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MetaCyc Pathway: spermine and spermidine degradation II
Inferred from experiment

Pathway diagram: spermine and spermidine degradation II

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 II

Superclasses: Degradation/Utilization/AssimilationAmines and Polyamines DegradationSpermine and Spermidine Degradation

Some taxa known to possess this pathway include : Zea mays

Expected Taxonomic Range: Viridiplantae

General Background

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 response 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 then oxidize spermidine to putrescine [Moschou08]. Putrescine can be further degraded by putrescine oxidase (see putrescine degradation IV).

About This Pathway

The terminal catabolic pathway has only been found in monocots. PAOs involved in this route have been characterized in maize, barley, millet, and oat [Federico90]. The association of these PAOs with cell walls suggested they could play specific roles in apoplastic processes such as cell wall maturation and lignification, wound healing, and cell wall reinforcement during pathogen invasion. 1,3-diaminopropane formed from either spermine or spermidine, is a precursor in β-alanine biosynthesis I.

Variants: spermine and spermidine degradation I, spermine and spermidine degradation III

Created 24-Feb-2010 by Zhang P, TAIR


Cona06: Cona A, Rea G, Angelini R, Federico R, Tavladoraki P (2006). "Functions of amine oxidases in plant development and defence." Trends Plant Sci 11(2);80-8. PMID: 16406305

Federico90: Federico R, Cona A, Angelini R, Schinina ME, Giartosio A (1990). "Characterization of maize polyamine oxidase." Phytochemistry 29(8);2411-4. PMID: 1366693

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

Rea04: Rea G, de Pinto MC, Tavazza R, Biondi S, Gobbi V, Ferrante P, De Gara L, Federico R, Angelini R, Tavladoraki P (2004). "Ectopic expression of maize polyamine oxidase and pea copper amine oxidase in the cell wall of tobacco plants." Plant Physiol 134(4);1414-26. PMID: 15064377

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Binda99: Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A (1999). "A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase." Structure Fold Des 7(3);265-76. PMID: 10368296

Cervelli01: Cervelli M, Cona A, Angelini R, Polticelli F, Federico R, Mariottini P (2001). "A barley polyamine oxidase isoform with distinct structural features and subcellular localization." Eur J Biochem 268(13);3816-30. PMID: 11432750

Cona04: Cona A, Manetti F, Leone R, Corelli F, Tavladoraki P, Polticelli F, Botta M (2004). "Molecular basis for the binding of competitive inhibitors of maize polyamine oxidase." Biochemistry 43(12);3426-35. PMID: 15035614

Cona05: Cona A, Moreno S, Cenci F, Federico R, Angelini R (2005). "Cellular re-distribution of flavin-containing polyamine oxidase in differentiating root and mesocotyl of Zea mays L. seedlings." Planta 221(2);265-76. PMID: 15578214

Federico89: Federico R., Alisi C., Forlani F. "Properties of polyamines oxidase from the cell wall of maize seedlings." Phytochemistry (1989) 28 : 45-46.

Galston90: Galston AW, Sawhney RK (1990). "Polyamines in plant physiology." Plant Physiol 94(2);406-10. PMID: 11537482

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

McIntire93: McIntire W.S., Hartman C. "Copper-contaiing amine oxidases." Principle and application of quinoproteins (1993) Davisonm V.L., ed., pp.97-171. Marcel Dekker Inc, NY.

Sebela01: Sebela M, Radova A, Angelini R, Tavladoraki P, Frebort , Pec P (2001). "FAD-containing polyamine oxidases: a timely challenge for researchers in biochemistry and physiology of plants." Plant Sci 160(2);197-207. PMID: 11164591

Tavladoraki98: Tavladoraki P, Schinina ME, Cecconi F, Di Agostino S, Manera F, Rea G, Mariottini P, Federico R, Angelini R (1998). "Maize polyamine oxidase: primary structure from protein and cDNA sequencing." FEBS Lett 426(1);62-6. PMID: 9598979

Vianello93: Vianello F, Di Paolo ML, Stevanato R, Gasparini R, Rigo A (1993). "Purification and characterization of amine oxidase from soybean seedlings." Arch Biochem Biophys 307(1);35-9. PMID: 8239662

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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