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J Integr Plant Biol
Arabidopsis ADC1 functions as an Nδ‐acetylornithine decarboxylase
Yann‐Ru Lou1†, Sheaza Ahmed2, Jian Yan3, Adewale M. Adio1‡, Hannah M. Powell1, Paul F. Morris2 and Georg Jander1*
1Boyce Thompson Institute for Plant Research, Ithaca, NY 14853, USA
2Department of Biological Sciences, Bowling Green State University, Bowling Green, OH 43403, USA
3Key Laboratory of Agro‐Environment in the Tropics, Ministry of Agriculture and Rural Affairs, South China Agricultural University, Guangzhou 510642, China

Present address: Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA
Present address: Bayer Crop Science, 700 Chesterfield Parkway West, Chesterfield, MO 63017, USA
*Correspondence:
Email: Georg Jander(gj32@cornell.edu)
doi: 10.1111/jipb.12821
Abstract

Polyamines are small aliphatic amines found in almost all organisms, ranging from bacteria to plants and animals. In most plants, putrescine, the metabolic precursor for longer polyamines, such as spermidine and spermine, is produced from arginine, with either agmatine or ornithine as intermediates. Here we show that Arabidopsis thaliana (Arabidopsis) arginine decarboxylase 1 (ADC1), one of the two known arginine decarboxylases in Arabidopsis, not only synthesizes agmatine from arginine, but also converts Nδacetylornithine to N‐acetylputrescine. Phylogenetic analyses indicate that duplication and neofunctionalization of ADC1 and NATA1, the enzymes that synthesize Nδacetylornithine in Arabidopsis, co‐occur in a small number of related species in the Brassicaceae. Unlike ADC2, which is localized in the chloroplasts, ADC1 is in the endoplasmic reticulum together with NATA1, an indication that these two enzymes have access to the same substrate pool. Together, these results are consistent with a model whereby NATA1 and ADC1 together provide a pathway for the synthesis of N‐acetylputrescine in Arabidopsis.

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Received: 23 March 2019      Accepted:
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