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4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
anhydrogalacturonate + H2O
?
citrus pectin + H2O
methanol + citrus pectate
citrus pectin + H2O
methanol + pectate
high methoxyl pectin + H2O
?
-
-
-
-
?
homogalacturonan + n H2O
?
-
-
-
?
homogalaturonan + H2O
?
-
-
-
?
methyl pectate + H2O
?
-
high molecular weight methyl pectate
-
-
?
methyl-esterfied oligogalacturonides + H2O
?
-
C6- and C1-substituted. De-esterification proceeds via a specific pattern, depending on the degree of polymerization. Initially, a first methyl ester of the oligomer is hydrolysed, resulting in one free carboxyl group. Subsequently this first product is preferred as a substrate and is de-esterified for a second time. This product is then accumulated and hereafter de-esterified further to the final product. The saturated hexamer is an exception to this: three methyl esters are removed very rapidly instead of two methyl esters.
-
?
methylated oligogalacturonides + H2O
?
-
-
-
-
?
pectin + H2O
methanol + pectate
pectin + n H2O
n methanol + pectate
additional information
?
-
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
anhydrogalacturonate + H2O
?
-
-
-
-
?
anhydrogalacturonate + H2O
?
-
-
-
-
?
citrus pectin + H2O
methanol + citrus pectate
-
-
-
?
citrus pectin + H2O
methanol + citrus pectate
-
highest activity with pectin with an esterification degree of 50%
-
?
citrus pectin + H2O
methanol + citrus pectate
-
highest activity with pectin with an esterification degree of 50%
-
?
citrus pectin + H2O
methanol + citrus pectate
-
-
-
?
citrus pectin + H2O
methanol + citrus pectate
-
-
?
citrus pectin + H2O
methanol + pectate
-
hydrolyzes pectin from citrus and sugar beet
-
-
?
citrus pectin + H2O
methanol + pectate
-
-
-
?
citrus pectin + H2O
methanol + pectate
-
-
-
-
?
citrus pectin + H2O
methanol + pectate
-
-
-
-
?
citrus pectin + H2O
methanol + pectate
-
best substrate
-
-
?
cyano-acetate + H2O
?
-
-
-
-
?
cyano-acetate + H2O
?
Citrus sp.
-
-
-
-
?
cyano-acetate + H2O
?
-
-
-
-
?
cyano-acetate + H2O
?
-
-
-
-
?
homogalacturonan + H2O
?
different homogalacturonan substrates, best at pH 4.0-6.0 for enzyme BcPME
-
-
?
homogalacturonan + H2O
?
different homogalacturonan substrates, best at pH 4.0-6.0 for enzyme BcPME
-
-
?
homogalacturonan + H2O
?
different homogalacturonan substrates, best at pH 4.0-6.0 for enzyme BcPME
-
-
?
homogalacturonan + H2O
?
-
-
-
-
?
homogalacturonan + H2O
?
different homogalacturonan substrates, best at pH 4.0-6.0 for enzyme BcPME
-
-
?
homogalacturonan + H2O
?
PME removes methyl ester groups from homogalacturonan, overview
-
-
?
pectin + H2O
?
-
-
-
-
?
pectin + H2O
?
-
maximum enzyme production is obtained after 4 days of batch growth
-
-
?
pectin + H2O
?
-
the enzyme is required for the growth of bacteria on oligomeric substrates, probably involved in the degradation of methylated oligogalacturonides present in the periplasm of the bacteria
-
-
?
pectin + H2O
?
-
the electrostatic potential is the trigger of plant cell-wall extension. Pectin methylesterase, together with the proton and cation concentration play a major part in the cell growth process
-
-
?
pectin + H2O
?
-
the enzyme builds up the Donnan potential at the cell surface, this response may be cooperative with respect to pH
-
-
?
pectin + H2O
?
-
constitutive enzyme
-
-
?
pectin + H2O
?
-
the enzyme allows pectin hydrolysis during cell growth
-
-
?
pectin + H2O
?
-
the enzyme deesterifies methoxylated pectin in the plant cell wall
-
-
?
pectin + H2O
methanol + pectate
Acrocylindrium sp.
-
-
-
?
pectin + H2O
methanol + pectate
Acrocylindrium sp.
-
-
-
?
pectin + H2O
methanol + pectate
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6 -
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, central role in the pollen tube growth and determination of pollen tube morphology
-
-
?
pectin + H2O
methanol + pectate
-
PME activity gives rise to negatively charged carboxylic groups and protons in the pectic matrix modifying the cell wall charge, apoplasmic pH and potentially the activity of apoplasmic proteins, the enzyme has several physiologic functions in the plant and is involved e.g. in plant growth, xylogenesis, fruit ripening, plant defense, and in general plant-stress signalling, detailed overview, high content of unmethylesterified HGA, generated by high PME activity in cell walls, correlates positively with the susceptibility of plant cultivars to abiotic and biotic stresses, model of PME involvement in plant defences, overview
-
-
?
pectin + H2O
methanol + pectate
O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6 PME plays an important role in elongation of the pollen tube in pistil, which is essential for delivering sperms into the female gametophyte in sexual plant reproduction, regulation mechanism, overview
-
-
?
pectin + H2O
methanol + pectate
-
degree of methylation of 90%
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
a medium methylated pectin of 46% degree of methylation is used
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
highly methylated citrus pectin
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
ripe var. Easy Pick fruit is characterized by pectin ultradegradation and easy fruit detachment from the calyx, while pectin depolymerization and dissolution in ripe var. Hard Pick fruit is limited, PME activity in vivo is detected only in fruit of the Easy Pick line and is associated with decreased pectin methylesterification, some PME isozymes are apparently inactive in vivo, particularly in green fruit and throughout ripening in the Hard Pick line, limiting polygalacturonase-mediated pectin depolymerization which results in moderately difficult fruit separation from the calyx
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
citrus pectin
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, important role in plant growth and differentiation, enzyme activity in Nausica variety is correlated with ambient temperature
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
Citrus reticulata Citrus sinensis
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
-
no activity if the degree of esterification is below 31%
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
gelling properties of commercial pectins after PME treatment are characterized. The final degree of esterification of the high- and low-methoxy pectins reaches 6% after the PME treatment, while deesterification of low-methoxy amidated pectin stops at 18%. Deesterification of high-methoxy pectin is tailored to be 40%, which is equivalent to the deesterification of commercial low-methoxy pectin. The pectin gel with relatively high peak molecular weight and low deesterification, which is produced from high-methoxy pectin, exhibits the greatest hardness, gumminess, chewiness, and resilience. The hardness of low-methoxy amidated pectin increases over 300% after PME deesterification
-
-
?
pectin + H2O
methanol + pectate
-
86% anhydrous galacturonic acid, 94% degree of methylation, containing minor amounts of galactose
-
-
?
pectin + H2O
methanol + pectate
-
a medium methylated pectin of 46% degree of methylation is used
-
-
?
pectin + H2O
methanol + pectate
Citrus sp.
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
Clostridium multifermentans
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
cranberry
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
PME activity gives rise to negatively charged carboxylic groups and protons in the pectic matrix modifying the cell wall charge, apoplasmic pH and potentially the activity of apoplasmic proteins, the enzyme has several physiologic functions in the plant and is involved e.g. in plant growth, xylogenesis, fruit ripening, plant defense, and in general plant-stress signalling, detailed overview, high content of unmethylesterified HGA, generated by high PME activity in cell walls, correlates positively with the susceptibility of plant cultivars to abiotic and biotic stresses, model of PME involvement in plant defences, overview
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, important for the control of hyperhydricity
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
the enzyme catalyses the essential first step in bacterial invasion of plant tissues
-
-
?
pectin + H2O
methanol + pectate
-
the enzyme shows a sequential pattern of demethylation due to the preferential binding of methylated sugar residues upstream of the catalytic site, and demethylated residues downstream, which drives the enzyme along the pectin molecule
-
-
?
pectin + H2O
methanol + pectate
-
the enzyme catalyzes the hydrolysis of methylester groups from the galacturonic acid residues of homogalacturonan chains, the major component of pectin
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
Diospyros sp.
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
Fragaria sp.
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, application of exogenous PME causes thickening of the apical cell wall and inhibits pollen tube growth
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
Macrosporium cladosporioides
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
pectin B
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, application of exogenous PME causes thickening of the apical cell wall and inhibits pollen tube growth
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
Oospora sp.
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
PME activity gives rise to negatively charged carboxylic groups and protons in the pectic matrix modifying the cell wall charge, apoplasmic pH and potentially the activity of apoplasmic proteins, the enzyme has several physiologic functions in the plant and is involved e.g. in plant growth, xylogenesis, fruit ripening, plant defense, and in general plant-stress signalling, detailed overview, high content of unmethylesterified HGA, generated by high PME activity in cell walls, correlates positively with the susceptibility of plant cultivars to abiotic and biotic stresses, model of PME involvement in plant defences, overview
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
Pellicularia filamentosa
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
low-temperature blanching of vegetables activates PME, which demethylates cell wall pectins and improves tissue firmness
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
PME activity gives rise to negatively charged carboxylic groups and protons in the pectic matrix modifying the cell wall charge, apoplasmic pH and potentially the activity of apoplasmic proteins, the enzyme has several physiologic functions in the plant and is involved e.g. in plant growth, xylogenesis, fruit ripening, plant defense, and in general plant-stress signalling, detailed overview, high content of unmethylesterified HGA, generated by high PME activity in cell walls, correlates positively with the susceptibility of plant cultivars to abiotic and biotic stresses, model of PME involvement in plant defences, overview
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
Prunus sp.
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
Ribes sp.
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
Sclerotinia libertiana
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
674118, 675674, 679554, 680286, 680321, 694603, 714657, 716357, 729017, 729774, 730611 -
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
-
no activity if the degree of esterification is below 31%
-
?
pectin + H2O
methanol + pectate
involved in important physiological processes, such as microsporogenesis, pollen growth, seed germination, root development, polarity of leaf growth, stem elongation, fruit ripening, and loss of tissue integrity
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
low-temperature blanching of vegetables activates PME, which demethylates cell wall pectins and improves tissue firmness
-
-
?
pectin + H2O
methanol + pectate
the enzyme is responsible for the demethylation of galacturonyl residues in high-molecular weight pectin and play s an important role in cell wall metabolism, role of PMEU1 in fruit ripening, overview
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
Torulopsis candida
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
the lower the degree of esterification, the higher the enzyme affinity to the substrate
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
best substrate is Citrus pectin with 85% methyl esterification
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
best substrate is Citrus pectin with 85% methyl esterification
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
substrate is Citrus pectin with 82% degree of methylesterification
-
-
?
pectin + n H2O
n methanol + pectate
substrate is Citrus pectin with a degree of methyl esterification (DM) of 30%, 65% and 90%, best substrate for enzyme AtPME is pectin DM 90% at pH 7.5
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
substrate is Citrus pectin with 82% degree of methylesterification
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
capillary electrophoresis of de-methylesterified pectin, substrate is apple pectin with an approximately sample-averaged 35% degree of methylesterification. Non-processive (or near-random) de-methylesterification by Ani-PME2 at pH 4.2 or by strong base at pH 11.5 is confirmed by a plethora of fragments of varying length and charge. Unmodified apple pectin is preserved upon treatment with a strong base
-
-
?
pectin + n H2O
n methanol + pectate
substrates are citrus pectin with 77% methyl-esterified (DE77) and citrus pectin with 85% methyl-esterified (DE85)
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
substrates are citrus pectin with 77% methyl-esterified (DE77) and citrus pectin with 85% methyl-esterified (DE85)
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
substrate is Citrus pectin with a degree of methylesterification (DM) of 30%, 65% and 90%, best substrate for enzyme BcPME is pectin DM 90% at pH 6.0
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
substrate is Citrus pectin with a degree of methylesterification (DM) of 30%, 65% and 90%, best substrate for enzyme BcPME is pectin DM 90% at pH 6.0
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
substrate is Citrus pectin with a degree of methylesterification (DM) of 30%, 65% and 90%, best substrate for enzyme CsPME is pectin DM 90% at pH 7.5
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
substrate is apple pectin
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
enzyme Sl-PME shows 100% of relative activity for 85% DM pectin, 51.1% for 55-70% DM pectin, 22.4% for 42% DM pectin and only 6.6% for 20-34% DM pectin
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
sisal fibre + H2O
?
-
-
-
-
?
sisal fibre + H2O
?
-
-
-
-
?
additional information
?
-
substrate specificity of CtPME is analysed against various pectic substrates (1%, w/v), viz. Citrus pectin of varying degrees of methyl esterification (85, 75-50 and 25%), apple pectin and poly galacturonic acid (PGA) from Citrus fruit, pectic galactan from potato and lupin, rhamnogalacturonan from soybean (RGS) and potato (RGP), overview
-
-
?
additional information
?
-
-
substrate specificity of CtPME is analysed against various pectic substrates (1%, w/v), viz. Citrus pectin of varying degrees of methyl esterification (85, 75-50 and 25%), apple pectin and poly galacturonic acid (PGA) from Citrus fruit, pectic galactan from potato and lupin, rhamnogalacturonan from soybean (RGS) and potato (RGP), overview
-
-
?
additional information
?
-
substrate specificity of CtPME is analysed against various pectic substrates (1%, w/v), viz. Citrus pectin of varying degrees of methyl esterification (85, 75-50 and 25%), apple pectin and poly galacturonic acid (PGA) from Citrus fruit, pectic galactan from potato and lupin, rhamnogalacturonan from soybean (RGS) and potato (RGP), overview
-
-
?
additional information
?
-
mature PMEs presumably have different modes of action, depending on the environmental conditions such as pH, the initial degree of demethylesterification of pectins, and the presence of cation, overview
-
-
?
additional information
?
-
mature PMEs presumably have different modes of action, depending on the environmental conditions such as pH, the initial degree of demethylesterification of pectins, and the presence of cation, overview
-
-
?
additional information
?
-
mature PMEs presumably have different modes of action, depending on the environmental conditions such as pH, the initial degree of demethylesterification of pectins, and the presence of cation, overview
-
-
?
additional information
?
-
mature PMEs presumably have different modes of action, depending on the environmental conditions such as pH, the initial degree of demethylesterification of pectins, and the presence of cation, overview
-
-
?
additional information
?
-
mature PMEs presumably have different modes of action, depending on the environmental conditions such as pH, the initial degree of demethylesterification of pectins, and the presence of cation, overview
-
-
?
additional information
?
-
mature PMEs presumably have different modes of action, depending on the environmental conditions such as pH, the initial degree of demethylesterification of pectins, and the presence of cation, overview
-
-
?
additional information
?
-
mature PMEs presumably have different modes of action, depending on the environmental conditions such as pH, the initial degree of demethylesterification of pectins, and the presence of cation, overview
-
-
?
additional information
?
-
mature PMEs presumably have different modes of action, depending on the environmental conditions such as pH, the initial degree of demethylesterification of pectins, and the presence of cation, overview
-
-
?
additional information
?
-
mature PMEs presumably have different modes of action, depending on the environmental conditions such as pH, the initial degree of demethylesterification of pectins, and the presence of cation, overview
-
-
?
additional information
?
-
mature PMEs presumably have different modes of action, depending on the environmental conditions such as pH, the initial degree of demethylesterification of pectins, and the presence of cation, overview
-
-
?
additional information
?
-
mature PMEs presumably have different modes of action, depending on the environmental conditions such as pH, the initial degree of demethylesterification of pectins, and the presence of cation, overview
-
-
?
additional information
?
-
-
the overall PME activity greatly decreases with a pectic substrate with a degree of methylation of 60%
-
-
?
additional information
?
-
substrate specificity, overview. Homogalacturonan substrates are HG96B20, HG96B39 HG96B56, HG96B69, HG96B82, HG96P14, HG96P36, HG96P56, HG96P64, and HG96P75. Spectrometric quantification
-
-
?
additional information
?
-
-
enzyme immobilized on CNBr-Sepharose 4B show about 11.5% of the activity of the free enzyme
-
-
?
additional information
?
-
-
enzyme immobilized on polyethylene terephthalate shows 23.1% of the activity of the free enzyme
-
-
?
additional information
?
