AbstractPectin methylesterases (PMEs) modify homogalacturonan’s chemistry and thereby play a key role in regulating primary cell wall mechanical properties. How PME activity can fine-tune pectin structure in the growing plant has remained elusive, in part due to the lack of available biochemically-characterized enzymes to empirically test functional properties. Here we report on AtPME2, which we found to be highly expressed during lateral root emergence as well as root and hypocotyl elongation. Production of mature active enzyme in Pichia pastoris allowed its biochemical characterization. We show that AtPME2 can switch from full processivity (at pH 8), creating large blocks of unmethylated galacturonic acid, to low processivity (at pH 5) and relate these observations to the differences in electrostatic potential of the protein. We also produced a generic plant PME antiserum suitable for detecting recombinant and native enzyme independent of species source. In the context of acidified apoplast, we showed using reverse genetics that low-processive demethylesterification by AtPME2 can loosen the cell wall, with consequent increase in cell elongation and etiolated hypocotyl length. Our study brings insights into how the pH-dependent regulation by PME activity could affect pectin structure and associated cell wall mechanical properties in expansion.