This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Synonyms: polyamine degradation III
|Superclasses:||Degradation/Utilization/Assimilation → Amines and Polyamines Degradation → Spermine and Spermidine Degradation|
Some taxa known to possess this pathway include : Arabidopsis thaliana col
Expected Taxonomic Range: Viridiplantae
Polyamines are widespread in both prokaryotes and eukaryotes, with spermine, spermidine, and putrescine being the most abundant ones. Polyamines play important roles in cell growth and differentiation, in responses to abiotic stress such as potassium deficiency, osmotic shock, drought and salt stress, and in plant-pathogen interactions.
In plants, polyamines can be degraded via two routes, the so-called terminal catabolic pathway and the back-conversion pathway. In both cases, H2O2 was produced as a by-product. In the terminal catabolic pathway, plant apoplastic polyamine oxidases (PAOs) oxidize spermine and spermidine to 1,3-diaminopropane, H2O2 and the corresponding aminoaldehydes. These compounds cannot be converted directly to other polyamines. Therefore, this route is referred to as the terminal catabolic pathway [Cona06]. In the back-conversion pathway, polyamines are interconverted. The peroxisome-localized PAOs oxidize spermine to spermidine, and consequently oxidize spermidine to putrescine [Moschou08]. Putrescine can be further degraded by putrescine oxidase (see putrescine degradation IV).
About This Pathway
In the back-conversion pathway, unlike in mammals where acetyl-derivatives of spermine and spemidine are the best substrates of PAOs, the plant PAOs characterized so far act much better on spermine and/or spermidine than their acetyl-derivatives [Moschou08, KamadaNobusada08, Tavladoraki06].
KamadaNobusada08: Kamada-Nobusada T, Hayashi M, Fukazawa M, Sakakibara H, Nishimura M (2008). "A putative peroxisomal polyamine oxidase, AtPAO4, is involved in polyamine catabolism in Arabidopsis thaliana." Plant Cell Physiol 49(9);1272-82. PMID: 18703589
Moschou08: Moschou PN, Sanmartin M, Andriopoulou AH, Rojo E, Sanchez-Serrano JJ, Roubelakis-Angelakis KA (2008). "Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis." Plant Physiol 147(4);1845-57. PMID: 18583528
Tavladoraki06: Tavladoraki P, Rossi MN, Saccuti G, Perez-Amador MA, Polticelli F, Angelini R, Federico R (2006). "Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion." Plant Physiol 141(4);1519-32. PMID: 16778015
Bianchi06: Bianchi M, Polticelli F, Ascenzi P, Botta M, Federico R, Mariottini P, Cona A (2006). "Inhibition of polyamine and spermine oxidases by polyamine analogues." FEBS J 273(6);1115-23. PMID: 16519678
Vujcic02: Vujcic S, Diegelman P, Bacchi CJ, Kramer DL, Porter CW (2002). "Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin." Biochem J 367(Pt 3);665-75. PMID: 12141946
Wang01e: Wang Y, Devereux W, Woster PM, Stewart TM, Hacker A, Casero RA (2001). "Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure." Cancer Res 61(14);5370-3. PMID: 11454677
Wang03e: Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA (2003). "Properties of purified recombinant human polyamine oxidase, PAOh1/SMO." Biochem Biophys Res Commun 304(4);605-11. PMID: 12727196
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493