title: Enkephalinase: selective inhibitors and partial characterization.
abstract: There are at least two types of enzymes in brain, endopeptidases and aminopeptidases, which metabolize enkephalins. Evidence is presented to suggest that enkephalinase, an endopeptidase cleaving at the Gly-Phe bond, is specific for the endogenous enkephalinergic system. Selective inhibitors are described for each enzyme. These are parachloromercuriphenylsulfonic acid and puromycin in the case of aminopeptidases and various enkephalin fragments in the case of enkephalinase. Some characteristics of the two types of enzymes are described. Enkephalinase has many properties in common with the well-characterized brain angiotensin-converting enzyme. These two enzymes, however, behaved differently when tested for chloride dependence, for activity in several buffers and for susceptibility to specific inhibitors.
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors; D000818:Animals; D002417:Cattle; D002421:Caudate Nucleus / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D004723:Endorphins / Q000494:pharmacology*; D004743:Enkephalin, Leucine; D004745:Enkephalins / Q000037:antagonists & inhibitors / Q000494:pharmacology*; D015260:Neprilysin; D009842:Oligopeptides / Q000494:pharmacology*; D011480:Protease Inhibitors; D051381:Rats; D013329:Structure-Activity Relationship
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D004723:Endorphins; D004745:Enkephalins; D009842:Oligopeptides; D011480:Protease Inhibitors; D004743:Enkephalin, Leucine; D015260:Neprilysin