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Updated: Jan 15, 2026

Enzymatic Cascade Reactions for the Synthesis of Chiral Amino Alcohols from L-lysine
Published on: February 16, 2018
New polyamine oxidases from Ogataea parapolymorpha DL-1: expanding view on non-conventional yeast polyamine
Diana I Golovina1,2,3, Egor P Sergeev1,2, Ivan I Lentin2
1Laboratory of Molecular Engineering, Federal Research Centre "Fundamentals of Biotechnology" RAS, Moscow, 119071, Russia.
Abstract:
Polyamines are ubiquitous and essential for cellular physiology, yet their metabolic pathways and functions remain only partially understood. Polyamine oxidases (PAO) are key to elucidating their physiological roles. In the methylotrophic yeast Ogataea parapolymorpha, we identified three putative PAO-encoding genes. Biochemical characterization showed that two of them function as PAOs, whereas the third has unknown substrate specificity. In contrast to previously studied yeasts, including Saccharomyces cerevisiae, which contain only a single PAO, O. parapolymorpha harbors multiple and functionally distinct PAOs. These findings highlight an unexpected diversification of polyamine catabolism in yeast and suggest previously unrecognized roles of PAOs in cellular physiology.

