Active Site

Pectinesterase, Asp active site (IPR033131)

Short name: Pectinesterase_Asp_AS

Description

Pectinesterase (EC:3.1.1.11) (pectin methylesterase) catalyses the hydrolysis of pectin into pectate and methanol. In plants, it plays an important role in cell wall metabolism during fruit ripening, cell wall extension and during pollen germination. In plant bacterial pathogens such as Erwinia carotovora and in fungal pathogens such as Aspergillus niger, pectinesterase is involved in maceration and soft-rotting of plant tissue. Plant pectinesterases are regulated by pectinesterase inhibitors, which are ineffective against microbial enzymes [PMID: 15722470].

Prokaryotic and eukaryotic pectinesterases share a few regions of sequence similarity [PMID: 3371355, PMID: 2837615, PMID: 1303747]. The crystal structure of pectinesterase from Erwinia chrysanthemi revealed a beta-helix structure similar to that found in pectinolytic enzymes, though it is different from most structures of esterases [PMID: 11162105]. The putative catalytic residues are in a similar location to those of the active site and substrate-binding cleft of pectate lyase.

This entry represents a conserved octapeptide located in the central part of these enzymes containing an active site aspartate [PMID: 11964128].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns