A novel proenkephalin processing carboxypeptidase and its activation by cyclic AMP dependent protein kinase.
Carboxypeptidase B-like enzymes cleaving Met-enkephalin-Arg from synaptosomes of the rat striatum purified using a DEAE-cellulose column and Met-Arg-CH-Sepharose 4B affinity column proved to be different from enkephalin-convertase, lysosomal carboxypeptidase B-like enzyme, pancreas carboxypeptidase B and carboxypeptidase Y, in effects of inhibitors and activators, pH optimum (7.5-8.5) and molecular size (50,000). This enzyme, named "Processin CP-E" was activated by cAMP dependent protein kinase, and the Vmax was increased from 4.3 to 13.3 microM/min/mg protein, while the Km (28.2 microM) was unchanged.
D000818:Animals; D043424:Carboxypeptidase B; D002268:Carboxypeptidases / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D002417:Cattle; D000242:Cyclic AMP / Q000494:pharmacology; D004744:Enkephalin, Methionine / Q000031:analogs & derivatives / Q000378:metabolism; D004745:Enkephalins / Q000378:metabolism*; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011494:Protein Kinases / Q000494:pharmacology*; D011498:Protein Precursors / Q000378:metabolism*; D051381:Rats; D013574:Synaptosomes / Q000201:enzymology
D004745:Enkephalins; D011498:Protein Precursors; C029992:proenkephalin; D004744:Enkephalin, Methionine; C028719:enkephalin-Met, Arg(6)-; D000242:Cyclic AMP; D011494:Protein Kinases; D002268:Carboxypeptidases; D043424:Carboxypeptidase B