Heterologous Expression and Characterization of Tea () Polyamine Oxidase Homologs and Their Involvement in Stresses.

Polyamine oxidase (PAO) is a key enzyme maintaining polyamine homeostasis, which affects plant physiological activities. Until now, the gene members and function of PAOs in tea () have not been fully identified. Here, through the expression in and , we identified six genes annotated as in tea genome and transcriptome and determined their enzyme reaction modes and gene expression profiles in tea cultivar 'Yinghong 9'. We found that CsPAO1,2,3 could catalyze spermine, thermospermine, and norspermidine, and CsPAO2,3 could catalyze spermidine in the back-conversion mode, which indicated that the precursor of γ-aminobutyric acid might originate from the oxidation of putrescin but not spermidine. We further investigated the changes of CsPAO activity with temperature and pH and their stability. Kinetic parameters suggested that CsPAO2 was the major PAO modifying polyamine composition in tea, and it could be inactivated by β-hydroxyethylhydrazine and aminoguanidine. Putrescine content and expression were high in tea flowers. responded to wound, drought, and salt stress; might be the main member responding to cold stress; anoxia induced . We conclude that in terms of phylogenetic tree, enzyme characteristics, and expression profile, might be the dominant in the polyamine degradation pathway.