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Amino peptidases in brassica napus part 2 effect of metal ions amino acid composition and catalytic properties of the relative alanine specific amino peptidase



Amino peptidases in brassica napus part 2 effect of metal ions amino acid composition and catalytic properties of the relative alanine specific amino peptidase



Biochemie und Physiologie der Pflanzen (BPP) 170(2): 143-151



Evidence was presented that the relative alanine specific aminopeptidase does not exist as a metal-enzyme-complex. Bivalent cations decrease the enzyme activity in the following order: Mg2+ < Mn2+ < Co2+ < Cu2+ < Zn2+ < Hg2+. The kinetic parameters of the hydrolysis of p-substituted L-alanine-anilides are correlated with the electronic properties of the substituents. The results were evidence for nucleophilic properties of the active site. Sulfhydryl groups are important for the maintenance of the catalytic activity, although it is not clear whether they are part of the active center. The decline of the enzyme activity curve was greatest when the 2 sulfhydryl groups were blocked by Hg2+ or Ag2+. Reducing sulfhydryl compounds do not act as stabilizers or activators of the aminopeptidase. The amino acid composition of the aminopeptidase is characterized by a relatively high content of hydrophobic amino acid residues and of residues with ionizable side chains.

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Accession: 004710728

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