| Abstract: | In this study, a highly active foliar aminopeptidase preferentially releasing N-terminal alanine from artificial substrates was purified and characterized from cucumber (Cucumis sativus L. suyo). The enzyme had a molecular mass of 200 kDa consisting of two subunits of 95 kDa. It was a metalloprotease the pH optimum of which was 8 to 9. It cleaved Ala-, Gly-, Met-, Ser-, Leu-, Lys-, and Arg artificial substrates. An internal amino acid sequence was similar to those of aminopeptidase N (clan MA, family M1) of microorganisms, and was very similar to that of a putative aminopeptidase N of Arabidopsis thaliana. From these results, the highly active aminopeptidase in cucumber leaves was identified to be a plant aminopepitdase N. |
