title: Aminopeptides of pea.
abstract: Studies of crude extracts of pea seeds (Pisum sativum, var. Green feast) revealed the presence of three enzymes that hydrolyse the amide bond of aminoacyl beta-naphthylamides. They differ in their specificity towards the aminoacyl moiety; one is proline-specific, whereas the other two hydrolyse the beta-naphthylamides of primary amino acids. Of the latter, one is highly specific for hydrophobic aminoacyl residues whereas the other has a broader, somewhat complementary specificity, showing preferential hydrolysis of non-hydrophobic aminoacyl residues. These latter two aminoacyl-beta-naphthylamidases have been separated and partly characterized with regard to substrate specificity and antagonism by inhibitors. Both are true aminopeptidases, requiring the presence of a free amino group and hydrolysing the amide bonds of amino acid amides, dipeptides and oligopeptides consecutively from the N-terminal end.
mesh_terms: D000626:Aminopeptidases / Q000032:analysis* / Q000378:metabolism; D002498:Centrifugation; D002850:Chromatography, Gel; D003956:Dialysis; D004590:Electrophoresis, Paper; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*; D011392:Proline; D013053:Spectrophotometry
chemical_list: D011392:Proline; D000626:Aminopeptidases