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: putrescine biosynthesis in plants, ODC and ADC putrescine biosynthesis
|Superclasses:||Biosynthesis → Amines and Polyamines Biosynthesis → Putrescine Biosynthesis|
Some taxa known to possess this pathway include : Arabidopsis thaliana col , Avena sativa , Brassica juncea , Capsicum annuum , Datura stramonium , Dianthus caryophyllus , Glycine max , Malus domestica , Nicotiana tabacum , Oryza sativa , Pisum sativum , Solanum lycopersicum , Theobroma cacao
Expected Taxonomic Range: Viridiplantae
This pathway produces the polyamine putrescine. This metabolite like other polyamines is cationic and may be involved in interactions with proteins, DNA and RNA molecules. It particpates in the developmental and physiological functions as well as in aiding regulatory processes. In plants polyamines are also known to be stress molecules [Eller06]. The biosynthesis of putrescine in plants occurs via either the ornithine decarboxylase or arginine decarboxylase route, sometimes by both, unlike putrescine biosynthesis in microbes, where either one of these routes are exclusively followed. The pathway depicted here is one where the two routes are connected in plants. In tobacco, putrescine is a precursor of nicotine which is a powerful anti-herbivore toxin. Nicotine is induced by wounding or by elicitation by methyljasmonate treatment. The enzymes of this pathway are recruited during stress and characterized by high transcript accumulation during the stress periods [Chen04].
Polyamines also accumulate in plant organs as conjugates of hydrocinnamate, formed by an amide bond. The polyamines are stored in organs in any one predominant form of the conjugated putrescine [Michael96].
Alabadi98: Alabadi D, Carbonell J (1998). "Expression of ornithine decarboxylase is transiently increased by pollination, 2,4-dichlorophenoxyacetic acid, and gibberellic acid in tomato ovaries." Plant Physiol 118(1);323-8. PMID: 9733552
Almrud00: Almrud JJ, Oliveira MA, Kern AD, Grishin NV, Phillips MA, Hackert ML (2000). "Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding." J Mol Biol 295(1);7-16. PMID: 10623504
Andrell09: Andrell J, Hicks MG, Palmer T, Carpenter EP, Iwata S, Maher MJ (2009). "Crystal structure of the acid-induced arginine decarboxylase from Escherichia coli: reversible decamer assembly controls enzyme activity." Biochemistry 48(18);3915-27. PMID: 19298070
Applebaum75: Applebaum D, Sabo DL, Fischer EH, Morris DR (1975). "Biodegradative ornithine decarboxylase of Escherichia coli. Purification, properties, and pyridoxal 5'-phosphate binding site." Biochemistry 1975;14(16);3675-81. PMID: 240388
Balasundaram94: Balasundaram D, Xie QW, Tabor CW, Tabor H (1994). "The presence of an active S-adenosylmethionine decarboxylase gene increases the growth defect observed in Saccharomyces cerevisiae mutants unable to synthesize putrescine, spermidine, and spermine." J Bacteriol 176(20);6407-9. PMID: 7929015
Bell90: Bell E, Malmberg RL (1990). "Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing." Mol Gen Genet 224(3);431-6. PMID: 2266946
Bitonti87: Bitonti AJ, Casara PJ, McCann PP, Bey P (1987). "Catalytic irreversible inhibition of bacterial and plant arginine decarboxylase activities by novel substrate and product analogues." Biochem J 1987;242(1);69-74. PMID: 3297044
Blethen68: Blethen SL, Boeker EA, Snell EE (1968). "Argenine decarboxylase from Escherichia coli. I. Purification and specificity for substrates and coenzyme." J Biol Chem 1968;243(8);1671-7. PMID: 4870599
BSUB93: "Bacillus subtilis and Other Gram-Positive Bacteria: Biochemistry, Physiology, and Molecular Genetics." (1993). Editors: Sonenshein, A.L., Hoch, J.A., Losick, R. American Society For Microbiology, Washington, DC.
Carvajal04: Carvajal N, Orellana MS, Salas M, Enriquez P, Alarcon R, Uribe E, Lopez V (2004). "Kinetic studies and site-directed mutagenesis of Escherichia coli agmatinase. A role for Glu274 in binding and correct positioning of the substrate guanidinium group." Arch Biochem Biophys 430(2);185-90. PMID: 15369817
Forouhar10: Forouhar F, Lew S, Seetharaman J, Xiao R, Acton TB, Montelione GT, Tong L (2010). "Structures of bacterial biosynthetic arginine decarboxylases." Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 12);1562-6. PMID: 21139196
Gardan97: Gardan R, Rapoport G, Debarbouille M (1997). "Role of the transcriptional activator RocR in the arginine-degradation pathway of Bacillus subtilis." Mol Microbiol 1997;24(4);825-37. PMID: 9194709
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