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Pectin lyase

About: Pectin lyase is a research topic. Over the lifetime, 572 publications have been published within this topic receiving 14993 citations. The topic is also known as: polymethylgalacturonic transeliminase & PMGL.

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Journal ArticleDOI
TL;DR: The regulation of pel genes requires several regulatory systems, including the KdgR repressor, which mediates the induction of all the pectinolysis genes in the presence of pectin catabolites.
Abstract: ▪ Abstract Erwinia chrysanthemi is an enterobacterium that causes various plant diseases. Its pathogenicity results from the secretion of pectinolytic enzymes responsible for the disorganization of the plant cell wall. The E. chrysanthemi strain 3937 produces two pectin methylesterases, at least seven pectate lyases, a polygalacturonase, and a pectin lyase. The extracellular degradation of the pectin leads to the formation of oligogalacturonides that are catabolized through an intracellular pathway. The pectinase genes are expressed from independent cistrons, and their transcription is favored by environmental conditions such as presence of pectin and plant extracts, stationary growth phase, low temperature, oxygen or iron limitation, and so on. Moreover, transcription of the pectin lyase gene responds to DNA-damaging agents. The differential expressions of individual pectinase genes presumably reflect their role during plant infection. The regulation of pel genes requires several regulatory systems, incl...

408 citations

Journal ArticleDOI
01 Aug 1987
TL;DR: A review of the sources, regulation, purification, and properties of these polysaccharide eliminases can be found in this paper, with a focus on enzymes of microbial origin.
Abstract: Polysaccharide lyases (or eliminases) are a class of enzymes (EC 4.2.2.-) that act to cleave certain activated glycosidic linkages present in acidic polysaccharides. These enzymes act through an eliminase mechanism, rather than through hydrolysis, resulting in unsaturated oligosaccharide products. Acidic polysaccharides are ubiquitous and so are the lyases that degrade them. This review article examines lyases that act on acidic polysaccharides of plant, animal, and microbial origin. These lyases are predominantly of microbial origin and come from a wide variety of both pathogenic and nonpathogenic bacteria and fungi. The lyases discussed include alginate lyase (EC, pectin lyase (EC, pectate lyase (EC, oligogalacturonide lyase (EC, exopolygalacturonate lyase (EC, chondroitin lyases (EC and EC, hyaluronate lyase (EC, heparin lyase (EC, heparan lyase (EC, and other unclassified lyases. This review examines the sources, regulation, purification, and properties of these polysaccharide lyases.

294 citations

Journal ArticleDOI
TL;DR: Models of the apple pectin molecules presented show that the neutral sugars are present as side chains, arranged in blocks (in so-called ‘hairy regions’) and the galacturonate residues in the hairy regions are esterified with methanol.

228 citations

Journal ArticleDOI
TL;DR: This review tries to fill the gap by providing all relevant information exclusively for pectin lyase by covering structural aspects, substrate specificity, molecular biology, biotechnological applications and future prospects of pECTin lyases.

215 citations

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