Properties of "enkephalinase" from rat kidney: comparison of dipeptidyl-carboxypeptidase and endopeptidase activities
Malfroy, B.; Schwartz, J.C.
Biochemical and Biophysical Research Communications 106(2): 276-285
1982
ISSN/ISBN: 0006-291X PMID: 7049171 Document Number: 184617
The enkepalinase i.e. the metallopeptidase cleaving the Gly3-Phe4 amide bond of enkephalins from rat kidney was studied in its membrane-bound form and in a highly purified preparation. It seems identical or very close to 3 other enzyme activities: enkephalinase from cerebral membranes, an endopeptidase from bovine pituitary and the neutral endopeptidase from rabbit kidney. Specificity constants of substrates were higher for peptides with a free terminal carboxylate as compared to amidified or typical endopeptidase substrates which were also cleaved. The dipeptidyl carboxypeptidase specificity of enkephalinase is attributable to the presence of a critical arginine residue in its active site.