A dipeptidyl carboxypeptidase in brain synaptic membranes active in the metabolism of enkephalin containing peptides.
A dipeptidyl carboxypeptidase activity has been localized in synaptic plasma membranes which have been prepared from isolated rat brain cortical synaptosomes. The specificity of this proteolytic activity towards various synthetic and biological active peptides is compared to the peptidase activities of intact synaptosomes. In contrast to the synaptosomal peptidases which are capable of cleaving all peptide bonds of Met-enkephalin-Arg6-Phe7 the peptidase activity associated with the synaptic plasma membrane exclusively hydrolyses a dipeptide from the carboxyl terminus of all hepta- and hexapeptides tested. The fact that this dipeptidyl carboxypeptidase does not cleave the Gly3-Phe4 peptide bond of Met-enkephalin suggests that this enzyme is different from "enkephalinase". The synaptic membrane dipeptidyl carboxypeptidase is inhibited by metal chelating agents and thiols but is not affected by compounds known to inhibit serine proteases, thermolysin and "enkephalinase".
D000595:Amino Acid Sequence; D000818:Animals; D002540:Cerebral Cortex / Q000201:enzymology*; D010450:Endopeptidases / Q000378:metabolism*; D004745:Enkephalins / Q000378:metabolism*; D007700:Kinetics; D051381:Rats; D013379:Substrate Specificity; D013570:Synaptic Membranes / Q000201:enzymology*; D013574:Synaptosomes / Q000201:enzymology
D004745:Enkephalins; D010450:Endopeptidases; C020071:dipeptidyl carboxypeptidase