-
-
the immobilized enzyme, unlike the free pectin esterase, does not act on pectin showing a higher esterification degree
-
-
?
additional information
?
-
generally PMEs from fungal have broad substrate specificity because the methyl groups on pectin are attacked by these enzymes in a random manner. Enzyme PME-ZJ5A shows significant potential for increasing the clarity of pineapple juice
-
-
?
additional information
?
-
-
generally PMEs from fungal have broad substrate specificity because the methyl groups on pectin are attacked by these enzymes in a random manner. Enzyme PME-ZJ5A shows significant potential for increasing the clarity of pineapple juice
-
-
?
additional information
?
-
lack of processivity by isozyme Ani-PME2, overview
-
-
?
additional information
?
-
-
lack of processivity by isozyme Ani-PME2, overview
-
-
?
additional information
?
-
generally PMEs from fungal have broad substrate specificity because the methyl groups on pectin are attacked by these enzymes in a random manner. Enzyme PME-ZJ5A shows significant potential for increasing the clarity of pineapple juice
-
-
?
additional information
?
-
substrate specificity, overview. Homogalacturonan substrates are HG96B20, HG96B39 HG96B56, HG96B69, HG96B82, HG96P14, HG96P36, HG96P56, HG96P64, and HG96P75. Spectrometric quantification
-
-
?
additional information
?
-
substrate specificity, overview. Homogalacturonan substrates are HG96B20, HG96B39 HG96B56, HG96B69, HG96B82, HG96P14, HG96P36, HG96P56, HG96P64, and HG96P75. Spectrometric quantification
-
-
?
additional information
?
-
the increase in the calcium sensitivity of the PME-treated pectin indicates a blockwise mode of action, pectin treated with papaya PME is precipitated by CaCl2
-
-
?
additional information
?
-
-
the increase in the calcium sensitivity of the PME-treated pectin indicates a blockwise mode of action, pectin treated with papaya PME is precipitated by CaCl2
-
-
?
additional information
?
-
-
role of enzyme in juice clarification
-
-
?
additional information
?
-
-
role of enzyme in juice clarification
-
-
?
additional information
?
-
substrate specificity, overview. Homogalacturonan substrates are HG96B20, HG96B39 HG96B56, HG96B69, HG96B82, HG96P14, HG96P36, HG96P56, HG96P64, and HG96P75. Spectrometric quantification
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
the mildly basic and polymorphic protein causes allergic reactions in humans determined by secific IgE production
-
-
?
additional information
?
-
-
the mildly basic and polymorphic protein causes allergic reactions in humans determined by secific IgE production
-
-
?
additional information
?
-
involved in cell wall stiffening
-
?
additional information
?
-
involved in cell wall stiffening
-
?
additional information
?
-
involved in cell wall stiffening
-
?
additional information
?
-
-
PME suppressed tobacco mosaic virus reproduction, including short- and long-distance virus movement in plants
-
-
?
additional information
?
-
-
PME suppressed tobacco mosaic virus reproduction, including short- and long-distance virus movement in plants
-
-
?
additional information
?
-
the enzyme inhibits intrusive and symplastic cell growth in developing wood cells of hybrid aspen acting as a negative regulator of both, PME1 is involved in xylogenesis and mechanisms determining fiber width and length in the wood of aspen trees, overview
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
immobilized enzymes show about 7.5% of the activity of the free enzyme
-
-
?
additional information
?
-
-
the immobilized enzyme, unlike the free pectin esterase, does not act on pectin showing a higher esterification degree
-
-
?
additional information
?
-
-
the pectinmethylesterase catalyzes pectin de-esterification accelerates by increasing pressure up to 200 MPa in presence of tomato polygalacturonase
-
-
?
additional information
?
-
the enzyme is active on pectin substrates with degree of methylesterification (DM): sugar beet pectin (DM 42%) apple pectin (DM 70-75%), and citrus pectin (DM 20-34%, 55-70%, and over 85%), but not on polygalacturonic acid
-
-
?
additional information
?
-
-
the enzyme is active on pectin substrates with degree of methylesterification (DM): sugar beet pectin (DM 42%) apple pectin (DM 70-75%), and citrus pectin (DM 20-34%, 55-70%, and over 85%), but not on polygalacturonic acid
-
-
?
additional information
?
-
role in cell wall stiffening
-
?
additional information
?
-
role in cell wall stiffening
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
citrus pectin + H2O
methanol + pectate
-
best substrate
-
-
?
pectin + H2O
methanol + pectate
pectin + n H2O
n methanol + pectate
additional information
?
-
pectin + H2O
?
-
maximum enzyme production is obtained after 4 days of batch growth
-
-
?
pectin + H2O
?
-
the enzyme is required for the growth of bacteria on oligomeric substrates, probably involved in the degradation of methylated oligogalacturonides present in the periplasm of the bacteria
-
-
?
pectin + H2O
?
-
the electrostatic potential is the trigger of plant cell-wall extension. Pectin methylesterase, together with the proton and cation concentration play a major part in the cell growth process
-
-
?
pectin + H2O
?
-
the enzyme builds up the Donnan potential at the cell surface, this response may be cooperative with respect to pH
-
-
?
pectin + H2O
?
-
constitutive enzyme
-
-
?
pectin + H2O
?
-
the enzyme allows pectin hydrolysis during cell growth
-
-
?
pectin + H2O
?
-
the enzyme deesterifies methoxylated pectin in the plant cell wall
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, central role in the pollen tube growth and determination of pollen tube morphology
-
-
?
pectin + H2O
methanol + pectate
-
PME activity gives rise to negatively charged carboxylic groups and protons in the pectic matrix modifying the cell wall charge, apoplasmic pH and potentially the activity of apoplasmic proteins, the enzyme has several physiologic functions in the plant and is involved e.g. in plant growth, xylogenesis, fruit ripening, plant defense, and in general plant-stress signalling, detailed overview, high content of unmethylesterified HGA, generated by high PME activity in cell walls, correlates positively with the susceptibility of plant cultivars to abiotic and biotic stresses, model of PME involvement in plant defences, overview
-
-
?
pectin + H2O
methanol + pectate
O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6 PME plays an important role in elongation of the pollen tube in pistil, which is essential for delivering sperms into the female gametophyte in sexual plant reproduction, regulation mechanism, overview
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
ripe var. Easy Pick fruit is characterized by pectin ultradegradation and easy fruit detachment from the calyx, while pectin depolymerization and dissolution in ripe var. Hard Pick fruit is limited, PME activity in vivo is detected only in fruit of the Easy Pick line and is associated with decreased pectin methylesterification, some PME isozymes are apparently inactive in vivo, particularly in green fruit and throughout ripening in the Hard Pick line, limiting polygalacturonase-mediated pectin depolymerization which results in moderately difficult fruit separation from the calyx
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, important role in plant growth and differentiation, enzyme activity in Nausica variety is correlated with ambient temperature
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
Citrus reticulata Citrus sinensis
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
PME activity gives rise to negatively charged carboxylic groups and protons in the pectic matrix modifying the cell wall charge, apoplasmic pH and potentially the activity of apoplasmic proteins, the enzyme has several physiologic functions in the plant and is involved e.g. in plant growth, xylogenesis, fruit ripening, plant defense, and in general plant-stress signalling, detailed overview, high content of unmethylesterified HGA, generated by high PME activity in cell walls, correlates positively with the susceptibility of plant cultivars to abiotic and biotic stresses, model of PME involvement in plant defences, overview
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, important for the control of hyperhydricity
-
-
?
pectin + H2O
methanol + pectate
-
the enzyme catalyses the essential first step in bacterial invasion of plant tissues
-
-
?
pectin + H2O
methanol + pectate
-
the enzyme catalyzes the hydrolysis of methylester groups from the galacturonic acid residues of homogalacturonan chains, the major component of pectin
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, application of exogenous PME causes thickening of the apical cell wall and inhibits pollen tube growth
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, application of exogenous PME causes thickening of the apical cell wall and inhibits pollen tube growth
-
-
?
pectin + H2O
methanol + pectate
-
PME activity gives rise to negatively charged carboxylic groups and protons in the pectic matrix modifying the cell wall charge, apoplasmic pH and potentially the activity of apoplasmic proteins, the enzyme has several physiologic functions in the plant and is involved e.g. in plant growth, xylogenesis, fruit ripening, plant defense, and in general plant-stress signalling, detailed overview, high content of unmethylesterified HGA, generated by high PME activity in cell walls, correlates positively with the susceptibility of plant cultivars to abiotic and biotic stresses, model of PME involvement in plant defences, overview
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
low-temperature blanching of vegetables activates PME, which demethylates cell wall pectins and improves tissue firmness
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
PME activity gives rise to negatively charged carboxylic groups and protons in the pectic matrix modifying the cell wall charge, apoplasmic pH and potentially the activity of apoplasmic proteins, the enzyme has several physiologic functions in the plant and is involved e.g. in plant growth, xylogenesis, fruit ripening, plant defense, and in general plant-stress signalling, detailed overview, high content of unmethylesterified HGA, generated by high PME activity in cell walls, correlates positively with the susceptibility of plant cultivars to abiotic and biotic stresses, model of PME involvement in plant defences, overview
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + H2O
methanol + pectate
involved in important physiological processes, such as microsporogenesis, pollen growth, seed germination, root development, polarity of leaf growth, stem elongation, fruit ripening, and loss of tissue integrity
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity
-
-
?
pectin + H2O
methanol + pectate
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
-
low-temperature blanching of vegetables activates PME, which demethylates cell wall pectins and improves tissue firmness
-
-
?
pectin + H2O
methanol + pectate
the enzyme is responsible for the demethylation of galacturonyl residues in high-molecular weight pectin and play s an important role in cell wall metabolism, role of PMEU1 in fruit ripening, overview
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
pectin + H2O
methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
pectin + n H2O
n methanol + pectate
-
-
-
?
additional information
?
-
the mildly basic and polymorphic protein causes allergic reactions in humans determined by secific IgE production
-
-
?
additional information
?
-
-
the mildly basic and polymorphic protein causes allergic reactions in humans determined by secific IgE production
-
-
?
additional information
?
-
involved in cell wall stiffening
-
?
additional information
?
-
involved in cell wall stiffening
-
?
additional information
?
-
involved in cell wall stiffening
-
?
additional information
?
-
-
PME suppressed tobacco mosaic virus reproduction, including short- and long-distance virus movement in plants
-
-
?
additional information
?
-
-
PME suppressed tobacco mosaic virus reproduction, including short- and long-distance virus movement in plants
-
-
?
additional information
?
-
the enzyme inhibits intrusive and symplastic cell growth in developing wood cells of hybrid aspen acting as a negative regulator of both, PME1 is involved in xylogenesis and mechanisms determining fiber width and length in the wood of aspen trees, overview
-
-
?
additional information
?
-
role in cell wall stiffening
-
?
additional information
?
-
role in cell wall stiffening
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CaCl2
-
activates with increasing temperature to a maximal value
Cr3+
-
216.5% activity at 1 mM
Cs+
activates slightly at 5 mM
Cu2+
-
104.5% activity at 1 mM
EDTA
-
229% activity at 1 mM
Fe3+
-
107.1% activity at 1 mM
Ni2+
-
331.8% activity at 1 mM
Pb2+
-
139.2% activity at 1 mM
SDS
-
105.9% activity at 1 mM
(NH4)2SO4
-
activates
aluminium
-
a toxic metal in soils that inhibits plant root elongation, can be modulated by PME activity, overexpression of PME activity leads to increases in aluminium content in the plant, which correlates to reductions in the degree of pectin methylesterification, overview
aluminium
a toxic metal in soils that inhibits plant root elongation, can be modulated by PME activity, overexpression of PME activity leads to increases in aluminium content in the plant, which correlates to reductions in the degree of pectin methylesterification, overview
aluminium
-
a toxic metal in soils that inhibits plant root elongation, can be modulated by PME activity, overexpression of PME activity leads to increases in aluminium content in the plant, which correlates to reductions in the degree of pectin methylesterification, overview
aluminium
-
a toxic metal in soils that inhibits plant root elongation, can be modulated by PME activity, overexpression of PME activity leads to increases in aluminium content in the plant, which correlates to reductions in the degree of pectin methylesterification, overview
Ca2+
40% activation at 5 mM
Ca2+
Acrocylindrium sp.
-
activates
Ca2+
Acrocylindrium sp.
-
CaCl2, activates
Ca2+
specific activity is higher in the presence than in the absence of 5 mM Ca2+
Ca2+
Ca2+ strongly stimulates activity at 5 mM
Ca2+
-
the highest PME activity occurrs at 20 mM of Ca2+, further increase in concentration results in the decline of the enzyme activity
Ca2+
-
specific activity is higher in the presence than in the absence of 5 mM Ca2+
Ca2+
-
Ca2+ slightly stimulates activity at 5 mM
Ca2+
-
optimal concentration: 0.05 M
Ca2+
-
313.2% activity at 1 mM
Ca2+
-
CaCl2, stimulates, optimal concentration is 0.1 M
Ca2+
-
stimulates, optimal concentration is 0.01 M
Ca2+
-
CaCl2, isoenzyme PE I is stimulated to a higher degree than isoenzyme PE II
Ca2+
-
60 mM Ca2+ increases activity at elevated pressure up to 300 MPa, but decreases enzyme activity at atmospheric pressure and 45-60°C
Co2+
activates at 5 mM
Co2+
-
351.2% activity at 1 mM
K+
Acrocylindrium sp.
-
KCl, activates
K+
-
the activity of the enzyme increases with increase in the concentration of K+, further increase in concentration results in the decline of the enzyme activity
K+
-
126.1% activity at 1 mM
Li+
Acrocylindrium sp.
-
-
Li+
Acrocylindrium sp.
-
LiCl, activates
Li+
-
118.2% activity at 1 mM
Mg2+
40% activation at 5 mM
Mg2+
Acrocylindrium sp.
-
activates
Mg2+
-
highest activity at 15 mM Mg2+, further increase in concentration results in the decline of the enzyme activity
Mg2+
-
379.5% activity at 1 mM
Mn2+
activates at 5 mM
Mn2+
-
369.9% activity at 1 mM
Na+
pme31 mutants are more sensitive to Na+ toxicity than the wild-type
Na+
-
the activity of the enzyme increases with increase in the concentration of Na+, further increase in concentration results in the decline of the enzyme activity
Na+
-
137.2% activity at 1 mM
NaCl
activates slightly at 5 mM
NaCl
Acrocylindrium sp.
-
activates
NaCl
-
activating at 100 mM, especially at pH under 7.0
NaCl
required, at 0.8 M. Without added NaCl, protein activity is highly reduced. At pH 7.0 and above in the presence of 100 mM NaCl, Ani-PME2 is nearly inactive
NaCl
-
enzyme is not affected by NaCl from 0.1 M to 0.5 M concentrations
NaCl
-
0.13 M NaCl required for optimum activity
NaCl
-
maximum activity at 2 M
NaCl
-
dependent on NaCl, 0.2 M
NaCl
activates, PME is salt-dependent, best at 0.25 M
NaCl
-
optimal concentration: 0.3-0.5 M
NaCl
-
highest activity in the presence of 1 M NaCl. No enzyme activity (assayed at pH 7.0) is detected in salt-free water washes of pulp (measured at pH 3.8)
NaCl
-
optimum activity in the presence of 0.3 M NaCl
NaCl
-
optimum activity in the presence of 0.3 M NaCl
NaCl
-
optimum activity in the presence of 0.3 M NaCl
NaCl
-
optimal concentration: 0.2 M
NaCl
-
activating at 100 mM at pH under 7.0
NaCl
-
optimal concentration: 0.2 M
NaCl
-
optimal concentration: 0.18 M
NaCl
-
stimulates, optimal concentration is 0.1 M
NaCl
-
isoenzyme PE I is stimulated to a higher degree than the enzyme PE II
NaCl
apricot PME activity is dependent on NaCl. With NaCl concentration increasing in the assay mixture, the PME activity increases gradually and reaches the maximum level at 0.15 M
NaCl
-
highest activity at 0.15 M
NaCl
-
optimal concentration: 0.3-0.5 M
NaCl
-
activates, optimal concentration 0.1-0.15 mM
SrCl2
Acrocylindrium sp.
