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Last update 08 May 2025

PAOX

Last update 08 May 2025

Basic Info

Synonyms

PAO, PAOX, Peroxisomal N(1)-acetyl-spermine/spermidine oxidase

+ [1]

Introduction

Flavoenzyme which catalyzes the oxidation of N(1)-acetylspermine to spermidine and is thus involved in the polyamine back-conversion (PubMed:12477380). Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs (PubMed:12477380).

Drugs associated with PAOX

MDL-72527

Target

PAOX x SMOX

Mechanism

PAOX inhibitors [+2]

Active Org.

Johns Hopkins University School of Advanced International [+3]

Originator Org.

Aventis SA

Active Indication

Diabetic Retinopathy [+1]

Inactive Indication

Neoplasms

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with PAOX

100 Translational Medicine associated with PAOX

0 Patents (Medical) associated with PAOX

623

Literatures (Medical) associated with PAOX

01 Jul 2025·Plant Science

ERD15 promotes peach and tomato ripening by activating polyamine catabolism

Article

Author: Tang, Guangcai ; Jia, Zhiqi ; Liu, Keke ; Cheng, Xin ; Fan, Bingli ; Zhang, Shiwen

Polyamine oxidase (PAO) is a key enzyme in polyamine (PA) catabolism and plays a vital role during fruit ripening. However, regulatory mechanisms that control PAO expression during maturation remain unclear. This study identifies the transcription factor PpeERD15 through yeast one-hybrid (Y1H) screening with the PpePAO1 promoter. ERD15 (early response to dehydration 15), a member of the early response to dehydration protein family, is known for its role in abiotic stress responses, but its function in fruit ripening remains largely unexplored. Subcellular localization analysis demonstrated that PpeERD15 was localized in both the nucleus and cytoplasm. Y1H and LUC assays confirmed that PpeERD15 directly binds the PpePAO1 promoter. Transient silencing of PpEDR15 in peach fruit downregulated PpePAO1 expression, promoted PA accumulation, inhibited ethylene production, increased fruit firmness, and delayed fruit ripening. Conversely, overexpression of PpeEDR15 upregulated PpePAO1, decreased PA content, promoted ethylene production, reduced fruit firmness, and accelerated fruit ripening. The role of homologous gene of ERD15 was also validated in tomato. This study discovered that PpeEDR15 regulates fruit ripening by promoting PA catabolism via PpePAO1 expression.

01 May 2025·Journal of Plant Physiology

Barley root tip peroxidases convert DAF-FM and DAR-4M to an NO-independent fluorescent product using H2O2 derived from polyamine catabolism by polyamine oxidases

Article

Author: Valentovičová, Katarína ; Zelinová, Veronika ; Liptáková, Ľubica ; Demecsová, Loriana ; Tamás, Ladislav

The aim of our study was to investigate the possible involvement of barley root tip peroxidases and polyamine oxidases in the conversion of DAF-FM or DAR-4M into an NO-independent fluorescent product after the exogenous application of polyamines. Application of spermidine or spermine into the incubation medium increased H₂O₂ production by root tip segments in a dose-dependent manner. This spermidine- or spermine-induced increase in H₂O₂ production was accompanied by intensified fluorescence of both DAF-FM and DAR-4M in a polyamine dose-dependent manner, similarly to exogenously added H₂O₂. On the contrary, exogenous putrescine neither evoked H₂O₂ production nor increased DAF-FM or DAR-4M fluorescence. Application of guazatine, a polyamine oxidase inhibitor, into the incubation medium inhibited both H₂O₂ production and DAF-FM or DAR-4M fluorescence. Spermidine- or spermine-induced DAF-FM or DAR-4M fluorescence decreased with an increasing amount of catalase or guaiacol, a competitive substrate for peroxidase, in the incubation medium. Exogenous application of indole-3-acetic acid, a well-known activator of NO generation in roots, but not of H₂O₂, spermidine or spermine, induces NO accumulation in the root tips. Exogenous application of spermidine or spermine to plant tissues with high polyamine oxidase and peroxidase activity, as are the barley root tips, generates an NO-independent fluorescence signal from either DAF-FM or DAR-4M, giving a false positive signal for NO emission.

01 Mar 2025·Plant Physiology and Biochemistry

The basic helix-loop-helix transcription factor PpeUNE12 regulates peach ripening by promoting polyamine catabolism and anthocyanin synthesis

Article

Author: Tan, Bin ; Wang, Xiaobei ; Zhang, Shiwen ; Ye, Xia ; Chen, Yang ; Guo, Luyue ; Liu, Shihao ; Zhang, Langlang ; Cheng, Jun ; Zheng, Xianbo ; Qiao, Gaozheng ; Tang, Guangcai ; Zhang, Haipeng ; Jiang, Yabo ; Wang, Wei ; Feng, Jiancan

The basic helix-loop-helix (bHLH) transcription factors (TFs) play important roles in various plant developmental and biological processes. However, the precise mechanisms by which bHLH TFs regulate fruit ripening warrant further investigation. Polyamine oxidase (PAO) is crucial for polyamine (PA) catabolism and plays crucial roles in fruit ripening. However, the regulatory mechanism of PAO gene expression during fruit ripening remains largely unexplored. In this study, we identified a peach bHLH TF, PpeUNE12, which directly binds to and activates the promoter of PpePAO1. Silencing PpeUNE12 substantially increased PA accumulation and delayed peach fruit ripening, while overexpressing PpeUNE12 decreased PA accumulation and accelerated peach fruit ripening. Additionally, anthocyanin content decreased in PpeUNE12-silenced fruits but increased in PpeUNE12-overexpressing peach fruits compared to the control. RNA-seq and RT-qPCR analyses revealed that the majority of genes involved in anthocyanin biosynthesis, including PpeF3H, PpeCHS, PpeDFR, PpeUFGT and PpeMYB10.1 exhibited down-regulation in fruits with silenced PpeUNE12, while these genes were up-regulated in fruits overexpressing PpeUNE12. Although PpeUNE12 exhibited no direct binding to the promoters of PpeUFGT and PpeMYB10.1, it substantially activated their activity. This investigation is the first to provide evidence that bHLH regulates fruit maturation via promoting both PA catabolism and anthocyanin synthesis. It reveals a novel mechanism of bHLH in regulating fruit ripening and enhances our comprehension of the regulatory mechanism of PA catabolism and anthocyanin synthesis during fruit maturation.

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