C. Hanfrey et al., Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase andthe mechanism of arginine decarboxylase activity, PLANT J, 27(6), 2001, pp. 551-560
Unlike other eukaryotes, which can synthesize polyamines only from ornithin
e, plants possess an additional pathway from arginine. Occasionally non-enz
ymatic decarboxylation of ornithine could be detected in Arabidopsis extrac
ts; however, we could not detect ornithine decarboxylase (ODC; EC 4. 1.1.17
) enzymatic activity or any activity inhibitory to the ODC assay. There are
no intact or degraded ODC sequences in the Arabidopsis genome and no ODC e
xpressed sequence tags. Arabidopsis is therefore the only plant and one of
only two eukaryotic organisms (the other being the protozoan Trypanosome cr
uzi) that have been demonstrated to lack ODC activity. As ODC is a key enzy
me in polyamine biosynthesis, Arabidopsis is reliant on the additional argi
nine decarboxylase (ADC; EC 4.1.1.9) pathway, found only in plants and some
bacteria, to synthesize putrescine. By using site-directed mutants of the
Arabidopsis ADC1 and heterologous expression in yeast, we show that ADC, li
ke ODC, is a head-to-tail homodimer with two active sites acting in trans a
cross the interface of the dimer. Amino acids K136 and C524 of Arabidopsis
ADC1 are essential for activity and participate in separate active sites. M
aximal activity of Arabidopsis ADC1 in yeast requires the presence of gener
al protease genes, and it is likely that dimer formation precedes proteolyt
ic processing of the ADC pre-protein monomer.