-
activates
SrCl2
-
activates with increasing temperature to a maximal value
Zn2+
-
highest activity at 15 mM Zn2+, further increase in concentration results in the decline of the enzyme activity
Zn2+
-
324.4% activity at 1 mM
additional information
no or poor effect by 5 mM of Ba2+, Li+, K+, and Cs+
additional information
-
no or poor effect by 5 mM of Ba2+, Li+, K+, and Cs+
additional information
-
the enzyme does not require salt for activity
additional information
-
not affected by Na+
additional information
-
no metal ions required for activity
additional information
PMEU1 is a salt-dependent isozyme
additional information
-
PMEU1 is a salt-dependent isozyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(-)-epigallocatechin
-
82% residual activity at 20 mg/ml
(-)-epigallocatechin gallate
exhibits 97.8% inhibition at 1 mg/ml and 47.0% at 0.1 mg/ml
(E)-1-(2-nitroethenyl)-4-(2-propenyloxy)-benzene
(NH4)2SO4
Acrocylindrium sp.
-
-
(NH4)Cl
Acrocylindrium sp.
-
-
1-(3,4-dihydroxyphenyl)-2-([1-(1-naphthyl)-1H-tetrazol-5-yl]thio)ethanone
1-(3,6-dichloro-9H-carbazoyl-9-yl)-3-morpholinopropan-2-ol
10-(hydroxymethylene)-9(10H)-phenanthrenone
2-(2-[4-(trifluoromethyl)phenyl]hydrazylidene)propanedinitrile
2-(3,4-dihydro-1(2H)-naphthalenylidene)hydrazinecarbothioamide
2-(3-chloro-2-fluorophenyl)-2,3-dihydroisothiazol-3-one
2-chloro-3-(2-methylphenoxy)-1,4-dihydro-naphthalene-1,4-dione
2-[(4-chlorophenyl)sulfonyl]-2,4-dihydro-4-(2-propen-1-yl)-5-propyl-3H-pyrazol-3-one
4-(3-hydroxy-3-methylbut-1-ynyl)benzaldehyde-2-phenylhydrazone
4-[1-(fur-2-oyl)pyrazol-5-yl]-5-methyl-1-phenylpyrazole
beta-mercaptoethanol
-
96% residual activity at 1 mM
Ca2+
-
60 mM Ca2+ decreases enzyme activity at atmospheric pressure and 45-60°C, but increases activity at elevated pressure up to 300 MPa
catechinhydrate
-
83% residual activity at 20 mg/ml
Co2+
-
52% residual activity at 100 mM
dense phase carbon dioxide
-
the maximum reduction of the residual activity of apple PME exposed to dense phase carbon dioxide is 94.57% at 55?C for 60 min, the residual activity of apple PME after dense phase carbon dioxide exhibits no reduction or reactivation for 4 weeks at 4°C
-
K+
-
73% residual activity at 100 mM
Mg2+
-
86% residual activity at 100 mM
Mn2+
-
61% residual activity at 100 mM
N'1-[2-(tert-butyl)-5-(trifluoromethyl)-pyrazolo[1,5-alpha]-pyrimidin-7-yl]-4-chlorobenzenohydrazide
N'6-[3,5-di-(trifluoromethyl)phenyl]-5-oxo-2,3-dihydro-5H-pyrimido-[2,1-b][1,3]thiazole-6-carbohydrazide
N-(1,4-dibenzoyl-5-phenyl-4,5-dihydro-1H-1,2,4-triazol-3-yl)-benzamide
N-(3,5-dichlorophenyl)-N'-[5-(2-furyl)-1H-pyrazol-3-yl]urea
N-(4-chloro-2-nitrophenyl)-N'-phenylurea
N-(4-methyl-2-thienyl)-N'-[4-(trifluoromethyl)phenyl]-urea
N-[(2-chlorobenzoyl)oxy]-2,1,3-benzoxadiazole-5-carboximidamide
N1-[3-(trifluoromethyl)phenyl]-3-(2-thienylthio)-propanamide
N4-(2-furylmethyl)-2-(2,3-dihydro-1,4-benzodioxin-2-yl)-1,3-thiazole-4-carboxamide
Pectin
-
inhibits hydrolysis of p-nitrophenyl acetate
pectin methylesterase inhibitor
-
pectin methylesterase inhibitor 7
PMEI7, inhibits the enzyme only at pH 5.0, not at pH 6.3-7.5, re-incubating the sample at pH values where the inhibitory capacity of AtPMEI7 is not expected, fully restores AtPME3 activity. PME3 enzyme-bound complex structure analysis, stability of the AtPME3-AtPMEI7 complex at acidic and neutral pH, overview. The mechanism of competition between intramolecular and intermolecular contacts is not isolated to a single pair of residues. Changes in the protonation of amino acids at the complex interface shift the network of interacting residues between intermolecular and intramolecular. These shifts ultimately regulate the stability of the PME3-PMEI7 complex and the inhibition of the PME as a function of the pH. Analysis of the conformational dynamics of the PMEI helices reveals a consistent twist of helix alphaII, which is mostly involved in the binding of AtPME3. The dihedral space explored by helix alphaII reveals the presence of several populations at pH 7.0, with values of psi dihedral angles shifting toward regions of the Ramachandran plot that do not characterize alpha-helices. PMEI7 mutated version E68A (as the wild-type protein) is able to inhibit PME activity, whereas E75A is not
-
pectin methylesterase inhibitor28
OsPMEI28, UniProt ID Q0J8J8, recombinant expression in Oryza sativa cv. Dongjin via Agrobacterium tumafaciens LBA4404-mediated transformation, RT-PCR and real-time PCR expression analysis. Pectin methylesterases (PMEs) belonging to carbohydrate esterase family 8 cleave the ester bond between a galacturonic acid and an methyl group. The resulting change in methylesterification level plays an important role during the growth and development of plants. Optimal pectin methylesterification status in each cell type is determined by the balance between PME activity and posttranslational PME inhibition by PME inhibitors (PMEIs). Cloning, sequence analysis, and tissue-specific expression of OsPMEI28, overview
-
pressure
-
250-400 MPa, highest enzyme inactivation occurred at 400 mPA after 25 min, pressure pulses between 250 and 400 MPa cause inactivation between 30% and 90%
-
Protein inhibitor
PMEI, isolated from kiwi (Actinidia deliciosa), formation at 1:1 complex with the enzyme especially at acidic conditions, no formation f enzyme-inhibitor complex at pH 8.5
-
proteinaceous pectin methylesterase inhibitor
-
[5-(4-chlorophenyl)-3-thienyl]-(piperidino)-methanone
(E)-1-(2-nitroethenyl)-4-(2-propenyloxy)-benzene
-
(E)-1-(2-nitroethenyl)-4-(2-propenyloxy)-benzene
-
1-(3,4-dihydroxyphenyl)-2-([1-(1-naphthyl)-1H-tetrazol-5-yl]thio)ethanone
-
1-(3,4-dihydroxyphenyl)-2-([1-(1-naphthyl)-1H-tetrazol-5-yl]thio)ethanone
-
1-(3,6-dichloro-9H-carbazoyl-9-yl)-3-morpholinopropan-2-ol
-
1-(3,6-dichloro-9H-carbazoyl-9-yl)-3-morpholinopropan-2-ol
-
10-(hydroxymethylene)-9(10H)-phenanthrenone
-
10-(hydroxymethylene)-9(10H)-phenanthrenone
-
2-(2-[4-(trifluoromethyl)phenyl]hydrazylidene)propanedinitrile
-
2-(2-[4-(trifluoromethyl)phenyl]hydrazylidene)propanedinitrile
-
2-(3,4-dihydro-1(2H)-naphthalenylidene)hydrazinecarbothioamide
-
2-(3,4-dihydro-1(2H)-naphthalenylidene)hydrazinecarbothioamide
-
2-(3-chloro-2-fluorophenyl)-2,3-dihydroisothiazol-3-one
-
2-(3-chloro-2-fluorophenyl)-2,3-dihydroisothiazol-3-one
-
2-chloro-3-(2-methylphenoxy)-1,4-dihydro-naphthalene-1,4-dione
-
2-chloro-3-(2-methylphenoxy)-1,4-dihydro-naphthalene-1,4-dione
-
2-methoxyacridin-9-amine
-
2-methoxyacridin-9-amine
-
2-[(4-chlorophenyl)sulfonyl]-2,4-dihydro-4-(2-propen-1-yl)-5-propyl-3H-pyrazol-3-one
-
2-[(4-chlorophenyl)sulfonyl]-2,4-dihydro-4-(2-propen-1-yl)-5-propyl-3H-pyrazol-3-one
-
3H-pyrazol-3-one
-
4-(3-hydroxy-3-methylbut-1-ynyl)benzaldehyde-2-phenylhydrazone
-
4-(3-hydroxy-3-methylbut-1-ynyl)benzaldehyde-2-phenylhydrazone
-
4-[1-(fur-2-oyl)pyrazol-5-yl]-5-methyl-1-phenylpyrazole
-
4-[1-(fur-2-oyl)pyrazol-5-yl]-5-methyl-1-phenylpyrazole
-
copper sulfate
-
copper sulfate
only slight inhibition
coumaric acid
-
-
Cu2+
-
D-glucose
-
-
EDTA
-
EDTA
-
partial inhibition at 10 mM; slight inhibition
EGTA
-
EGTA
-
EGTA treatment reduces PME activity, but the addition of Ca2+ with EGTA reinstates the activity in response to heat shock
epigallocatechin gallate
-
47% residual activity at 20 mg/ml
epigallocatechin gallate
-
natural inhibitor for pectin methyl esterase, acts as a non-specific pan-inhibitor for PME
epigallocatechin gallate
Citrus sp.
-
natural inhibitor for pectin methyl esterase, acts as a non-specific pan-inhibitor for PME
epigallocatechin gallate
-
natural inhibitor for pectin methyl esterase, acts as a non-specific pan-inhibitor for PME
epigallocatechin gallate
-
natural inhibitor for pectin methyl esterase, acts as a non-specific pan-inhibitor for PME
Fe2+
-
FeCl3
-
-
gallic acid
-
-
gallic acid
-
80% residual activity at 20 mg/ml
gallocatechin gallate
-
-
gallocatechin gallate
Citrus sp.
-
-
gallocatechin gallate
-
-
gallocatechin gallate
-
-
glycerol
-
-
Hg2+
almost complete inhibition at 5 mM
HgCl2
Acrocylindrium sp.
-
-
HgCl2
-
1.0 mM of HgCl2 results in approximately 50% loss of enzyme activity, while concentration of 8 mM produces complete loss of enzyme activity
hydrazine
-
Iodine
-
-
iodoacetic acid
-
-
N'1-[2-(tert-butyl)-5-(trifluoromethyl)-pyrazolo[1,5-alpha]-pyrimidin-7-yl]-4-chlorobenzenohydrazide
-
N'1-[2-(tert-butyl)-5-(trifluoromethyl)-pyrazolo[1,5-alpha]-pyrimidin-7-yl]-4-chlorobenzenohydrazide
-
N'6-[3,5-di-(trifluoromethyl)phenyl]-5-oxo-2,3-dihydro-5H-pyrimido-[2,1-b][1,3]thiazole-6-carbohydrazide
-
N'6-[3,5-di-(trifluoromethyl)phenyl]-5-oxo-2,3-dihydro-5H-pyrimido-[2,1-b][1,3]thiazole-6-carbohydrazide
-
N-(1,4-dibenzoyl-5-phenyl-4,5-dihydro-1H-1,2,4-triazol-3-yl)-benzamide
-
N-(1,4-dibenzoyl-5-phenyl-4,5-dihydro-1H-1,2,4-triazol-3-yl)-benzamide
-
N-(3,5-dichlorophenyl)-N'-[5-(2-furyl)-1H-pyrazol-3-yl]urea
-
N-(3,5-dichlorophenyl)-N'-[5-(2-furyl)-1H-pyrazol-3-yl]urea
-
N-(4-chloro-2-nitrophenyl)-N'-phenylurea
-
N-(4-chloro-2-nitrophenyl)-N'-phenylurea
-
N-(4-methyl-2-thienyl)-N'-[4-(trifluoromethyl)phenyl]-urea
-
N-(4-methyl-2-thienyl)-N'-[4-(trifluoromethyl)phenyl]-urea
-
N-[(2-chlorobenzoyl)oxy]-2,1,3-benzoxadiazole-5-carboximidamide
-
N-[(2-chlorobenzoyl)oxy]-2,1,3-benzoxadiazole-5-carboximidamide
-
N1-[3-(trifluoromethyl)phenyl]-3-(2-thienylthio)-propanamide
-
N1-[3-(trifluoromethyl)phenyl]-3-(2-thienylthio)-propanamide
-
N4-(2-furylmethyl)-2-(2,3-dihydro-1,4-benzodioxin-2-yl)-1,3-thiazole-4-carboxamide
-
N4-(2-furylmethyl)-2-(2,3-dihydro-1,4-benzodioxin-2-yl)-1,3-thiazole-4-carboxamide
-
NaCl
-
activity decreases in the presence of 0.1 M NaCl and is 4times lower in 0.5 M NaCl
NaCl
NaCl causes loss of 40% and 90% of enzyme activity at 0.1 M and 0.5 M, respectively
Ni2+
-
47% residual activity at 100 mM
pectate
-
-
pectin methylesterase inhibitor
PMEI
-
pectin methylesterase inhibitor
PMEI, 97 putative PMEI genes are identified in Brassica rapa genome. By a phylogenetic analysis, the PMEI family is divided into 10 clades with highly conserved structural characteristics. Chromosomal distribution and Ks analysis of PMEI family in Brassica rapa. Expression analysis of PMEI genes in response to male sterility, overview
-
pectin methylesterase inhibitor
-
PMEI, two tomato PMEIs, SolycPMEI13 and SolycPMEI14, exhibit PMEI activities and inhibit enzyme PME. In the tomato genome, there exist 48 PMEI genes with temporally and spatially regulated expression, realtime PCR expression analysis show tissue-specific expression. Recombinant expression of MBP-tagged PMEIs in Escherichia coli strain BL21 CodonPlus (DE3)-RIPL. The highest PME activity is detected in samples isolated from green fruits, whereas soluble proteins isolated from green and red fruit possess the lowest PMEI activity
-
phenylmercuric acetate
-
PMEI
O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6 i.e. PME inhibitor; i.e. PME inhibitor; i.e. PME inhibitor; i.e. PME inhibitor; i.e. PME inhibitor; i.e. PME inhibitor; i.e. PME inhibitor; i.e. PME inhibitor; i.e. PME inhibitor; i.e. PME inhibitor; i.e. PME inhibitor
-
Polygalacturonate
-
-
Polygalacturonate
-
competitive
Polygalacturonate
-
completely deesterified pectin, a competitive inhibitor of PME
polygalacturonic acid
-
end-product inhibition
polygalacturonic acid
-
end-product inhibition
polygalacturonic acid
-
end-product inhibition
polygalacturonic acid
-
end-product inhibition
polygalacturonic acid
-
end-product inhibition
polygalacturonic acid
competitive inhibitor, inhibits the alpha isoform at pH 5.6 and the gamma isoform at pH 5.6 and pH 7.6
polyphenon 60
PP60, commercial inhibitor mixture that contains 60% catechin (which consists of 34% (-)-epigallocatechin-3-gallate, 16.7% (-)-epigallocatechin, 8.7% (-)-epicatechin-3-gallate, 7.3% (-)-epicatechin, 2.8% (-)-gallocatechin gallate, and 0.5% (-)-catechin gallate), tannic acid, or (-)-epigallocatechin-3-gallate
-
polyphenon 60
PP60, commercial inhibitor mixture that contains 60% catechin (which consists of 34% (-)-epigallocatechin-3-gallate, 16.7% (-)-epigallocatechin, 8.7% (-)-epicatechin-3-gallate, 7.3% (-)-epicatechin, 2.8% (-)-gallocatechin gallate, and 0.5% (-)-catechin gallate), tannic acid, or (-)-epigallocatechin-3-gallate
-
polyphenon 60
PP60, exhibits 94.8% inhibition at 1 mg/ml and 26.8% at 0.1 mg/ml
-
PP60
-
concentration-dependent inhibition
PP60
Citrus sp.
