Title : Molecular cloning and amino acid
sequence of rat
enkephalinase
Abstract :
- cDNA clones encoding rat enkephalinase ( neutral endopeptidase , EC 3.4.24.11) have been isolated in lambda gt10 libraries from both brain and kidney mRNAs and the complete 742 amino acid sequence of rat enkephalinase is presented
- The enzyme possesses a single transmembrane spanning domain near the N-terminal of the molecule but lacks a signal sequence
- Because enkephalinase has it active site located extracellularly and is thus an ectopeptidase, we suggest that the N-terminal transmembrane region of the enzyme anchors the protein in membranes and that the majority of the protein, including the carboxy terminus , is extracellular
- Enkephalinase , a zinc-containing metallo enzyme , displays homology with other zinc metallo enzymes such as carboxypeptidase A, B and E , suggesting enzymatic similarities in these enzymes