Abstract
In plants, putrescine is synthesized directly from the decarboxylation of ornithine and/or by the alternative arginine decarboxylase pathway. The prevalence of one or the other depends on the tissue and stress conditions. In both amino acid decarboxylation reactions, the corresponding enzymes use pyridoxal phosphate (PLP) as co-factor. PLP combines with the α-amino acid to form a Schiff base, which acts as substrate in the carboxyl group removal and CO2 formation. We describe the methodology employed for the determination of ODC and ADC activities in plant tissues by detecting the release of (C14) CO2 using (C14) labelled substrates (ornithine or arginine).
References
Pegg AE, Casero RA Jr (2011) Current status of the polyamine research field. Methods Mol Biol 720:3–35
Fuell C, Elliott KA, Hanfrey CC, Franceschetti M, Michael AJ (2010) Polyamine biosynthetic diversity in plants and algae. Plant Physiol Biochem 48:513–520
Tiburcio AF, Altabella T, Bitrián M, Alcázar R (2014) The roles of polyamines during the lifespan of plants: from development to stress. Planta 240:1–18
Hanfrey C, Sommer S, Mayer MJ, Burtin D, Michael AJ (2001) Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity. Plant J 27:551–560
Carbonell J, Blázquez MA (2009) Regulatory mechanisms of polyamine biosynthesis in plants. Genes Genomics 31:107–118
Alcázar R, Altabella T, Marco F, Bortolotti C, Reymond M, Koncz C, Carrasco P, Tiburcio AF (2010) Polyamines: molecules with regulatory functions in plant abiotic stress tolerance. Planta 231:1237–1249
Bitrián M, Zarza X, Altabella T, Tiburcio AF, Alcázar R (2012) Polyamines under abiotic stress: metabolic crossroads and hormonal crosstalks in plants. Meta 2:516–528
Slocum RD (1991) Tissue and subcellular localization of polyamines and enzymes of polyamine metabolism. In: Slocum RD, Flores HE (eds) Biochemistry and Physiology of Polyamines in Plants. CRC Press, Inc., Boca Raton, FL, pp 93–103
Bortolotti C, Cordeiro A, Alcázar R, Borrell A, Culiañez-Macià FA, Tiburcio AF, Altabella T (2004) Localization of arginine decarboxylase in tobacco plants. Physiol Plant 120:84–92
Borrell A, Culiañez-Macia FA, Altabella T, Besford RT, Flores D, Tiburcio AF (1995) Arginine decarboxylase is localized in chloroplasts. Plant Physiol 109:771–776
Lee J, Michael AJ, Martynowski D, Goldsmith EJ, Phillips MA (2007) Phylogenetic diversity and the structural basis of substrate specificity in the beta/alpha-barrel fold basic amino acid decarboxylases. J Biol Chem 282:27115–27125
Jordan F, Patel H (2013) Catalysis in enzymatic Decarboxylations: comparison of selected cofactor-dependent and cofactor-independent examples. ACS Catal 3:1601–1617
Metcalf BW, Bey P, Danzin C, Jung MJ, Casara P, Ververt JP (1978) Catalytic irreversible inhibition of mammalian ornithine decarboxylase (EC 4.1.1.17) by substrate and product analogs. J Am Chem Soc 100:2551–2553
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 242:69–74
McCann PP, Pegg AE, Sjodersma A (eds) (1987) Inhibition of polyamine metabolism. Academic Press, Inc., San Diego, CA
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer Science+Business Media LLC
About this protocol
Cite this protocol
Alcázar, R., Tiburcio, A.F. (2018). Determination of Arginine and Ornithine Decarboxylase Activities in Plants. In: Alcázar, R., Tiburcio, A. (eds) Polyamines. Methods in Molecular Biology, vol 1694. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7398-9_11
Download citation
DOI: https://doi.org/10.1007/978-1-4939-7398-9_11
Published:
Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-7397-2
Online ISBN: 978-1-4939-7398-9
eBook Packages: Springer Protocols