-
concentration-dependent inhibition
PP60
-
concentration-dependent inhibition
PP60
-
concentration-dependent inhibition
proteinaceous pectin methylesterase inhibitor
-
PMEI, isolated from kiwi fruit (Actinidia chinensis cv. Hayward), competitive, medium inhibition
-
proteinaceous pectin methylesterase inhibitor
-
specific inhibition
-
proteinaceous pectin methylesterase inhibitor
-
PMEI, isolated from kiwi fruit (Actinidia chinensis cv. Hayward), noncompetitive,strong inhibition
-
proteinaceous pectin methylesterase inhibitor
-
PMEI, isolated from kiwi fruit (Actinidia chinensis cv. Hayward), noncompetitive, slight inhibition
-
proteinaceous pectin methylesterase inhibitor
-
specific inhibition
-
SDS
-
SDS
-
78% residual activity at 10 mg/ml SDS
SDS
-
0.1% complete inactivation
Silver nitrate
complete inhibition
Silver nitrate
complete inhibition
sucrose
-
-
Tannic acid
-
10 mg/ml tannic acid completely inhibits the enzyme
Tannic acid
exhibits 99.5% inhibition at 1 mg/ml and 55.2% at 0.1 mg/ml
tannin
-
-
-
Zn2+
strong inhibition at 5 mM
[5-(4-chlorophenyl)-3-thienyl]-(piperidino)-methanone
-
[5-(4-chlorophenyl)-3-thienyl]-(piperidino)-methanone
-
additional information
no inhibition by Tween 20 and Triton X100 at 5 mM
-
additional information
-
no inhibition by Tween 20 and Triton X100 at 5 mM
-
additional information
-
effects of hormones and stresses on isozyme expression, overview
-
additional information
-
a purified kiwi (Actinidia chinensis) pectin methylesterase inhibitor has no effect on the activity of the enzyme
-
additional information
analysis of inhibition of the enzyme by polyphenols such as catechins and tannic acid, overview
-
additional information
endogenous inhibitor PMEI5 does not act through HMS in the embryo cell wall
-
additional information
-
no inhibition by proteinaceous pectin methylesterase inhibitor isolated from kiwi fruit
-
additional information
-
not inhibited by proteinaceous pectin methylesterase inhibitor from kiwi fruit
-
additional information
-
10 mg/ml sucrose and 10 mg/ml coumaric acid have no effect on enzyme activity
-
additional information
-
not inhibited by proteinaceous pectin methylesterase inhibitor from kiwi fruit
-
additional information
analysis of inhibition of the enzyme by polyphenols such as catechins and tannic acid, or polyphenon 60 mixture, overview. The fungal PME is not sensitive to inhibition, overview
-
additional information
-
analysis of the effect of high hydrostatic pressure treatment combined with moderate processing temperatures (25-50°C) on the inactivation of pectin methyl esterase in orange juice. The greatest reduction of pectin methyl esterase of 90.05% is obtained at 50°C and 500 MPa of pressure for 15 min, therefore, the pectin methyl esterase enzyme is highly resistant to the treatments by high hydrostatic pressure
-
additional information
analysis of inhibition of the enzyme by polyphenols such as catechins and tannic acid, overview
-
additional information
rice contains 49 PMEIs, including OsPMEI28
-
additional information
-
no inhibition by up to 10 mM spermidine at 30°C
-
additional information
-
not inhibited by proteinaceous pectin methylesterase inhibitor from kiwi fruit
-
additional information
-
inhibition of the activation of the enzyme PME retardes the hydrolysis of pectin and texture softening during storage, e.g. by lowering pH and ethylene concentration
-
additional information
-
the pectinmethylesterase catalyzes pectin de-esterification accelerates by increasing pressure up to 200 MPa in presence of tomato polygalacturonase, higher pressures diminished the tomato pectinmethylesterase activity becoming even lower as compared to atmospheric pressure
-
additional information
no inhibition by PME inhibitor from kiwi fruits
-
additional information
-
no inhibition by PME inhibitor from kiwi fruits
-
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Adenocarcinoma
Establishment and characterization of a novel human myoepithelial cell line and matrix-producing xenograft from a parotid basal cell adenocarcinoma.
Asthma
Identification of the main allergen sensitizers in an Iran asthmatic population by molecular diagnosis.
Carcinoma
Establishment and characterization of a novel human myoepithelial cell line and matrix-producing xenograft from a parotid basal cell adenocarcinoma.
Carcinoma
The human myoepithelial cell exerts antiproliferative effects on breast carcinoma cells characterized by p21WAF1/CIP1 induction, G2/M arrest, and apoptosis.
Dehydration
Ozone fumigation for safety and quality of wine grapes in postharvest dehydration.
Dehydration
Pectin methylesterase, polyphenol oxidase and physicochemical properties of typical long-storage cherry tomatoes cultivated under water stress regime
Dehydration
Postharvest ethylene treatment affects berry dehydration, polyphenol and anthocyanin content by increasing the activity of cell wall enzymes in Aleatico wine grape
Dehydration
Use of pectinmethylesterase and calcium in osmotic dehydration and osmodehydrofreezing of strawberries
Diphtheria
Pollen ablation of transgenic tobacco plants by expression of the diphtheria toxin A-chain gene under the control of a putative pectin esterase promoter from Chinese cabbage.
Hepatitis B
Pectinesterase Inhibitor from Jelly Fig (Ficus awkeotsang Makino) Achene Inhibits Surface Antigen Expression by Human Hepatitis B Virus.
Hypersensitivity
A mutation in the Arabidopsis thaliana cell wall biosynthesis gene pectin methylesterase 3 as well as its aberrant expression cause hypersensitivity specifically to Zn.
Hypersensitivity
A recombinant Sal k 1 isoform as an alternative to the polymorphic allergen from Salsola kali pollen for allergy diagnosis.
Hypersensitivity
Pollensomes as Natural Vehicles for Pollen Allergens.
Infections
Changes in cell wall pectin and pectinase activity in apple and tomato fruits during Penicillium expansum infection
Infections
Developmentally regulated Arabidopsis thaliana susceptibility to tomato spotted wilt virus infection.
Infections
Effect of NaHCO
Infections
Mechanism of Cell Wall Polysaccharides Modification in Harvested 'Shatangju' Mandarin (Citrus reticulate Blanco) Fruit Caused by Penicillium italicum.
Infections
Pectin methylesterase is induced in Arabidopsis upon infection and is necessary for a successful colonization by necrotrophic pathogens.
Infections
Pyramiding PvPGIP2 and TAXI-III But Not PvPGIP2 and PMEI Enhances Resistance Against Fusarium graminearum.
Infections
Single-dose treatment with a humanized neutralizing antibody affords full protection of a human transgenic mouse model from lethal Middle East respiratory syndrome (MERS)-coronavirus infection.
Infections
The changes in pectin metabolism in flax infected with Fusarium.
Infections
The effect of infection with tobacco-mosaic virus on the levels of nitrogen, phosphorus, protease, and pectase in tobacco leaves and on their response to fertilizers.
Infections
The MAP Kinase Kinase Gene AbSte7 Regulates Multiple Aspects of Alternaria brassicicola Pathogenesis.
Infections
Transgenic expression of pectin methylesterase inhibitors limits tobamovirus spread in tobacco and Arabidopsis.
Infertility, Male
Pectin methylesterase inhibitor (PMEI) family can be related to male sterility in Chinese cabbage (Brassica rapa ssp. pekinensis).
Leukemia
Pectinesterase Inhibitor from Jelly Fig (Ficus awkeotsang Makino) Achene Induces Apoptosis of Human Leukemic U937 Cells.
Macular Degeneration
Clinically significant pseudophakic cystoid macular edema after bag-in-the-lens implantation.
Mycoses
Overexpression of pectin methylesterase inhibitors in Arabidopsis restricts fungal infection by Botrytis cinerea.
Mycoses
The ectopic expression of a pectin methyl esterase inhibitor increases pectin methyl esterification and limits fungal diseases in wheat.
Nematode Infections
Comparative serial analysis of gene expression of transcript profiles of tomato roots infected with cyst nematode.
Neoplasms
The human myoepithelial cell is a natural tumor suppressor.
Rhinitis, Allergic, Seasonal
A recombinant Sal k 1 isoform as an alternative to the polymorphic allergen from Salsola kali pollen for allergy diagnosis.
Virus Diseases
Systemic movement of a tobamovirus requires host cell pectin methylesterase.
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1 - 6
-
pH 1.0: about 75% of maximal activity, pH 6.0: about 35% of maximal activity, hydrolysis of low molecular pectic acid methyl ester
2 - 5
-
about 75% of maximal activity at pH 2.0 and at pH 5.0, hydrolysis of pectin
3.3 - 4.2
over 70% of maximal activity within this range
3.5 - 5.5
-
about 50% activity at pH 3.5 and pH 5.5
4 - 6.5
-
pH 4.0: about 45% of maximal activity, pH 6.5: about 50% of maximal activity, pectin hydrolase II
4 - 8
-
pH 4: 24% of maximal activity, pH 8: 98% of maximal activity, no activity at pH 9, isoenzyme PE II
4 - 9
-
very low activity at pH 4, sudden increase of activity at higher pH up to pH 7, slight decrease of activity at higher pH
4.5 - 5
-
about 90% activity at pH 4.5,4.6, and 4.8, 100% activity at pH 4.7, about 60% activity at pH 4.9, about 50% activity at pH 5.0
4.5 - 8.5
Acrocylindrium sp.
-
pH 4.5: about 75% of maximal activity, pH 8.5: about 80% of maximal activity
4.5 - 9
-
rapid increase of activity between pH 4.5-6.5, low loss of activity at pH values above 7.5, 83% of maximum activity at pH 9.0
4.7 - 9
-
pH 4.7: about 45% of maximal activity, pH 9.0: about 65% of maximal activity
4.8 - 6.8
-
about 55% of maximal activity at pH 4.8 and at pH 6.8, pectin hydrolase I
5 - 6
-
about 55% activity at pH 5-6
5 - 9
-
pH 5: 58% of maximal activity, pH 9: 64% of maximal activity, isoenzyme PE I
5.2 - 7.6
-
pH 5.2: about 75% of maximal activity, pH 7.6: about 70% of maximal activity
5.6 - 7.6
isoform alpha activity is similar at pH 5.6 and pH 7.6, isoform gamma activity is higher at pH 5.6
6 - 10
-
about 70% of maximal activity at pH 6.0 and at pH 10.0
6 - 7
Cucumis sativa
-
maximum stability
6 - 9.5
-
no enzyme activity below pH 6 at 50 mM NaCl, minimal level of activity at 10 mM NaCl between pH 7.5 and 9.5, no enzyme activity at 10 mM below pH 7.5
6.5 - 8.5
-
pH 6.5: about 50% of maximal activity, pH 8.5: about 60% of maximal activity
6.5 - 9
over 50% of maximal activity within this range
7.5 - 11
-
pH 7.5: about 50% of maximal activity, pH 11.0: about 85% of maximal activity
3 - 9
-
-
3 - 9
-
poor activity at pH 3.0 to pH 5.0, slight activity at pH 6.0, optimum range at pH 7.0 to pH 9.0 with an activity maximum at pH 8.0
3 - 9
-
poor activity at pH 3.0 to pH 5.0, slight activity at pH 6.0, optimum range at pH 7.0 to pH 9.0 with an activity maximum at pH 8.0
3.5 - 4.5
-
-
4.5 - 8
-
pH-dependent activity pattern, pH-profile, overview
4.5 - 8
-
pH-dependent activity pattern, pH-profile, overview
4.5 - 9.5
-
4.5 - 9.5
-
at pH 4.5 no activity without added NaCl or in the presence of 25 mM NaCl, activity detected in the presence of 200 mM NaCl, at pH 6.5 no activity without added NaCl, activity detected in the presence of 25 or 200 mM NaCl, at pH 7.5 activity detected with and without added NaCl, at pH 9.5 maximum activity without added NaCl or in the presence of 25 mM NaCl, significantly lower activity in the presence of 200 mM NaCl
5 - 10
-
less than 50% of activity at pH 5 and 10
5 - 10
-
no activity at pH 5, sudden increase of activity at higher pH up to pH 8, strong decrease of activity at pH 10
5 - 10
-
no activity at pH 5, sudden increase of activity at higher pH up to pH 8, strong decrease of activity at pH 10
6 - 9
-
pH 6.0: about 40% of maximal activity, pH 9.0: about 70% of maximal activity
6 - 9
inactive at pH 5.0 and above pH 10.0, over 90% of maximal activity at pH 6.0-8.0
7 - 10
-
high activity is observed between pH 7.0 and 10.0
7 - 10
-
high activity is observed between pH 7.010.0
7 - 10
-
high activity is observed between pH 7.0 and 10.0
7 - 8
over 70% of maximal activity in a narrow pH range with the maximal activity occurring at pH 7.5, whereas enzyme activity at lower and higher pH values is very low
7 - 8
-
pH 7.0: about 35% of maximal activity, pH 8.0: about 25% of maximal activity
additional information
at pH 7.0 and above in the presence of 100 mM NaCl, Ani-PME2 is nearly inactive
additional information
-
at pH 7.0 and above in the presence of 100 mM NaCl, Ani-PME2 is nearly inactive
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-
-
brenda
-
low activity
brenda
low expression of PME31
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
low activity
brenda
-
brenda
gene PME34 is highly expressed in guard cells and in response to the phytohormone abscisic acid
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
germinating shoot, 1 month old shoot, and young culm
brenda
-
-
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
-
recombinant enzyme
brenda
-
brenda
-
-
brenda
-
highest activity
brenda
-
highest activity
brenda
-
highest activity
brenda
-
-
brenda
pectin methylesterase activity is present before the onset of veraison and increases during skin maturation
brenda
moderate to lower expression of PME31
brenda
-
moderate to lower expression of PME31
-
brenda
-
-
brenda
-
brenda
-
-
brenda
-
Easy Pick and Hard Pick fruits with different states of pectin polymerization, higher activity in immature than in mature fruits
brenda
-
ripe var. Easy Pick fruit is characterized by pectin ultradegradation and easy fruit detachment from the calyx, while pectin depolymerization and dissolution in ripe var. Hard Pick fruit is limited, PME activity in vivo is detected only in fruit of the Easy Pick line and is associated with decreased pectin methylesterification, some PME isozymes are apparently inactive in vivo, particularly in green fruit and throughout ripening in the Hard Pick line, overview
brenda
-
-
brenda
esocarp-exocarp tissue of unripe fruits, decreasing activity of PME from ripe to senescence stage fruits
brenda
-
-
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juice
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Citrus reticulata Citrus sinensis
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juice
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juice
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rag tissue
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isoform PME1 is a minor citrus fruit thermolabile pectin methylesterase
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isoform PME2 is the major thermolabile pectin methylesterase isoenzyme accumulated in citrus pulp tissue
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maximum PME activity is detected in green fruits and steadily decreases to reach a minimum in senescent fruits
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PME activity increases with fruit maturation
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the fruits pass from the ripe to overripe stage with increased pectin hydrolysis
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isoenzyme A is the predominant enzyme form
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young developing, isozyme profile, expression analysis, overview
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isoenzyme B and C in comparable amounts
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Citrus reticulata Citrus sinensis
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low activity
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PME occurs in cream, pellet, and serum layers
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PME occurs in cream, pellet, and serum layers
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very low expression of PME31
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very low expression of PME31
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neutral PME activity is the major isozyme in control and hyperhydric leaves of the three varieties, whilst a decrease in the activity of the acidic isoforms is observed in hyperhydric leaves, high activity in hyperhydrated leaves
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photosynthetic active and vascular tissues
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2 month old leaf and flag leaf
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isozyme profile, expression analysis, overview
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pollen specific PME detected exclusively in mature pollen and not in any other tissue examined, high activity in pollen tube
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O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6 tube, the enzyme belongs to the group I of pectinesterases in Arabidopsis thaliana pollen
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O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6 tube, the enzyme belongs to the group II of pectinesterases in Arabidopsis thaliana pollen
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the enzyme is expressed in pollen grains from 4 days before anthesis till anther dehiscence and in pollinated carpels
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higher activity in pulp than in juice, relatively low activity in Navel oranges compared with the other strains
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germinating root, 1 month old root, and 2 month old root
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isoenzyme C is the predominant enzyme form
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enzyme PME31 is highly expressed in dry seeds
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enzyme PME31 is highly expressed in dry seeds
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low expression of PME31
