Purification of an aminopeptidase preferentially releasing N-terminal alanine from cucumber leaves and its identification as a plant aminopeptidase N

Article abstract of DOI:10.1271/bbb.65.2802

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.

Full text of DOI:10.1271/bbb.65.2802

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Bioscience, Biotechnology, and Biochemistry
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Purification of an Aminopeptidase Preferentially
Releasing N-terminal Alanine from Cucumber Leaves
and Its Identification as a Plant Aminopeptidase N
Yasuo YAMAUCHIa, Yukinori EJIRIa & Kiyoshi TANAKAa
a Faculty of Agriculture, Tottori University
Published online: 22 May 2014.
To cite this article: Yasuo YAMAUCHI, Yukinori EJIRI & Kiyoshi TANAKA (2001) Purification of an Aminopeptidase
Preferentially Releasing N-terminal Alanine from Cucumber Leaves and Its Identification as a Plant Aminopeptidase N,
Bioscience, Biotechnology, and Biochemistry, 65:12, 2802-2805, DOI: 10.1271/bbb.65.2802
To link to this article: http://dx.doi.org/10.1271/bbb.65.2802
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