4.2.2.10: pectin lyase
This is an abbreviated version!
For detailed information about pectin lyase, go to the full flat file.
Word Map on EC 4.2.2.10
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4.2.2.10
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cellulase
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xylanase
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aspergillus
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polysaccharide
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polygalacturonase
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juice
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niger
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pectinolytic
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amylase
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pulp
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peel
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pectate
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penicillium
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citrus
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erwinia
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saccharification
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hemicellulase
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polygalacturonic
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methylesterase
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lyases
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xylan
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bran
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endo-polygalacturonase
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rhamnogalacturonan
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wall-degrading
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glucanase
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enzyme-assisted
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cellulolytic
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carotovora
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pectinesterase
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cellobiase
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tannase
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homogalacturonans
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chrysanthemi
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cmcase
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box-behnken
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3.2.1.15
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nutrition
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synthesis
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fibrobacter
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pomace
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scouring
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industry
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mannanase
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oligogalacturonides
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bagasse
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flavefaciens
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agriculture
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d-galacturonic
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degumming
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food industry
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carbohydrases
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agro-industrial
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ruminicola
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cazymes
- 4.2.2.10
- cellulase
- xylanase
- aspergillus
- polysaccharide
- polygalacturonase
- juice
- niger
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pectinolytic
- amylase
- pulp
- peel
- pectate
- penicillium
- citrus
- erwinia
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saccharification
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hemicellulase
- polygalacturonic
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methylesterase
- lyases
- xylan
- bran
- endo-polygalacturonase
- rhamnogalacturonan
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wall-degrading
- glucanase
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enzyme-assisted
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cellulolytic
- carotovora
- pectinesterase
- cellobiase
- tannase
- homogalacturonans
- chrysanthemi
- cmcase
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box-behnken
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3.2.1.15
- nutrition
- synthesis
- fibrobacter
- pomace
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scouring
- industry
- mannanase
- oligogalacturonides
- bagasse
- flavefaciens
- agriculture
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d-galacturonic
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degumming
- food industry
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carbohydrases
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agro-industrial
- ruminicola
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cazymes
Reaction
Synonyms
commercial pectic enzyme, CPE, enda-PL, endo PNL, endo-pectin lyase, family 1 pectin lyase A, Forylase PA, lyase, pectin, Macerin G 10X, pectin lyase, pectin lyase 1, pectin lyase A, pectin methyltranseliminase, pectin transeliminase, pectinase, pectinliase, pectinlyase, pectolyase Y23, Pel1, PGL, phytolyase, PL, PL1A, Pla, PLB, PLD, plg1, plg2, PLI, PLII, PNL, pnl-zj5a, Pnl1, Pnl2, PnlH, poly(methoxygalacturonide) lyase, polymethylgalacturonic transeliminase, Rohapect PTE, Ultrazym-100, Ultrazym-20, Ultrazym-40
ECTree
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Substrates Products
Substrates Products on EC 4.2.2.10 - pectin lyase
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REACTION DIAGRAM
partially methyl-esterified pectin
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prepared from citrus and Aspergillus sp.