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low expression of PME31
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highest expression in the basal part of the inflorescence stem
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low expression of PME31
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low expression of PME31
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tissues active in secondary growth and during dormancy, PME1 expression patterns, overview
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additional information
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isoform PME3 is ubiquitously expressed in Arabidopsis thaliana, particularly in vascular tissues
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additional information
analysis of seed anatomy and embryo cell sizes throughout development of wild-type and hms-1 mutant
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additional information
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highest activity was observed in germinating tissues, young culm, and spikelets, where cells are actively elongating. PMEs exhibit spatial- and stress-specific expression patterns during rice development. Rice PMEs and tissue-specific transcriptional analysis, overview
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additional information
no expression is located in other vegetative or floral tissues
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additional information
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no expression is located in other vegetative or floral tissues
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additional information
isoform PE2 expression is not detected in tissues surrounding seeds, such as locular tissue, seed, placenta, and core
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additional information
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isoform PE2 expression is not detected in tissues surrounding seeds, such as locular tissue, seed, placenta, and core
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additional information
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the highest PME activity is detected in samples isolated from green fruits, whereas soluble proteins isolated from green and red fruit possess the lowest PMEI inhibitor activity. Root and stems possess high PME activities, while low activities are detected in leaf tissues, suggesting that vegetative tissues also undergo dynamic pectin modification
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additional information
no difference in the expression of pmt gene by laboratory wild-type Xoo strain (BXO43) grown in either nutrient rich PS medium or in plant mimic XOM2 medium
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additional information
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no difference in the expression of pmt gene by laboratory wild-type Xoo strain (BXO43) grown in either nutrient rich PS medium or in plant mimic XOM2 medium
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additional information
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no difference in the expression of pmt gene by laboratory wild-type Xoo strain (BXO43) grown in either nutrient rich PS medium or in plant mimic XOM2 medium
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additional information
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no difference in the expression of pmt gene by laboratory wild-type Xoo strain (BXO43) grown in either nutrient rich PS medium or in plant mimic XOM2 medium
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additional information
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no difference in the expression of pmt gene by laboratory wild-type Xoo strain (BXO43) grown in either nutrient rich PS medium or in plant mimic XOM2 medium
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evolution
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depending on the presence or absence of the PME inhibitor (PMEI) domain at the N-terminus (also known as the PRO region), PMEs are grouped into either type-1 PME (with PMEI domain) or type-2 PME (without PMEI domain), phylogenetic analysis
evolution
in Arabidopsis thaliana, 66 PMEs and a similarly high number of pectin methylesterase inhibitors, PMEIs, have so far been identified
evolution
sequence comparisons of pectinesterase enzymes from Citrus sinensis, Arabidopsis thaliana, and Botrytis cinerea
evolution
sequence comparisons of pectinesterase enzymes from Citrus sinensis, Arabidopsis thaliana, and Botrytis cinerea
evolution
sequence comparisons of pectinesterase enzymes from Citrus sinensis, Arabidopsis thaliana, and Botrytis cinerea
evolution
the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8
evolution
the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
evolution
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the enzyme belongs to the family of class 8 carbohydrate esterases. PMEs are classified into either Type-1 (with a PMEI domain at the N-terminus) or Type-2 (no PMEI domain). The highest PME activity is detected in samples isolated from green fruits, whereas soluble proteins isolated from green and red fruit possess the lowest PMEI inhibitor activity. Root and stems possess high PME activities, while low activities are detected in leaf tissues, suggesting that vegetative tissues also undergo dynamic pectin modification
evolution
thermostable pectin methylesterase (CtPME) from Clostridium thermocellum belongs to family 8 carbohydrate esterase (CE8)
evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8
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evolution
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in Arabidopsis thaliana, 66 PMEs and a similarly high number of pectin methylesterase inhibitors, PMEIs, have so far been identified
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evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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thermostable pectin methylesterase (CtPME) from Clostridium thermocellum belongs to family 8 carbohydrate esterase (CE8)
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evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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the enzyme belongs to the family 8 of carbohydrate esterases (CE8) of the pectin methylesterase superfamily
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evolution
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sequence comparisons of pectinesterase enzymes from Citrus sinensis, Arabidopsis thaliana, and Botrytis cinerea
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malfunction
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the number of adventitious roots is 30% increased in the pme3-1 mutant
malfunction
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loss-of-function mutant alleles of pectin methylesterase35 show a pendant stem phenotype and an increased deformation rate of the stem
malfunction
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suppressing expression of PMEs in tomato fruit reduces the amount of Ca2+ bound to the cell wall, and also reduces fruit susceptibility to Blossom-end rot
malfunction
a defect in mucilage extrusion is observed in a PME6 mutant and is shown to be a pleiotropic effect of the changes in embryo. hms-1 Embryo defect phenotype, the embryo cell size is decreased, the hms-1 radicals and cotyledons both have a reduced cell perimeter compared with the wild-type, overview. The PME activity is decreased and the degree of methyl esterification is increased in hms-1 7-DPA mutant seeds
malfunction
Atpme3-1 loss-of-function mutants exhibit phenotypes distinct from the wild-type, and show earlier germination and reduction of root hair production, correlated with the accumulation of a 21.5-kDa protein in the different organs of 4-day-old Atpme3-1 seedlings grown in the dark, as well as in 6-week-old mutant plants. Microarray analysis shows significant downregulation of the genes encoding several pectin-degrading enzymes and enzymes involved in lipid and protein metabolism in the hypocotyl of 4-day-old dark grown mutant seedlings. Accordingly, there is a decrease in proteolytic activity of the mutant as compared with the wild-type. Among the genes specifying seed storage proteins, two encoding cruciferins are upregulated. Overexpression of four cruciferin genes in the mutant Atpme3-1, in which precursors of the alpha- and beta-subunits of CRUCIFERIN accumulate
malfunction
expression analysis of enzyme inhibiting PMEI genes in response to male sterility, overview
malfunction
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inhibition of the activation of the enzyme PME retardes the hydrolysis of pectin and texture softening during storage, e.g. by lowering pH and ethylene concentration
malfunction
mutations in the pglA, pmt, pel and pelL genes have minimal effects on virulence
malfunction
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mutations in the pglA, pmt, pel and pelL genes have minimal effects on virulence
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malfunction
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mutations in the pglA, pmt, pel and pelL genes have minimal effects on virulence
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malfunction
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Atpme3-1 loss-of-function mutants exhibit phenotypes distinct from the wild-type, and show earlier germination and reduction of root hair production, correlated with the accumulation of a 21.5-kDa protein in the different organs of 4-day-old Atpme3-1 seedlings grown in the dark, as well as in 6-week-old mutant plants. Microarray analysis shows significant downregulation of the genes encoding several pectin-degrading enzymes and enzymes involved in lipid and protein metabolism in the hypocotyl of 4-day-old dark grown mutant seedlings. Accordingly, there is a decrease in proteolytic activity of the mutant as compared with the wild-type. Among the genes specifying seed storage proteins, two encoding cruciferins are upregulated. Overexpression of four cruciferin genes in the mutant Atpme3-1, in which precursors of the alpha- and beta-subunits of CRUCIFERIN accumulate
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malfunction
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mutations in the pglA, pmt, pel and pelL genes have minimal effects on virulence
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metabolism
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the role of PME on CH4 efflux potential is examined. PME is found to substantially reduce the potential for aerobic CH4 emissions upon demethylation of pectin
metabolism
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the role of PME on CH4 efflux potential is examined. PME is found to substantially reduce the potential for aerobic CH4 emissions upon demethylation of pectin
metabolism
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the role of PME on CH4 efflux potential is examined. PME is found to substantially reduce the potential for aerobic CH4 emissions upon demethylation of pectin
metabolism
guard cell walls concerted with the action of cell-wall enzymes, acting on the cell wall polymers for stomatal movements, regulation, overview
physiological function
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compared to six fruit rot fungi, Aspergillus niger and Aspergillus flavus produce higher PME after 14 days of incubation and in both these species are responsible for higher PME after 4 days of incubation in grape juice extract
physiological function
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compared to six fruit rot fungi, Aspergillus niger and Aspergillus flavus produce higher PME after 14 days of incubation and in both these species are responsible ofr higher PME after 4 days of incubation period in grape juice extract
physiological function
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although foliar pectin methylesterase activity is related to methanol emission, other factors must also be considered when predicting methanol emission
physiological function
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in tubers containing a higher level of total PME activity, there is a reduced degree of methylation of cell wall pectin and consistently higher peak force and work done values during the fracture of cooked tuber samples
physiological function
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in tubers containing a higher level of total PME activity, there is a reduced degree of methylation of cell wall pectin and consistently higher peak force and work done values during the fracture of cooked tuber samples
physiological function
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isoform PME3 plays a role in adventitious rooting
physiological function
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the enzyme is involved in the metabolism (i.e., remodelling) of the cell-wall pectin and, hence, takes part in important physiological processes associated with both vegetative and reproductive plant development, including cell wall extension and stiffening, cellular adhesion and separation, fruit ripening, wood development, stem elongation, leaf growth, microsporogenesis, seed germination, and pollen tube growth. In addition, the enzyme is associated with plant defence responses upon biotic (including insect herbivory) or abiotic (e.g., cold, wounding) stresses. Pectin methylesterase is a ribosome-inactivating protein, inhibiting the translation process
physiological function
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the enzyme is involved in the metabolism (i.e., remodelling) of the cell-wall pectin and, hence, takes part in important physiological processes associated with both vegetative and reproductive plant development, including cell wall extension and stiffening, cellular adhesion and separation, fruit ripening, wood development, stem elongation, leaf growth, microsporogenesis, seed germination, and pollen tube growth. In addition, the enzyme is associated with plant defence responses upon biotic (including insect herbivory) or abiotic (e.g., cold, wounding) stresses. Pectin methylesterase is a ribosome-inactivating protein, inhibiting the translation process
physiological function
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the recovery of heat shock protein-released Ca2+ in Ca2+-pectate reconstitution through pectin methylesterase activity is required for cell wall remodelling during heat shock protein in soybean which, in turn, retains plasma membrane integrity and co-ordinates with heat shock proteins to confer thermotolerance
physiological function
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high expression of pectin methylesterases increases Ca2+ bound to the cell wall, subsequently decreasing Ca2+ available for other cellular functions and thereby increasing fruit susceptibility to Blossom-end rot
physiological function
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isoform PME3 acts as a susceptibility factor and is required for the initial colonization of the host tissue by Pectobacterium carotovorum and Botrytis cinerea
physiological function
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isoform PME35-mediated demethylesterification of the primary cell wall directly regulates the mechanical strength of the supporting tissue
physiological function
the enzyme catalyzes the de-methylesterification of pectin in plant cell walls during cell elongation
physiological function
Aspergillus niger contains a non-processive, salt-requiring, and acidophilic pectin methylesterase
physiological function
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enzyme pectin methylesterase catalyzes hydrolysis of the methoxyl group of pectins, producing pectin acid. The decrease in the degree of pectin methoxylation may, in turn, trigger various processes that can affect fruit texture and firmness. PME activity is related to fruit softening with the disintegration of the cell wall and modifications of the pectin fraction. Because their principal substrate is the methoxyl group of pectins, hydrolysis of these compounds occurs. The fruits pass from the ripe to overripe stage with increased pectin hydrolysis. Activity of pectin methylesterase affets the layer of candeuba wax solid lipid nanoparticles (SLN) and xanthan gum (XG, xanthan gum derived from Xanthomonas campestris) as coatings on guava fruits, that shall inhibit the maturation process of the fruits. The best results are achieved from the fruits coated with 65 g/L of SLN and stored at 10°C, as they show the lowest O2 and CO2 respiration rates and, consequently, less weight loss. They also have the best retention of ascorbic acid and total phenol content, with less change in fruit color compared to the control guava and those coated only with XG. These findings indicate that this batch continues the natural maturation process, but at a slower rate than the other samples. The firmness is affected by the activity of the enzyme pectin methylesterase, but results show that the 65 g/l coating is efficient in maintaining fruit texture. 75 g/l Coating produces epoxy compounds in the fruit, causing physiological damage, and the guava coated with XG only have a maturation rate similar to that of the control fruit. Coating with lower concentration of submicron particles presenting a greater firmness can be related to its higher total phenol content, phenolic-pectin interactions demonstrate conservation of cell wall integrity explained by the cross-linking between a hydroxycinnamic acid, such as gallic acid, and the polysaccharide, such as pectin, in the cell wall, which leads to the formation of esterified phenolic compounds. This crosslinking may increase plant cell wall rigidity which helps to preserve firmness
