Jul 1, 1974

Aminopeptides of pea

The Biochemical Journal
T C Elleman

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.

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Mentioned in this Paper

Electrophoresis, Paper
Amides
Enzymes, antithrombotic
SDS-PAGE
Amino Acids, I.V. solution additive
Aminopeptidase
Proline
Centrifugation
Amide local anesthetics
Enzymes for Treatment of Wounds and Ulcers

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