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Title

Inhibition of endogenous urease activity by NBPT application reveals differential N metabolism responses to ammonium or nitrate nutrition in pea plants: A physiological study

AuthorsCruchaga, Saioa; Lasa, Berta; Jauregui, Iván; González-Murua, Carmen; Aparicio-Tejo, Pedro María ; Ariz, Idoia
KeywordsNBPT
Arginine catabolism
Ammonium nutrition
Protein turnover
Urea metabolism
Urease inhibitor
Urease
Issue Date2013
PublisherKluwer Academic Publishers
CitationPlant and Soil 373(1-2): 813-827 (2013)
AbstractBackground and aims: Urea is the predominant form of N applied as fertilizer to crops, but it is also a significant N metabolite of plants themselves. As such, an understanding of urea metabolism in plants may contribute significantly to subsequent N fertilizer management. It currently appears that arginase is the only plant enzyme that can generate urea in vivo. The aim of this work was, therefore, to gain a more in-depth understanding of the significance of the inhibition of endogenous urease activity and its role in N metabolism depending on the N source supplied. Methods: Pea (Pisum sativum cv. Snap-pea) plants were grown with either ammonium or nitrate as the sole N source in the presence or absence of the urease inhibitor NBPT. Results: When supplied, NBPT is absorbed by plants and translocated from the roots to the leaves, where it reduces endogenous urease activity. Different N metabolic responses in terms of N-assimilatory enzymes and N-containing compounds indicate a different degree of arginine catabolism activation in ammonium- and nitrate-fed plants. Conclusions: The arginine catabolism is more highly activated in ammonium-fed plants than in nitrate-fed plants, probably due to the higher turnover of substrates by enzymes playing a key role in N recycling and remobilization during catabolism and in early flowering and senescence processes, usually observed under ammonium nutrition. © 2013 Springer Science+Business Media Dordrecht.
URIhttp://hdl.handle.net/10261/97598
DOI10.1007/s11104-013-1830-x
Identifiersdoi: 10.1007/s11104-013-1830-x
issn: 0032-079X
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