiotensin-converting enzyme (ACE), dipeptidyl carboxypeptidase
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