The organism was originally isolated because of its ability to digest pectin and pectate.

Pectinesterase catalyses the de-esterification of pectin into pectate and methanol.

The putative catalytic residues are in a similar location to those of the active site and substrate-binding cleft of pectate lyase.

It has been suggested that the pollen expression of pectate lyase genes might relate to a requirement for pectin degradation during pollen tube growth.

The first beta-helix was observed in the enzyme pectate lyase, which contains a seven-turn helix that reaches 34 Å (3.4 nm) long.

Polygalacturonase (PG) (pectinase) catalyzes the random hydrolysis of 1,4-alpha-D-galactosiduronic linkages in pectate and other galacturonans.

SP Lei et al., Characterization of the Erwinia carotovora pelB gene and its product pectate lyase.

The first being a contribution to the stiffening of the cell wall by producing blocks of unesterified carboxyl groups that can interact with calcium ions forming a pectate gel.

Similarly, the second most abundant component of cell walls (pectin) is the assumed target of nematode-encoded pectate lyase and exo-polygalacturonase, both functions also postulated to have been acquired by HGT.

Erwinia carotovora is a plant pathogen that causes soft rot in a number of crops such as potatoes and carrots by using N-hexanoyl-l-HSL (C6-HSL) quorom sensing to evade the plant's defense systems and coordinate its production of pectate lyase during the infection process.