Further characterization of the substrate specificity of a TRH hydrolysing pyroglutamate aminopeptidase from guinea-pig brain.
In this study the substrate specificity of a pyroglutamate aminopeptidase from synaptosomal membranes of guinea-pig brain was investigated. The enzyme was found to be specific for tripeptides, tripeptide-amides and tetrapeptides which possess the N-terminal sequence Glp-His and as such is specific for Thyrotropin Releasing Hormone or only very closely related peptides. The enzyme was found not to hydrolyse a number of analogues of Thyrotropin Releasing Hormone which have been shown to have therapeutical value in certain neuronal disorders.
Elmore
M A
MA
Department of Biochemistry, University College, Galway, Ireland.
Griffiths
E C
EC
O'Connor
B
B
O'Cuinn
G
G
D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D006168:Guinea Pigs; D006868:Hydrolysis; D007700:Kinetics; D011751:Pyroglutamyl-Peptidase I / Q000378:metabolism*; D013379:Substrate Specificity; D013574:Synaptosomes / Q000201:enzymology; D013973:Thyrotropin-Releasing Hormone / Q000378:metabolism*
D013973:Thyrotropin-Releasing Hormone; D000626:Aminopeptidases; D011751:Pyroglutamyl-Peptidase I