Inhibitors of calf-brain enkephalinase A and B

Enkephalinase A and B isolated from calf-brain striatum have comparable substrate specificity (Km for Leu-enkephalin = 1-3.10(-5) microM) but a quite different affinity for certain inhibitors: phosphate, Secobarbital and Thiorphan are effective inhibitors for Enkephalinase A (IC50 of 2.5 mM, 30 microM and 4 nM respectively), while Enkephalinase B does not react with any of these compounds. Both enzymes are inhibited by 1 mM EDTA and o-phenanthroline indicating the presence of a metal atom in or near their active sites. Although with different abilities, both enzymes recognize dipeptides having at least one hydrophobic amino-acid side chain. The potency of such dipeptides can be used for a description of the active site.