Rabbit brain thiol-activated endopeptidase. Hydrolysis of bradykinin and kininogen.
A neutral brain endopeptidase which hydrolyzes bradykinin (Arg1-Pro2-Pro3-Gly4-Phe5-Ser6-Pro7-Phe8-Arg9) at the Phe5-Ser6 peptide bond was activated about 10 times by dithiothreitol. The preferential specificity of the enzyme for small peptides was suggested on the basis of the absence of activity toward a bradykinin-related protein such as S-carboxymethylated plasma kininogen.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001920:Bradykinin / Q000378:metabolism*; D001921:Brain / Q000201:enzymology* / Q000648:ultrastructure; D004229:Dithiothreitol / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D066298:In Vitro Techniques; D007704:Kininogens / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D010455:Peptides / Q000032:analysis; D011817:Rabbits; D013347:Subcellular Fractions / Q000201:enzymology; D013438:Sulfhydryl Compounds / Q000494:pharmacology*; D013997:Time Factors
D000596:Amino Acids; D007704:Kininogens; D010455:Peptides; D013438:Sulfhydryl Compounds; D010447:Peptide Hydrolases; D001920:Bradykinin; D004229:Dithiothreitol