Polygalacturonase

![Image of polygalacturonase from Fusarium moniliforme (1HG8) showing active site in magenta[5]](/uploads/202502/03/PG_with_active_site2724.png)
![The mechanism of polygalacturonase: hydrolysis of polygalacturonan.[11]](/uploads/202502/03/Polygalacturonase_mechanism2724.png)
![Polygalacturonase inhibitor protein found in Phaseolus vulgaris (1OGQ). Residues that interact with PG active site are highlighted in blue.[24]](/uploads/202502/03/PGIP_competitive_inhibition2724.png)
Polygalacturonase (EC3.2.1.15), also known as pectin depolymerase, PG, pectolase, pectin hydrolase, and poly-alpha-1,4-galacturonide glycanohydrolase, is an enzyme that hydrolyzes the alpha-1,4 glycosidic bonds between galacturonic acid residues. Polygalacturonan, whose major component is galacturonic acid, is a significant carbohydrate component of the pectin network that comprises plant cell walls. Therefore, the activity of the endogenous plant PGs works to soften and sweeten fruit during the ripening process. Similarly, phytopathogens use PGs as a means to weaken the pectin network, so that digestive enzymes can be excreted into the plant host to acquire nutrients.