Molecular Cloning and Heterologous Expression of Pea Seedling Copper Amine Oxidase
作者： Tomoyoshi KOYANAGI , Kiyoyuki MATSUMURA , Shun’ichi KURODA , Katsuyuki TANIZAWA
DOI: 10.1271/BBB.64.717
关键词: Enzyme 、 Pichia pastoris 、 Peptide sequence 、 Molecular biology 、 Yeast 、 Cofactor 、 Amine oxidase (copper-containing) 、 Enzyme assay 、 Heterologous expression 、 Biochemistry 、 Biology
摘要: The cDNA coding for copper amine oxidase has been cloned from etiolated pea seedlings (Pisum sativum). deduced amino acid sequence, consisting of 674 residues including the signal peptide, agreed well with those reported enzymes a different cultivar P. sativum and other plant sources, except several evolutionary replacements located mostly on molecular surface. A heterologous expression system enzyme was constructed yeast Pichia pastoris, using AOX1 promoter α-factor secretion signal. Adding to culture medium increased an active, quinone-containing enzyme. Furthermore, inactive produced in copper-deficient activated considerably by subsequent incubation excess cupric ions. These results strongly suggest that Tyr-derived redox cofactor, 2,4,5-trihydroxyphenylalanylquinone (topa quinone, TPQ), is post-translational modification proceeds through copper-dependent, self-processing mechanism, as bacteria yeast.
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