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Arabidopsis ADC1 functions as an N δ ‐acetylornithine decarboxylase
Author(s) -
Lou YannRu,
Ahmed Sheaza,
Yan Jian,
Adio Adewale M.,
Powell Hannah M.,
Morris Paul F.,
Jander Georg
Publication year - 2020
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/jipb.12821
Subject(s) - agmatine , arabidopsis , arginine decarboxylase , putrescine , arabidopsis thaliana , arginine , biochemistry , spermine , ornithine , spermidine , biology , chemistry , enzyme , amino acid , gene , mutant
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 N δ ‐ acetylornithine to N ‐acetylputrescine. Phylogenetic analyses indicate that duplication and neofunctionalization of ADC1 and NATA1 , the enzymes that synthesize N δ ‐ acetylornithine 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 .