cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1).
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Gebhard W, Schube M, Eulitz M
cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1).
Eur J Biochem. 1989 Jan 2;178(3):603-7.
- PubMed ID
- 2912725 [ View in PubMed]
- Abstract
The human plasma metallo-protease carboxypeptidase N of Mr 280,000 consists of two small, enzymatically active subunits of Mr 50,000 and two large subunits. Only the large subunits are glycosylated. They may have a function in stabilizing the complex in plasma. The N-terminal sequence of the small subunit was determined from the isolated protein and used to specify a unique 59-mer oligonucleotide probe. A cDNA clone of 1.7 kbp containing the entire coding sequence of the small subunit of carboxypeptidase N was isolated from a human-liver cDNA library. The cDNA clone encodes a signal sequence of 20 amino acids and the 438 amino acids of the mature subunit. There is a remarkable primary structure similarity of 49% to bovine carboxypeptidase E (enkephalin convertase). A more distant relationship to the bovine pancreatic, digestive carboxypeptidases A and B or even to the metallo-endopeptidases is based mainly on the occurrence of conserved, mechanistically important residues.