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Molecular cloning and amino acid sequence of human enkephalinase (neutral endopeptidase)
Author(s) -
Malfroy Bernard,
Kuang Wun-Jing,
Seeburg Peter H.,
Mason Anthony J.,
Schofield Peter R.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80828-7
Subject(s) - enkephalinase , endopeptidase , complementary dna , neprilysin , peptide sequence , amino acid , microbiology and biotechnology , biology , cdna library , biochemistry , molecular cloning , transmembrane domain , homology (biology) , enzyme , chemistry , gene , enkephalin , receptor , opioid
We have isolated a cDNA clone encoding human enkephalinase (neutral endopeptidase, EC 3.4.24.11) in a λgt10 library from human placenta, and present the complete 742 amino acid sequence of human enkephalinase. The human enzyme displays a high homology with rat and rabbit enkephalinase. Like the rat and rabbit enzyme, human enkephalinase contains a single N‐terminal transmembrane region and is likely to be inserted through cell membranes with the majority of protein, including its carboxy‐terminus, located extracellularly.