physiological function
functional properties of pectin rely on molecular weight and degree of esterification, and thus deesterification by PME influences the pectin functionality
physiological function
highly methyl esterified seeds' (gene PME6) is a pectin methyl esterase involved in embryo development, it is required for normal embryo development. Enzyme HMS causes the softening of plant tissues. Isozyme HMS plays an important role in embryo growth
physiological function
pectin is an important cell wall polysaccharide required for cellular adhesion, extension, and plant growth. The pectic methylesterification status of guard cell walls influences the movement of stomata in response to different stimuli. Pectin methylesterase (PME) has a profound effect on cell wall modification, especially on the degree of pectic methylesterification during heat response. Isozyme PME34 plays a significant role in heat tolerance through the regulation of stomatal movement, PME34 specifically regulates stomatal aperture in response to heat, overview. The opening and closure of stomata is mediated by changes in response to a given stimulus, might require a specific cell wall modifying enzyme to function properly
physiological function
pectin methylesterases (PMEs) are present in phytopathogens such as bacteria and fungi
physiological function
pectin methylesterases (PMEs) belonging to carbohydrate esterase family 8 cleave the ester bond between a galacturonic acid and an methyl group. The resulting change in methylesterification level plays an important role during the growth and development of plants. Optimal pectin methylesterification status in each cell type is determined by the balance between PME activity and posttranslational PME inhibition by PME inhibitors (PMEIs)
physiological function
pectin methylesterases (PMEs) play a central role in pectin remodeling during plant development
physiological function
pectin methylesterases (PMEs) play a central role in pectin remodeling during plant development
physiological function
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pectin, which is enriched in primary cell walls and middle lamellae, is an essential polysaccharide in all higher plants. Homogalacturonans (HGA), a major form of pectin, are synthesized and methylesterified by enzymes localized in the Golgi apparatus and transported into the cell wall. Depending on cell type, the degree and pattern of pectin methylesterification are strictly regulated by cell wall-localized pectin methylesterases (PMEs). The removal of methyl groups by PMEs play important roles in rice growth and development. Optimal pectin methylesterification status in each cell type is determined by the balance between PME activity and posttranslational PME inhibition by PME inhibitors (PMEIs)
physiological function
plant and bacterial pectin methylesterases (PMEs) perform the catalysis with a processive catalytic mechanism, unlike fungal PME whose activity leads to a random repartition of non-esterified carboxyl groups
physiological function
presence of four pectin homogalacturonan (HG) degrading genes in the genome of Xoo. The four HG degrading genes include one polygalacturonase (pglA), one pectin methyl esterase (pmt) and two pectate lyases (pel and pelL). PglA is the major pectin degrading enzyme produced by Xoo. The pectin methyl esterase, Pmt, is the pectin deesterifying enzyme secreted by Xoo as evident from the enzymatic activity assay performed using pectin as the substrate. Compared to cellulases and xylanases, the HG degrading enzymes may not have a major role in the pathogenicity of strain BXO43
physiological function
regulation of enzyme PME may control the physical properties and structure of the plant cell wall. Evidence for a link between AtPME3, present in the cell wall, and CRUCIFERIN metabolism that occurs in vacuoles is provided
physiological function
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presence of four pectin homogalacturonan (HG) degrading genes in the genome of Xoo. The four HG degrading genes include one polygalacturonase (pglA), one pectin methyl esterase (pmt) and two pectate lyases (pel and pelL). PglA is the major pectin degrading enzyme produced by Xoo. The pectin methyl esterase, Pmt, is the pectin deesterifying enzyme secreted by Xoo as evident from the enzymatic activity assay performed using pectin as the substrate. Compared to cellulases and xylanases, the HG degrading enzymes may not have a major role in the pathogenicity of strain BXO43
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physiological function
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presence of four pectin homogalacturonan (HG) degrading genes in the genome of Xoo. The four HG degrading genes include one polygalacturonase (pglA), one pectin methyl esterase (pmt) and two pectate lyases (pel and pelL). PglA is the major pectin degrading enzyme produced by Xoo. The pectin methyl esterase, Pmt, is the pectin deesterifying enzyme secreted by Xoo as evident from the enzymatic activity assay performed using pectin as the substrate. Compared to cellulases and xylanases, the HG degrading enzymes may not have a major role in the pathogenicity of strain BXO43
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physiological function
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regulation of enzyme PME may control the physical properties and structure of the plant cell wall. Evidence for a link between AtPME3, present in the cell wall, and CRUCIFERIN metabolism that occurs in vacuoles is provided
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physiological function
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pectin methylesterases (PMEs) are present in phytopathogens such as bacteria and fungi
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physiological function
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presence of four pectin homogalacturonan (HG) degrading genes in the genome of Xoo. The four HG degrading genes include one polygalacturonase (pglA), one pectin methyl esterase (pmt) and two pectate lyases (pel and pelL). PglA is the major pectin degrading enzyme produced by Xoo. The pectin methyl esterase, Pmt, is the pectin deesterifying enzyme secreted by Xoo as evident from the enzymatic activity assay performed using pectin as the substrate. Compared to cellulases and xylanases, the HG degrading enzymes may not have a major role in the pathogenicity of strain BXO43
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additional information
analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
additional information
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meta-analysis of biotic stress responsive expression of Oryza sativa PMEs
additional information
molecular dynamics simulations and electrostatic potential calculations. The substrate-binding groove is negatively charged. Enzyme sequence and activity comparisons to processive pectin methylesterases, e.g. from Aspergillus (Emericella) nidulans and Trichoderma reesei (Hypocrea jecorina), overview. Detailed structure analysis of a fungal isozyme Ani-PME2, which, while preserving key active-site residues, has distinctly different loop structures and surface electrostatic potential compared with plant, bacterial, and insect PMEs, molecular dynamics simulations on Ani-PME2. Homology modeling of the structure of isozyme Ani-PME1
additional information
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molecular dynamics simulations and electrostatic potential calculations. The substrate-binding groove is negatively charged. Enzyme sequence and activity comparisons to processive pectin methylesterases, e.g. from Aspergillus (Emericella) nidulans and Trichoderma reesei (Hypocrea jecorina), overview. Detailed structure analysis of a fungal isozyme Ani-PME2, which, while preserving key active-site residues, has distinctly different loop structures and surface electrostatic potential compared with plant, bacterial, and insect PMEs, molecular dynamics simulations on Ani-PME2. Homology modeling of the structure of isozyme Ani-PME1
additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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additional information
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analysis of the conserved and semi-conserved amino acid residues, homology modelling of CtPME structure reveals a characteristic right handed parallel alpha-helices, structure comparisons, overview. Molecular dynamic simulation of CtPME modelled structure, docking study of CtPME. Active site and ligand binding structures
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100000
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isoenzyme I, gel filtration
13000
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bands of 37000, 27000, and 13000 Da are detected in crude PME extract, SDS-PAGE
25100
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isozyme PME1, gel filtration
28500
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isoenzyme PE II from seed hull, gel filtration
30000
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isoenzyme PE II from pod, gel filtration
32400
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1 * 32400, gel filtration
33300
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x * 33300, mature enzyme, estimated from SDS-PAGE
33792
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x * 33792, calculation from nucleotide sequence
34341
x * 34341, isoform PME4, MALDI-TOF mass spectrometry
34467
x * 34467, isoform PME2, MALDI-TOF mass spectrometry
34485
x * 34485, isoform PME1, MALDI-TOF mass spectrometry
35000 - 37000
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isoenzyme PE II, gel filtration
35400
calculated from amino acid sequence
35900
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x * 35900, isoenzyme A, SDS-PAGE
36000
-
bands of 37000, 27000, and 13000 Da are detected in crude PME extract, SDS-PAGE
36900
x * 36900, isoform PME2, calculated from amino acid sequence
37214
x * 40000, native enzyme, SDS-PAGE, x * 37214, native glycosylated enzyme, mass spectrometry
37386
x * 37386, isoform Ole e 11.0101, calculated from amino acid sequence
37500
-
x * 37500, SDS-PAGE
37800
x * 37800, isoform PME8, calculated from amino acid sequence
37900
x * 37900, isoform PME5, calculated from amino acid sequence
38200
x * 38200, isoform PME6, calculated from amino acid sequence
39647
x * 39647, recombinant enzyme, calculated from amino acid sequence
400000
Clostridium multifermentans
-
-
40300
-
x * 40300, isoenzyme B, SDS-PAGE
40800
-
x * 40800, SDS-PAGE
42000
the three PME isoforms show the same molecular weight of 42000 Da, SDS-PAGE
43200
-
x * 43200, isoenzyme C, SDS-PAGE
44000
-
isoenzyme PE I from seed hull, gel filtration
47000
-
isoform II, SDS-PAGE
47900
-
x * 47900, one of two principal glycoisoforms, MALDI-TOF mass spectrometry
5200
-
isozyme PME2, gel filtration
55000
-
x * 55000, SDS-PAGE
56000
isoform luPME1: 2 * 56000, SDS-PAGE, isoform luPME3: 2 * 58000, SDS-PAGE
57000
-
guava PME contains two isoforms, one with 57000 Da molecular mass, SDS-PAGE
58000
isoform luPME1: 2 * 56000, SDS-PAGE, isoform luPME3: 2 * 58000, SDS-PAGE
60300
-
x * 60300, calculated from the deduced amino acid sequence of the pre-pro-protein
65570
x * 65570, calculated from amino acid sequence
99000
-
guava PME contains two isoforms, one with 99000 Da molecular mass, SDS-PAGE
110000
-
isoenzyme II, gel filtration
110000
gel filtration, neutral and basic isoform
27000
-
-
27000
-
bands of 37000, 27000, and 13000 Da are detected in crude PME extract, SDS-PAGE
33000
SDS-PAGE
33000
-
x * 33000, SDS-PAGE
33000
-
x * 33000, SDS-PAGE
33000
-
x * 33000, SDS-PAGE
33000
-
x * 33000, SDS-PAGE, two different bands detected by SDS-PAGE
33500
-
SDS-PAGE
33500
-
two bands: 33500 Da and 43000 Da, SDS-PAGE
34000
-
gel filtration
34000
-
x * 34000, SDS-PAGE
34000
x * 34000, SDS-PAGE
35000
-
-
35000
x * 35000, isoform PME2, SDS-PAGE
36200
-
isoenzyme I and II, gel filtration
36200
x * 36200, isoform PME3, calculated from amino acid sequence
37000
-
gel filtration
37000
-
x * 37000, SDS-PAGE, two different bands detected by SDS-PAGE
37700
x * 37700, isoform PME1, calculated from amino acid sequence
37700
x * 37700, isoform PME7, calculated from amino acid sequence
37700
x * 37700, isoform PME9, calculated from amino acid sequence
38000
-
SDS-PAGE
38000
gel filtration, very basic isoform, i.e. luPME5
38000
-
x * 38000, SDS-PAGE
38000
-
x * 38000, SDS-PAGE, protein from host
38100
x * 38100, isoform PME4, calculated from amino acid sequence
38100
-
x * 38100, calculated from amino acid sequence
40000
-
x * 40000, SDS-PAGE
40000
-
x * 40000, SDS-PAGE
40000
-
1 * 40000, isoenzyme PE II, SDS-PAGE
40000
x * 40000, recombinant enzyme, SDS-PAGE
40000
x * 40000, native enzyme, SDS-PAGE, x * 37214, native glycosylated enzyme, mass spectrometry
41000
-
SDS-PAGE
41000
-
x * 41000, SDS-PAGE
43000
-
two bands: 33500 Da and 43000 Da, SDS-PAGE
43000
-
x * 43000, isoenzyme I, SDS-PAGE
45000
-
isoenzyme PE I, gel filtration
45000
-
x * 45000, SDS-PAGE
45000
-
x * 45000, SDS-PAGE, recombinant protein
46000
-
isoenzyme PE I from pod, gel filtration
46000
-
isoform I, SDS-PAGE
50000
-
gel filtration
50000
purified enzyme, SDS-PAGE
50000
x * 50000, SDS-PAGE
53000
-
gel filtration
53000
-
x * 53000, one of two principal glycoisoforms, MALDI-TOF mass spectrometry
additional information
-
-
additional information
-
-
additional information
-
primary structure
additional information
-
linear arrangement of disulfide bridges along the polypeptide chain with two consecutive disulfide bridges, disulfide bridges connect Cys98 with Cys125 and Cys166 with Cys200
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dimer
isoform luPME1: 2 * 56000, SDS-PAGE, isoform luPME3: 2 * 58000, SDS-PAGE
?
x * 35558, recombinant His6-tagged enzyme, MALDI-TOF mass spectrometry
?
-
x * 35558, recombinant His6-tagged enzyme, MALDI-TOF mass spectrometry
-
?
x * 40000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 33300, mature enzyme, estimated from SDS-PAGE
?
-
x * 40000, SDS-PAGE
-
?
x * 37000, recombinant enzyme, SDS-PAGE, x * 34800, sequence calculation
?
-
x * 37000, recombinant enzyme, SDS-PAGE, x * 34800, sequence calculation
-
?
-
x * 33792, calculation from nucleotide sequence
?
-
x * 33792, calculation from nucleotide sequence
-
?
x * 37000, recombinant enzyme, SDS-PAGE
?
-
x * 37000, recombinant enzyme, SDS-PAGE
-
?
-
x * 33000, SDS-PAGE, two different bands detected by SDS-PAGE
?
-
x * 37000, SDS-PAGE, two different bands detected by SDS-PAGE
?
x * 27000, native enzyme, SDS-PAGE
?
-
three different isoforms with molecular weights of 75000, 83000, and 91000 detected in SDS-PAGE
?
x * 34341, isoform PME4, MALDI-TOF mass spectrometry
?
x * 34467, isoform PME2, MALDI-TOF mass spectrometry
?
x * 34485, isoform PME1, MALDI-TOF mass spectrometry
?
x * 35000, isoform PME2, SDS-PAGE
?
-
x * 47900, one of two principal glycoisoforms, MALDI-TOF mass spectrometry
?
-
x * 53000, one of two principal glycoisoforms, MALDI-TOF mass spectrometry
?
-
x * 38000, SDS-PAGE, protein from host
?
-
x * 45000, SDS-PAGE, recombinant protein
?
x * 40000, native enzyme, SDS-PAGE, x * 37214, native glycosylated enzyme, mass spectrometry
?
-
x * 43000, isoenzyme I, SDS-PAGE
?
-
x * 39000-41500, calculated from the deduced amino acid sequence for the mature protein
?
-
x * 60300, calculated from the deduced amino acid sequence of the pre-pro-protein
?
x * 40000, recombinant enzyme, SDS-PAGE
?
x * 37386, isoform Ole e 11.0101, calculated from amino acid sequence
?
x * 39647, recombinant enzyme, calculated from amino acid sequence
?
-
x * 38100, calculated from amino acid sequence
?
-
x * 55000, SDS-PAGE
-
?
-
x * 38100, calculated from amino acid sequence
-
?
x * 36200, isoform PME3, calculated from amino acid sequence
?
x * 36900, isoform PME2, calculated from amino acid sequence
?
x * 37700, isoform PME1, calculated from amino acid sequence
?
x * 37700, isoform PME7, calculated from amino acid sequence
?
x * 37700, isoform PME9, calculated from amino acid sequence
?
x * 37800, isoform PME8, calculated from amino acid sequence
?
x * 37900, isoform PME5, calculated from amino acid sequence
?
x * 38100, isoform PME4, calculated from amino acid sequence
?
x * 38200, isoform PME6, calculated from amino acid sequence
?
-
x * 38200, isoform PME6, calculated from amino acid sequence
-
?
-
x * 37700, isoform PME1, calculated from amino acid sequence
-
?
-
x * 36900, isoform PME2, calculated from amino acid sequence
-
?
-
x * 36200, isoform PME3, calculated from amino acid sequence
-
?
-
x * 38100, isoform PME4, calculated from amino acid sequence
-
?
-
x * 37900, isoform PME5, calculated from amino acid sequence
-
?
-
x * 37700, isoform PME7, calculated from amino acid sequence
-
?
-
x * 37800, isoform PME8, calculated from amino acid sequence
-
?
-
x * 37700, isoform PME9, calculated from amino acid sequence
-
?
x * 65570, calculated from amino acid sequence
?
-
x * 35900, isoenzyme A, SDS-PAGE
?
-
x * 43200, isoenzyme C, SDS-PAGE
?
-
x * 40300, isoenzyme B, SDS-PAGE
?
-
x * 34500-35000, four isozymes, SDS-PAGE
?