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citrus pectin
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citrus pectin, with 72% of methylation, best substrate
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citrus pectin
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the activity increases with the degree of esterification, best substrate shows a degree of esterification of 85%
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under optimum conditions, the highest pectin lyase activity in the medium is with orange waste as carbon source
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orange waste
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under optimum conditions, the highest pectin lyase activity in the medium is with orange waste as carbon source
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pectin
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best substrate from citrus, acceptable substrate from apple
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pectin
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citrus pectin, depolymerization of pectin by elimination of the 6-methyl-DELTA4,5-D-galacturonate residues
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pectin
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among pectins with different degree of substitution, the enzyme preferably hydrolyzes highly etherized substrate. The enzyme has practically no effect on completely demethylated substrate
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pectin
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among pectins with different degree of substitution, the enzyme preferably hydrolyzes highly etherized substrate. The enzyme has practically no effect on completely demethylated substrate
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pectin
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citrus pectin, depolymerization of pectin by elimination of the 6-methyl-DELTA4,5-D-galacturonate residues
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pectin
DELTA4,5-unsaturated oligosaccharides
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citrus pectin, activity increases with increasing degree of methylation of the substrate
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pectin
DELTA4,5-unsaturated oligosaccharides
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citrus pectin, activity increases with increasing degree of methylation of the substrate
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44% of the activity with citrus pectin
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pectin with 70% methyl esterification
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44% of the activity with citrus pectin
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118% of the activity with citrus pectin
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pectin with 85% methyl esterification
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118% of the activity with citrus pectin
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the purified enzyme shows efficacy in retting of Crotalaria juncea fibers
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additional information
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the purified enzyme shows efficacy in retting of Crotalaria juncea fibers
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additional information
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the enzyme is able to macerate parenchymateous tissues, in which onion tissue is the most susceptible to be attacked by the enzyme
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additional information
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no activity with polygalacturonic acid, acts antagonistic to pectinesterase, EC 3.1.1.11
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additional information
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Pel1 enhances the reconstituted expansin-induced extension of the apical (elongating) segments of cucumber hypocotyls
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additional information
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no activity with polygalacturonic acid, acts antagonistic to pectinesterase, EC 3.1.1.11
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additional information
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pH driven conformational changes of the enzyme, wild-type and mutants
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additional information
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pH driven conformational changes of the enzyme, wild-type and mutants
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additional information
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substrate specificity, activity increases with increasing length of the substrate up to polymerization degree of 8 monomers, enzyme is very specific for fully methyl-esterified oligogalacturonides, removal of the methyl-ester or changing the type of ester, e.g. ethyl esterification, or transamidation result in almost complete loss of activity, enzyme is capable of cleaving the bond between a methyl-esterified and a non-esterified galacturonic acid residue, where the newly formed DELTA4,5 unsaturated non-reducing end residue always contains a methyl-ester, product determination by mass spectrometry
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additional information
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substrate specificity, activity increases with increasing length of the substrate up to polymerization degree of 8 monomers, enzyme is very specific for fully methyl-esterified oligogalacturonides, removal of the methyl-ester or changing the type of ester, e.g. ethyl esterification, or transamidation result in almost complete loss of activity, enzyme is capable of cleaving the bond between a methyl-esterified and a non-esterified galacturonic acid residue, where the newly formed DELTA4,5 unsaturated non-reducing end residue always contains a methyl-ester, product determination by mass spectrometry
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additional information
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pectinlyase breaks the glycosidic linkages at C-4 and simultaneously eliminates H from C-5, producing a 4,5-unsatured galacturonic acid group
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additional information
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pectin lyase shows retting ability for natural fibers of Cannabis sativa and Linum usitatissimum
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additional information
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pectin lyase shows retting ability for natural fibers of Cannabis sativa and Linum usitatissimum
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additional information
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KC571175
activity on substrates in decreasing order: pectin, orange peel, apple peel, papaya peel
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additional information
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Bacillus cereus GS2
KC571175
activity on substrates in decreasing order: pectin, orange peel, apple peel, papaya peel
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additional information
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Pel1 alone and Pel1 plus alpha-expansin cause 0.3% and 0.6% swelling of cotton fibers, respectively
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additional information
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enzyme activity leads to maceration of plant tissue by lysis of intercellular tissue
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additional information
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additional enzyme activities contained in the partially purified enzyme preparation, overview
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additional information
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enzyme is involved in cell wall degradation in plants, possible existence of a regulation system for enzyme production in addition to regulation system by recA, rdgA, and rdgB genes
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additional information
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the enzyme is capable of macerating potato and cucumber tissues
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additional information
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constitutive enzyme, probably involved in the soft rot disease caused by Pseudomonas fluorescens
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additional information
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constitutive enzyme, probably involved in the soft rot disease caused by Pseudomonas fluorescens
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additional information
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enzyme is active on highly esterified pectin, and decreases 40% the viscosity of pectin with a degree of esterification of 85%. The enzyme shows no activity on polygalacturonic acid and pectin from citrus fruit which is 8% esterified
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additional information
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enzyme is active on highly esterified pectin, and decreases 40% the viscosity of pectin with a degree of esterification of 85%. The enzyme shows no activity on polygalacturonic acid and pectin from citrus fruit which is 8% esterified
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