The N-terminal pro-peptides of pectinesterase are variable in size and sequence and show a low level of amino acid identity.
12.
Recently, particular attention has been devoted to molecular studies of pectinesterase leading to the characterisation of several related isoforms in various higher plant species.
13.
Homogalacturonan is highly methyl-esterified when exported into cell walls and is subsequently de-esterified by the action of pectinesterase and other pectic enzymes.
14.
Isoforms of pectinesterase differ in various biochemical parameters such as relative molecular mass, isoelectric point, optimum pH, substrate affinity, ion-requirement and location.
15.
Pectinesterase catalyses the de-esterification of methyl-esterified D-galactosiduronic acid units in pectic compounds yielding substrates for depolymerising enzymes, particularly acidic pectins and methanol.
16.
Pectinesterase is thought to be secreted to the apoplasm with highly methylated pectin although at some point along this secretory pathway the N-terminal pro-peptide is cleaved off.
17.
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.
18.
Pectinesterase isoforms are encoded by a family of genes, some of which are constitutively expressed throughout the plant, whereas others are differentially expressed in specific tissues and at different developmental stages.
19.
"' Pectinesterase "'( PE ) ( ) is a ubiquitous cell-wall-associated enzyme that presents several isoforms that facilitate plant cell wall modification and subsequent breakdown.
20.
During fruit ripening, pectin is broken down by the enzymes pectinase and pectinesterase, in which process the fruit becomes softer as the middle lamellae break down and cells become separated from each other.
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