Neuropeptide-specific peptidases: does brain contain a specific TRH-degrading enzyme?
The particulate fraction of brain homogenates contains an enzyme that cleaves the pyroglutamyl-histidyl bond of thyrotropin-releasing hormone (TRH) but is clearly distinct from the more widely distributed pyroglutamyl peptidase (EC 3.4.19.3). This particulate enzyme is highly localized to brain where it is found on synaptosomal membranes. It exhibits an unusual degree of substrate specificity. For example, it does not cleave the pyroglutamyl-histidyl bond of luteinizing hormone-releasing hormone (LHRH) or the pyroglutamyl histidyl bond of the chromogenic substrate pyroglutamyl-histidyl-2-naphthylamide. Evidence is reviewed supporting the possibility that this enzyme, first detected in serum and originally referred to as "thyroliberinase", may be the first neuropeptide-specific peptidase to be characterized.
D000626:Aminopeptidases; D000818:Animals; D001921:Brain / Q000201:enzymology*; D010450:Endopeptidases / Q000378:metabolism*; D011761:Pyrrolidonecarboxylic Acid / Q000031:analogs & derivatives; D013379:Substrate Specificity; D013574:Synaptosomes / Q000201:enzymology; D013973:Thyrotropin-Releasing Hormone / Q000378:metabolism*
D013973:Thyrotropin-Releasing Hormone; D010450:Endopeptidases; D000626:Aminopeptidases; C023166:pyroglutamyl-peptidase II; D011761:Pyrrolidonecarboxylic Acid