x * 50000, about, recombinant His-tagged enzyme, SDS-PAGE
monomer
-
1 * 50000, SDS-PAGE, native mass by gel filtration
monomer
-
1 * 37000, SDS-PAGE
monomer
-
1 * 32400, gel filtration
monomer
-
1 * 37000, SDS-PAGE, native mass by gel filtration
monomer
-
1 * 38000, gel filtration
monomer
isoform luPME5, 1 * 34000-40000, SDS-PAGE
monomer
-
1 * 40000, isoenzyme PE II, SDS-PAGE
monomer
-
1 * 45000-48000, isoenzyme PE I, SDS-PAGE
additional information
analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
additional information
-
analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
additional information
peptide mass fingerprint is performed by MALDI-TOF MS in reflectron mode with small molecule molecular weight range (500-5000 Da)
additional information
-
peptide mass fingerprint is performed by MALDI-TOF MS in reflectron mode with small molecule molecular weight range (500-5000 Da)
additional information
-
analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
-
additional information
-
peptide mass fingerprint is performed by MALDI-TOF MS in reflectron mode with small molecule molecular weight range (500-5000 Da)
-
additional information
-
analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
-
additional information
-
analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
-
additional information
-
analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
-
additional information
-
analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
-
additional information
-
analysis of secondary structure of CtPME shows alpha-helices (3.1%), beta-sheets (40.1%) and random coils (56.9%). Three-dimensional enzyme structure analysis and structure comparisons, overview
-
additional information
-
primary structures of isozymes, structural and processing motifs, three-dimensional structure analysis, overview
additional information
structure analysis of the deglycosylated fungal isozyme Ani-PME2, which, while preserving key active-site residues, has distinctly different loop structures and surface electrostatic potential compared with plant, bacterial, and insect PMEs
additional information
-
structure analysis of the deglycosylated fungal isozyme Ani-PME2, which, while preserving key active-site residues, has distinctly different loop structures and surface electrostatic potential compared with plant, bacterial, and insect PMEs
additional information
the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8
additional information
-
the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8
additional information
-
the deduced PME-ZJ5A protein structure contains a catalytic domain and a putative N-terminal signal peptide (residues 1-19) of carbohydrate esterase family 8
-
additional information
three-dimensional structure analysis, overview
additional information
-
the enzyme possesses a parallel beta-helix architecture, three dimensional structure of PME, overview
additional information
model of the three-dimensional structure with conserved parallel beta-sheet coiled into a large, right-handed cylinder based on the structure of the Erwinia chrysantemi enzyme with PDB ID 1QJV, overview
additional information
-
model of the three-dimensional structure with conserved parallel beta-sheet coiled into a large, right-handed cylinder based on the structure of the Erwinia chrysantemi enzyme with PDB ID 1QJV, overview
additional information
-
structural and processing motifs, three-dimensional structure analysis, overview
additional information
-
structural and processing motifs, three-dimensional structure analysis, overview
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food industry
-
fruit juice industry
D178A
-
site-directed mutagenesis, inactive mutant
D199A
-
site-directed mutagenesis, inactive mutant
M306A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q153A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q177A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R267A
-
site-directed mutagenesis, inactive mutant
T272A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V198A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W269A
-
site-directed mutagenesis, inactive mutant
395A396A
-
an enzymatically inactive proPME mutant
additional information
-
the degree of methylesterification of galacturonic acids is affected in the pme3-1 mutant enzyme
additional information
analysis of allelic T-DNA insertional KO mutants of the enzyme, pme31-1 (SALK_074820) and pme31-2 (CS25163). The pme31 mutants are more sensitive to Na+ toxicity than the wild-type, the mutations in PME31 lead to salt hypersensitive phenotypes, overview. The cotyledon greening rate of pme31 mutants are significantly lower in the presence of NaCl and NaNO3, but not in the presence of KCl, KNO3, and osmotic stress, pme31 mutants are only sensitive to Na+ toxicity
additional information
construction of a hms-1 mutant from gene PME6 by a transposon insertion. The hms-1 embryo defect phenotype is caused by a mutation in HMS, molecular complementation is performed, phenotype overview. Analysis of a second hms allele, allele gabi-kat-278G11, i.e. hms-2. The T-DNA in hms-2 is inserted at 229 from the +1 site in the 5' UTR. The hms-2 mutant has no mucilage phenotype, and HMS transcript in hms-2 is comparable with the wild-type. No other alleles are available in the coding region of HMS
additional information
construction of Atpme3-1 loss-of-function mutants, phenotypes with earlier germination and reduction of root hair production compared to wild-type, overview. A PME isoform with a pI 9.6 is lacking in all organs of the Atpme3-1 mutant, and loss of AtPME3 activity in the mutant cotyledon triggers the expression of the other PME isoform migrating at gpI 9.2. Altered Genome regulation in the mutant, overview. Genes encoding proteins putatively involved in cell wall organization and remodeling are mainly downregulated in hypocotyls of the Atpme3-1 mutant. Atpme3-1 seedlings display no specific phenotype except an increased adventitious rooting
additional information
-
construction of Atpme3-1 loss-of-function mutants, phenotypes with earlier germination and reduction of root hair production compared to wild-type, overview. A PME isoform with a pI 9.6 is lacking in all organs of the Atpme3-1 mutant, and loss of AtPME3 activity in the mutant cotyledon triggers the expression of the other PME isoform migrating at gpI 9.2. Altered Genome regulation in the mutant, overview. Genes encoding proteins putatively involved in cell wall organization and remodeling are mainly downregulated in hypocotyls of the Atpme3-1 mutant. Atpme3-1 seedlings display no specific phenotype except an increased adventitious rooting
-
additional information
-
analysis of allelic T-DNA insertional KO mutants of the enzyme, pme31-1 (SALK_074820) and pme31-2 (CS25163). The pme31 mutants are more sensitive to Na+ toxicity than the wild-type, the mutations in PME31 lead to salt hypersensitive phenotypes, overview. The cotyledon greening rate of pme31 mutants are significantly lower in the presence of NaCl and NaNO3, but not in the presence of KCl, KNO3, and osmotic stress, pme31 mutants are only sensitive to Na+ toxicity
-
additional information
for a Ani-PME2 construct, Saccharomyces cerevisiae consensus sequence AAAAAAATG and alpha-mating factor, as well as a Kex cleavage site AAAAGA are added to the sequence
additional information
-
for a Ani-PME2 construct, Saccharomyces cerevisiae consensus sequence AAAAAAATG and alpha-mating factor, as well as a Kex cleavage site AAAAGA are added to the sequence
additional information
generation of a recessive genic male sterile mutant (ftms) in Chinese cabbage. This mutant is a doubled haploid line with stable inheritance, derived from Chinese cabbage FT generated through a combination of radiation mutagenesis and isolated microspore culture. The transcriptome profiles of the floral buds of ftms and its wild-type line FT are determined using RNA-seq. A total of 17 PMEI genes are differentially expressed, all of them are downregulated in ftms compared to their levels in wild-type FT
additional information
-
generation of a recessive genic male sterile mutant (ftms) in Chinese cabbage. This mutant is a doubled haploid line with stable inheritance, derived from Chinese cabbage FT generated through a combination of radiation mutagenesis and isolated microspore culture. The transcriptome profiles of the floral buds of ftms and its wild-type line FT are determined using RNA-seq. A total of 17 PMEI genes are differentially expressed, all of them are downregulated in ftms compared to their levels in wild-type FT
additional information
-
expression of proPME enhances the GFP transgene-induced gene silencing accompanied by relocation of the DCL1 protein from nucleus to the cytoplasm and activation of siRNAs and miRNAs production, inhibition of proPME gene expression stimulates the TMV vector reproduction, overview
additional information
up- and down-regulation of PME1 expression in transgenic aspen trees leads to correspondently altered PME activity in wood-forming tissues, transgenic trees have modified homogalacturonan methylesterification patterns, changes in pectin methylesterification in transgenic trees that are specifically localized in expanding wood cells, transgenic plant phenotypes, overview
additional information
pmeu1 gene silencing of the major salt-dependent isoform of pectinesterase in tomato alters fruit softening, but does not results in any detectable phenotype within the leaf tissue, overview
additional information
-
pmeu1 gene silencing of the major salt-dependent isoform of pectinesterase in tomato alters fruit softening, but does not results in any detectable phenotype within the leaf tissue, overview
additional information
construction of a enzyme-deficient pmt- mutant strain by gene disruption. A complementing strain (pmt-/pHM1+ pmt) expressing the Pmt protein from the overexpression vector pHM1 restored the pectin deesterifying activity and thus formed a red zone like wild-type strain
additional information
-
construction of a enzyme-deficient pmt- mutant strain by gene disruption. A complementing strain (pmt-/pHM1+ pmt) expressing the Pmt protein from the overexpression vector pHM1 restored the pectin deesterifying activity and thus formed a red zone like wild-type strain
additional information
-
construction of a enzyme-deficient pmt- mutant strain by gene disruption. A complementing strain (pmt-/pHM1+ pmt) expressing the Pmt protein from the overexpression vector pHM1 restored the pectin deesterifying activity and thus formed a red zone like wild-type strain
-
additional information
-
construction of a enzyme-deficient pmt- mutant strain by gene disruption. A complementing strain (pmt-/pHM1+ pmt) expressing the Pmt protein from the overexpression vector pHM1 restored the pectin deesterifying activity and thus formed a red zone like wild-type strain
-
additional information
-
construction of a enzyme-deficient pmt- mutant strain by gene disruption. A complementing strain (pmt-/pHM1+ pmt) expressing the Pmt protein from the overexpression vector pHM1 restored the pectin deesterifying activity and thus formed a red zone like wild-type strain
-
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10 - 20
purified recombinant enzyme, pH 3.8, 1 h, completely stable
100
cranberry
-
5-15 min, complete inactivation
106 - 125
-
only slight loss of activity when incubated for 5 min
30 - 50
-
extracellular enzyme in orange juice, loss of about 70% activity at 30-40°C, inactivation after 5 min, thermal inactivation kinetics, overview
30 - 55
-
incubation at 30°C has little but significant effect on enzyme activity, the incubation at 55°C abolishes over 95% of enzyme activity
30 - 70
the enzyme is completely stable at 40°C for 10 min, shows over 50% activity in the range of 30-45°C, and loses all of its activity at 80°C after 10 min, t1/2 at 60°C, 65°C, and 79°C is 18.9 min, 5.4 min, and 2.2 min, respectively, thermal inactivation kinetics
35 - 45
-
the residual activity of apple pectin methyl esterase under atmospheric pressure exhibits some fluctuations after mild heat at 35, 45, and 55°C, it seems that apple pectin methyl esterase is activated at 35 or 45°C, but the two temperatures have no significant effects on the residual activity as compared to the control sample, although the residual activity of apple pectin methyl esterase is reduced at 55°C as the treatment time increases, and a significant reduction of the residual activity is obtained after 30 min, the maximum reduction of apple pectin methyl esterase activity is still less than 20% for 60 min
35 - 50
purified recombinant enzyme, pH 3.8, 1 h, about 50% activity remaining
38
Clostridium multifermentans
-
5-15 min, inactivation
4 - 50
-
the enzyme is very stable at 4°C. At 50°C the enzyme is stable up to 2 h as it retains 70% of its activity
40 - 70
recombinant enzyme, CtPME retains 80% activity
42 - 62
-
freshly squeezed orange juices processed at temperatures of 62°C or above are characterized by minor residual enzyme activities, the juice processed at 52°C with a residual enzyme activity of 33.8% is hardly inferior in terms of cloud stability within the first 14 days, after the juice is processed at 42°C rapid clarification occurs within the first 8 days consistent with undetectable enzyme deactivation
45
-
10 min, 45% loss of maximal activity
5 - 45
enzyme Sl-PME remains stable up to 35°C, activity decreases by 25% at 40°C and is completely abolished at 45°C
50 - 91
-
In the case of orange pectin methyl esterase no inactivation is achieved below 50°C and around 8% remaining activity is found at 83°C. As for inactivation of purified orange PME around 6% remaining activity is found at 72.5°C. In orange juice-milk based beverages from 65 to 72.5°C only the labile pectin methyl esterase fraction is inactivated whereas the stable fraction does not inactivate. It is necessary to increase the temperature to 90°C for 1 min to inactivate the stable fraction. As for pectin methyl esterase inactivation in the orange juice-milk based beverage, no inactivation is found below 63°C for 5 min and around 3.5% remaining activity is found at 91°C.
54 - 63
-
inactivation rate constants increase with increasing temperature
55 - 80
-
z-values for thermal inactivation range from 5 to 6.5 °C, z-value: temperature increase necessary to obtain a 10fold decrease of the time needed for 90% reduction of enzyme activity
62
-
1 min, 50% inactivation
64
-
inactivation above at atmospheric pressure
65 - 80
PME I and PME III retain about the 80% of their activity after 4 min of incubation at 65°C, whereas PME II retains 60% of activity, PME I is more resistant at 80°C than the other PME isoforms, retaining about 9% of its activity after 30 s where PME II and PME III retain only 1% of their activity
68
-
more than 90% of activity lost within 5 min
73 - 88
-
z-values for thermal inactivation range from 11 to 27.8 °C, enzyme from tomato juice, z-value: temperature increase necessary to obtain a 10fold decrease of the time needed for 90% reduction of enzyme activity
80 - 85
the protein melting curve of CtPME gives a peak at 80°C. The peak is shifted to 85°C in the presence of 5 mM Ca2+ ions, and the addition of 5 mM EDTA shifts back the melting peak to 80°C
85 - 95
-
5% of activity after 5 min
95
-
no inactivation after 30 s, 51% loss of activity after 60 s
98
-
purified PME1 specific activity increases by 9.63% after 60 min incubation at 98°C, while purified PME2 retains 66% of its specific activity
30
Acrocylindrium sp.
-
-
30
Acrocylindrium sp.
-
24 h, pH 4.0-8.5, quite stable
30
-
the optimum temperature for the activity of pectimethylesterase is 30°C, however, within 10 min of heating approximately 50% loss of enzyme activity is lost, additional 10 min of heating results in retention of only 9% enzyme activity, and further heating results in complete loss of enzyme activity
30
-
57% loss of activity after 20 h at pH 1.1, 23% loss of activity after 20 h at pH 2.0
30
-
pectinesterase II is labile
30
-
inactivation kinetics, overview
30
-
inactivation kinetics, overview
40
-
30 min, pH 4.0-9.0, isoenzyme PE II is stable
40
-
16 min, in absence of substrate, stable up to
40
-
the enzyme remains stable for 1 h at 40°C
40
-
no loss of activity at atmospheric pressure and at pressures up to 700 MPa
50
-
43% loss of activity within 15 min at atmospheric pressure
50
-
pH 8.0, stable up to
50
-
60 min, 20% loss of activity
50
-
10 min, pH 8.0, about 45% loss of activity
50
-
240 min, pH 5.0, 1 h, 50% loss of activity
50
-
10 min, pH 3.0 or 10.0, complete inactivation
50
-
90% of activity remaining after 50 min
50
-
pH 6.0, 16 min, 50% loss of activity
50
-
no loss of activity after 20 min
50
-
no loss of activity within 2 h
50
-
10 min, 50% loss of activity
50 - 60
recombinant enzyme, CtPME retains 90% activity in the temperature range
50 - 60
-
thermal inactivation at 50°C for 1 and 2 min, shows a PME relative activity of 20 and 15% respectively, there is virtually no reduction of the relative activity of the enzyme heated to 60°C for 30 s
50 - 98
-
no loss of activity within 60 min
50 - 98
-
guava PME retains 96.8% of activity after 300 min in 90°C, retains 101.85% of its specific activity after 60 min of incubation at 50°C, the PME enzyme retains 75.4%, 86.2% and 90.4% of its specific activity after 60 min of incubation, respectively, at 80°C, 90°C, and 98°C
52 - 92
-
total pectin methylesterase activity rapidly declines between 52 and 72°C after 12 s incubation. Heating at temperatures above 72°C for 12 s inactivates the thermo-labile pectin methylesterase isoenzymes almost completely
52 - 92
-
total pectin methylesterase activity rapidly declines between 52 and 72°C after 12 s incubation. Heating at temperatures above 72°C for 12 s inactivates the thermo-labile pectin methylesterase isoenzymes almost completely
52 - 92
-
total pectin methylesterase activity rapidly declines between 52 and 72°C after 12 s incubation. Heating at temperatures above 72°C for 12 s inactivates the thermo-labile pectin methylesterase isoenzymes almost completely
55
Acrocylindrium sp.
-
-
55
Acrocylindrium sp.
-
stable
55
-
97% loss of activity within 15 min at atmospheric pressure, no inactivation at pressures above 200 MPa up to at least 700 MPa
55
-
incubation at 55°C, atmospheric pressure an pH 4.5 for 10 min, more than 90% loss of activity, more than 75% of activity remaining after 30 min at 100 MPa
55
-
no inactivation at pressures above 400 MPa up to at least 700 MPa
55
-
stable up to, sharp inactivation above
55
-
pH 4.0, inactivation
55
-
10 min, pH 4.0, inactivation
55
-
75% of activity after 60 min
55
-
rapid inactivation at temperatures above 55°C
55
-
almost 50% loss of activity after 5 min
55
-
5-15 min, inactivation
55
-
50% loss of activity after 5 min
55 - 60
-
at pH 5.0 and a high ionic strength (0.5 M), the enzyme shows a high thermostability (inactivation at temperatures above 60°C), an enhancement of its heat stability is observed at pH 7.0 and temperatures above 55°C, addition of NaCl increases the thermal stability at pH 5.0 and 7.0, while addition of CaCl2 has no influence, regarding the thermal stability in the presence of NaCl at neutral pH, there is complete inactivation at 65°C and no increase of stability at temperatures above 65°C, adding sugars and adding polyols has a positive effect on heat stability
55 - 60
purified recombinant enzyme, pH 3.8, 1 h, about 20% activity remaining
55 - 70
-
PME thermal degradation kinetics, modeling, overview
55 - 70
-
PME thermal degradation kinetics, modeling, overview
60
-
50% of activity lost within 5 min
60
purified native enzyme, 10 min, retaining 60% activity
60
-
45% of activity remaining after 8 min
60
-
complete loss of activity after 5 min
60
-
complete loss of activity after 2 min
60
-
10 min, inactivation
60
-
20 min, about 50% loss of activity of the soluble enzyme, about 20% loss of activity of the immobilized enzyme
60
-
inactivation at atmospheric pressure
60
-
15 min stable, loss of activity after 15 min
60
-
5 min, thermolabile isozyme, complete inactivation
60 - 80
Cucumis sativa
-
maximal thermostability in Bis-Tris buffer, pH 6.7, supplemented with 60% glycerol and 1.25 M NaCl
60 - 80
-
the enzyme retains more than 90% activity at 60°C for 60 min. At 70°C, the enzyme loses 46 and 61% activity in 30 and 60 min, respectively. Activity is completely abolished at 80°C after 5 min of incubation
60 - 80
-
the enzyme retains more than 90% activity at 60°C for 60 min. At 70°C, the enzyme loses 46 and 61% activity in 30 and 60 min, respectively. Activity is completely abolished at 80°C after 5 min of incubation
60 - 80
-
the enzyme retains more than 90% activity at 60°C for 60 min. At 70°C, the enzyme loses 46 and 61% activity in 30 and 60 min, respectively. Activity is completely abolished at 80°C after 5 min of incubation
60 - 80
-
maximal thermostability in citrate buffer, pH 4.5, supplemented with 50% glycerol, addition of sucrose and trehalose increase thermal stability
60 - 90
-
kinetic model for thermal inactivation of multiple PME, kinetics, at pH 3.5-4.5, overview
60 - 90
-
kinetic model for thermal inactivation of multiple PME, kinetics, at pH 3.5-4.5, overview
63 - 91
-
thermostability of the enzyme from juice of different cultivars, overview
63 - 91
Citrus reticulata Citrus sinensis
-
thermostability of the enzyme from juice of different cultivars, overview
63 - 91
-
thermostability of the enzyme from juice of different cultivars, overview
65
-
progressive loss of activity even at high pressure conditions
65
-
20 min, about 75% loss of activity of the soluble enzyme, about 20% loss of activity of the immobilized enzyme
65
-
complete loss of activity after 5 min
65
-
native enzyme stable for 30 min, 60% of activity remaining after 2 h
65
-
20 min, complete loss of activity of the soluble enzyme, about 50% loss of activity of the immobilized enzyme
70
Acrocylindrium sp.
-
-
70
Acrocylindrium sp.
-
10 min, complete inactivation
70
-
complete loss of activity within 5 min
70
following heating of a crude pulp tissue cell wall extract at 70°C, the activity for the purified isoform PME2 is rapidly lost
70
-
20% of activity remaining after 2 h
70
-
5-15 min, inactivation
70
-
activity decreases at temperatures above 70°C
70
-
5 min, 45% loss of activity
70
-
5 min, thermostable isozyme, complete inactivation
70 - 90
-
the immobilized pectinesterase retains 35% of its optimum activity whereas the free pectinesterase is 85% active at 70°C, the free and immobilized pectinesterases retain 40% and 30% of their optimum activities at 80°C, free and immobilized pectinesterase enzymes lose about 95% and 80% of their original activities at 90°C for 45 min
70 - 90
-
z-values for thermal inactivation range from 15 to 24 °C, purified enzyme, z-value: temperature increase necessary to obtain a 10fold decrease of the time needed for 90% reduction of enzyme activity
75
-
10% of activity after 60 min
75
-
increase in activity after 30 min of incubation
80
-
5 min, purified enzyme, inactivation
80
-
1 min, complete loss of activity
80
-
5-15 min, complete inactivation
80
-
2 min, 17% loss of activity
80
-
7.6% of activity remaining after 1 min
80
-
5-15 min, complete inactivation
80
-
5 min, partially purified enzyme, inactivation
85
purified enzyme, 10 min, inactivation
85
purified enzyme, 10 min, inactivation
85
-
5-15 min, inactivation
85
-
more than 50% of activity remaining after 1 min treatment, less than 10% of activity remaining after 3 min treatment
85
purified enzyme, 10 min, inactivation
90
-
complete inactivation within 1 min
90
-
slight loss of activity within the first 4 h of incubation, then activity increases and remains high until at least 8 h of total incubation time
90
Sclerotinia libertiana
-
5-15 min, inactivation
90
-
temperature required for total inactivation
90
-
5-15 min, inactivation
additional information
-
-
additional information
-
activity not completely abolished after pasteurization
additional information
-
immobilization stabilzes the enzyme
additional information
-
thermal and high-pressure inactivation kinetics of the two major isoenzymes, a thermolabile and a thermostable one, inactivation kinetics at pH 6.0 are accurately described by a first-order model, overview, the thermostable isoenzyme is pressure-stable, overview
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4 enzyme forms: A, B, C and D
-
affinity purification with immobilized pectin methylesterase-inhibitor protein
ammonium sulfate fractionation
-
ammonium sulfate precipitation
-
ammonium sulfate precipitation and DEAE cellulose column chromatography
-
ammonium sulfate precipitation and NH-Sepharose 4B PME-inhibitor column chromatography
-
ammonium sulfate precipitation and Ni-NTA agarose column chromatography
-
ammonium sulfate precipitation, dialysis, and DEAE-Sephadex gel filtration
-
ammonium sulfate precipitation, HisTrap column chromatography, and SOURCE 30Q column chromatography
-
ammonium sulfate precipitation, HiTrap Q column chromatography, and Resource S column chromatography
-
ammonium sulfate precipitation, Q Sepharose column chromatography, and Superdex 200 gel filtration
ammonium sulfate precipitation, Sephadex G-100 gel filtration, and Sephadex C-50 gel filtration
-
DE52 column chromatography, SP-Sepharose column chromatography, Mono-S column chromatography, and Superdex 75 gel filtration
DEAE-Sepharose column chromatography and PME-IP affinity chromatography
-
further purification of a commercial preparation by gel filtration
-
good results of purification is obtained on silanized CPG or keratin coated silica gel supports
-
heparin-Sepharose column chromatography, S-sepharose column chromatography, and Superdex-75 gel filtration
Hi-Trap SP column chromatography and heparin affinity column chromatography
-
homogeneity, one-step purification
-
isoenzyme PE I and isoenzyme PE II
-
isoenzyme PE I and PE II
-
isoenzyme PME I and PME II
-
native enzyme 10.6fold from unripe fruits by anion exchange chromatography and gel filtration
native enzyme from fruits partially by ammonium sufate fractionation and dialysis
native enzyme from pollen by gel filtration, anion exchange chromatography and isoelectric focusing
native enzyme partially from fruits by ammonium sulfate fractionation and dialysis
-
native enzyme partially, 5.8fold by cation exchange chromatography
-
native isozymes about 12fold by ammonium sulfate fractionation, PME inhibitor PMEI affinity chromatography, and cation exchange chromatography
-
native isozymes PME1 389fold and PME2 125fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
Ni-NTA column chromatography
Ni-NTA His-bind resin chromatography, DEAE-Sephadex gel filtration, CM-cellulose column chromatography, and Shephacryl SH-100 gel filtration
-
partial purification by ammonium sulfate precipitation and dialysis
-
partial, 3 isoenzymes: I, II and III
-
partial, isoenzyme PE I and PE II
-
partially purified by CS174 EBA resin column chromatography
-
pectinesterase I and II
-
phenyl Sepharose column chromatography and Sephacryl S100 gel filtration
recombinant enzyme from Pichia pastoris cell-free culture medium by anion exchange chromatography and ultrafiltration
recombinant enzyme from Pichia pastoris strain GS115
recombinant enzyme from Pichia pastoris strain GS115 culture medium by dialysis and anion exchange chromatography
recombinant His-tagged enzyme from pastoris strain KM71H by nickel affinity chromatography
recombinant His-tagged isozyme PME31 from Escherichia coli strain JM101 by nickel affinity chromatography
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by metal affinity chromatography and dialysis
recombinant protein and native protein from host
-
resource Q column chromatography
-
Superdex-75 gel filtration
-
two isoforms, homogeneity
-
-
-
ammonium sulfate precipitation, Q Sepharose column chromatography, and Superdex 200 gel filtration
-
ammonium sulfate precipitation, Q Sepharose column chromatography, and Superdex 200 gel filtration
-
ammonium sulfate precipitation, Q Sepharose column chromatography, and Superdex 200 gel filtration
-
partial
-
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diverse isozymes, DNA sequence anaylsis, phylogenetic tree, PME transcriptomes, overview
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli
DNA sequence anaylsis, overview
DNA sequence anaylsis, phylogenetic tree, overview
-
DNA sequence anaylsis,phylogenetic tree, PME transcriptomes, overview
-
DNA sequence and phylogenetic analysis
O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6
expressed as GFP-fusion protein in host strain, overexpression of PME results in reduced pollen tube growth
-
expressed in Escherichia coli
expressed in Escherichia coli strain JM101, IPTG induction at 37°C instead of 25-28°C results in approximately 10times less PME activity in the extract
-
expressed in Escherichia coli strain M15, the recombinant PME proteins (full-length and mature) do not show either PME or RIP activity
-
expressed in Escherichia coli Top10F' cells
-
expressed in Nicotiana benthamiana fused with the gene for the green fluorescent protein
-
expressed in Nicotiana tabacum fused with the gene for the green fluorescent protein
-
expressed in Pichia pastoris
expressed in Pichia pastoris as secretory protein
-
expressed in Pichia pastoris strain GS115
expressed in Pichia pastoris strain KM71
expression in Bacillus subtilis
-
expression of wild-type and mutant enzymes in Escherichia coli strain NM522
-
expression under the control of the CaMV 35S promoter in transgenic Nicotiana tabacum
-
gene Cthe_2949, DNA and amino acid sequence determination and analysis and tree, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene Cthe_2949, sequence comparisons and phylogenetic analysis
gene pme-zj5a, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression in Pichia pastoris strain GS115 to 71.11 U/ml after induction with methanol for 20 h at 30°C
gene PME3, quantitative real-time RT-PCR enzyme expression analysis
gene PME6, DNA and amino acid sequence determination and analysis, recombinant expression of YFP-tagged enzyme in the seed coat and cells of the embryos, the HMS-YFP fusions does not have enough HMS activity to compensate for the hms mutation
gene pmeB, DNA and amino acid sequence determination and analysis, recombinant expression in Pichia pastoris, the recombinant enzyme is secreted to the culture medium
gene Pmeu1 encodes a salt-dependent isozyme, expression of PMEU1 and the antisense construct in leaves and fruits of transgenic tomato plants, expression analysis, overview
gene pmt, quantitative realtime PCR expression analysis
in the tomato genome, there exists 79 PMEs with temporally and spatially regulated expression, quantitative realtime PCR expression analysis
-
overexpression in Escherichia coli
-
overexpression under control of the Aspergilus oryzae TEF1 promoter
-
recombinant expression in Pichia pastoris strain GS115, the enzyme is secreted to the culture medium
recombinant expression of wild-type enzyme and mutants in Nicotiana benthamiana leaves via the Agrobacterium tumefaciens strain GV3101 transfection method, quantitative RT-PCR enzyme expression analysis
recombinant overexpression of His-tagged isozyme PME31 in Escherichia coli strain JM101
sequence comparisons of 43 pme genes in Oryza sativa, and phylogenetic analysis
-
sequence comparisons, the Sl-pectinase ORF, excluding the coding sequence for signal peptide, is cloned in frame with His-tag into pPICZalphaA and pPICZalphaB expression vectors, recombinant overexpression in Pichia pastoris strain KM71H
transient co-expression of the tobacco enzyme with Tobacco mosaic virus TMV-GFP fusion protein in Nicotiana benthamiana plants via transfection mediated by Agrobacterium tumefaciens strain GV3110, the co-expression results in increased virus-induced RNA silencing with inhibition of GFP production, virus RNA degradation, stimulation of siRNAs production, overview
-
YFP-tagged protein expressed in host
-
expressed in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Pichia pastoris
-
expressed in Pichia pastoris
expressed in Pichia pastoris strain GS115
-
expressed in Pichia pastoris strain GS115
-
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diagnostics
pectin methylesterase is an allergenic marker for the sensitization to Russian thistle, Salsola kali pollen
food industry
-
added as exogenous enzyme in fruit and vegetable processing, used to increase the yield during extraction, to clarify and concentrate fruit juices, for gelation of fruit, and to modify texture and rheology of fruit and vegetable based products
food industry
-
destabilizes pectinaceous materials in fruit juices and concentrates and modifies the texture of fruit and vegetable products
food industry
-
enzyme is known to be responsible for cloud loss in juice processing and storage
food industry
-
enzyme is known to be responsible for cloud loss in juice processing and storage
food industry
-
enzyme is known to be responsible for cloud loss in juice processing and storage
food industry
-
one of the most important enzymes in the industrialization and preservation of fruits, juices or other industrial products that involve the presence or absence of intact pectin
food industry
-
responsible for phase separation and cloud loss in fruit juice manufacturing
food industry
-
responsible for phase separation and cloud loss in fruit juice manufacturing
food industry
-
used for juice clarification and gelation of frozen concentrates, destabilizing agent for pectin material in fruit juices and concentrates
food industry
-
used for various applications in fruit processing e.g. texture improvement of fruit pieces, juice extraction, concentration and clarification of fruit juices
food industry
-
PME has a higher thermal resistance than the bacteria and yeasts existing in orange juice, therefore its inactivation is used as a parameter to define the time/temperature combination of the thermal process of pasteurisation of orange juice, which is necessary to prevent spoilage, overview
food industry
-
PME has a higher thermal resistance than the bacteria and yeasts existing in orange juice, therefore its inactivation is used as a parameter to define the time/temperature combination of the thermal process of pasteurisation of orange juice, which is necessary to prevent spoilage, overview
food industry
-
inhibition of pectin methylesterase directly after juice extraction is crucial in the production of storable citrus juice products
food industry
-
PME (0.12% (v/v)) and Ca2+ (0.5% (w/w)) in osmotic sugar solutions positively affect the relative hardness of dehydrated strawberry fruits, which is ascribed to the effect of PME and Ca2+ on the cell wall strength of the tissue (no cell wall damage and tissue particle alterations are observed upon dehydration)
food industry
-
exogenous pectin methylesterase is applied in texture engineering of thermally processed intact fruits and vegetables, for example, via enzyme infusion
food industry
-
exogenous pectin methylesterase is applied in texture engineering of thermally processed intact fruits and vegetables, for example, via enzyme infusion
food industry
-
exogenous pectin methylesterase is applied in texture engineering of thermally processed intact fruits and vegetables, for example, via enzyme infusion
food industry
-
pectin methylesterase can positively or negatively affect structural quality of plant-based foods (cloud stability, viscosity, texture)
food industry
-
pectin methylesterase can positively or negatively affect structural quality of plant-based foods (cloud stability, viscosity, texture)
food industry
-
total pectin methylesterase activity is an indicator of freshness that is universally applicable to Citrus juices derived from orange, mandarin, and lemon or blends thereof
food industry
-
total pectin methylesterase activity is an indicator of freshness that is universally applicable to Citrus juices derived from orange, mandarin, and lemon or blends thereof
food industry
-
total pectin methylesterase activity is an indicator of freshness that is universally applicable to Citrus juices derived from orange, mandarin, and lemon or blends thereof
food industry
-
due to very high de-esterification activity, easy denaturation and significant efficacy in incrementing clarification of fruit juice makes the enzyme useful for industrial application
food industry
-
due to very high de-esterification activity, easy denaturation and significant efficacy in incrementing clarification of fruit juice makes the enzyme useful for industrial application
food industry
-
due to very high de-esterification activity, easy denaturation and significant efficacy in incrementing clarification of fruit juice makes the enzyme useful for industrial application
food industry
-
the enzyme enhances the pectin degradation process in apple juice clarification
food industry
pectin methylesterase (PME) is a ubiquitous cell wall enzyme, which de-esterifies and modifies pectins for food applications. The papaya PME can be potentially utilized to modify pectin functionality at elevated temperature
food industry
the enzyme is suitable for both acidic and alkaline processing, such as coffee and tea fermentation
food industry
-
study of kinetic characterization, thermal stability and synergistic effect of temperature and pH for peroxidase (POD) and pectin methylesterase (PME) in tomato puree. Inactivation of both enzymes is very important, since these enzymes can have very negative effects on the color, odor, flavor and texture of juices and vegetable beverages during storage. The browning and loss of stability in juices and vegetable beverages, such as tomato puree, can be controlled by applying temperature and pH combinations capable of inactivating these enzymes in a total or partial way, but while respecting the limits organoleptic and legal for juices and vegetable beverages
industry
CtPME can be potentially used in food and textile industry applications
industry
-
CtPME can be potentially used in food and textile industry applications
-