Any feedback?
Information on EC 3.1.1.11 - pectinesterase and Organism(s) Solanum lycopersicum and UniProt Accession P14280
for references in articles please use BRENDA:EC3.1.1.11Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.1.11 pectinesteraseSpecify your search results
Word Map
- 3.1.1.11
- polygalacturonase
- juice
- tomato
- orange
-
ripening
-
firmness
- citrus
-
softening
-
pectic
- pmeis
-
texture
- esterification
- pectate
- cellulase
-
methylesterification
-
postharvest
- pulp
- homogalacturonans
-
de-esterification
-
shelf
-
galacturonic
- hemicellulose
-
pectinolytic
- pectinases
-
cloud
-
de-esterified
-
pasteurization
- carrot
- valencia
-
kiwi
- xyloglucan
-
expansins
- food industry
-
methoxylated
- endo-polygalacturonase
- chrysanthemi
- oligogalacturonides
-
pollen-specific
-
blanch
-
ripening-related
-
wall-modifying
- ficus
-
pectin-degrading
- mango
- 1-methylcyclopropene
-
methyl-esterified
- endo-pg
- grapefruit
- rhamnogalacturonan
- achene
-
wall-degrading
- industry
- diagnostics
The taxonomic range for the selected organisms is: Solanum lycopersicum
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pectin methylesterase, pectinesterase, pectin methyl esterase, pectinmethylesterase, pectin esterase, pme i, sal k 1, atpme3, hms-1, pmeu1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
P65
-
-
-
-
PE
-
-
-
-
pectase
-
-
-
-
pectin demethoxylase
-
-
-
-
pectin methoxylase
-
-
-
-
pectin methyl esterase
pectin methylesterase
pectinoesterase
-
-
-
-
pectofoetidin
-
-
-
-
PME
pectin methyl esterase
-
-
-
-
pectin methylesterase
-
-
-
-
pectin methylesterase
-
-
PME
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
pectin pectylhydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9025-98-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pectin + H2O
?
-
the enzyme deesterifies methoxylated pectin in the plant cell wall
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
-
the enzyme deesterifies methoxylated pectin in the plant cell wall
-
-
?
pectin + H2O
methanol + pectate
-
-
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
NaCl
additional information
Ca2+
-
60 mM Ca2+ increases activity at elevated pressure up to 300 MPa, but decreases enzyme activity at atmospheric pressure and 45-60°C
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
Ca2+
-
60 mM Ca2+ decreases enzyme activity at atmospheric pressure and 45-60°C, but increases activity at elevated pressure up to 300 MPa
epigallocatechin gallate
-
natural inhibitor for pectin methyl esterase, acts as a non-specific pan-inhibitor for PME
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
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
low-temperature blanching of vegetables activates PME, which demethylates cell wall pectins and improves tissue firmness
-
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
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
-
at pH 4.4 and normal pressure, temperature optimum shifted to higher temperatures at higher pressure
45
50
55
60
-
longer exposure to this optimum temperatures resulted in inactivation of the enzyme
65 - 70
-
at 200-300 MPa, optimal reaction conditions in the presence of Ca2+
45
-
at pH 8 and normal pressure, temperature optimum shifted to higher temperatures at higher pressure
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-10
25 - 65
-10
-
sharp increase in reaction rate as the temperature approaches the melting temperature in the four model freeze systems including carboxymethylcellulose, fructose, maltodextrin or sucrose
-10
-
sharp increase in reaction rate as the temperature approaches the melting temperature, fructose, maltodextrin and sucrose enhance this effect
25 - 65
-
activity increases with increasing temperature up to 45°C and decreases above
25 - 65
-
the rate of de-esterification increases substantially with increasing temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
young developing, isozyme profile, expression analysis, overview
additional information
isoform PE2 expression is not detected in tissues surrounding seeds, such as locular tissue, seed, placenta, and core
additional information
-
isoform PE2 expression is not detected in tissues surrounding seeds, such as locular tissue, seed, placenta, and core
additional information
-
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
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
malfunction
-
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
physiological function
physiological function
-
although foliar pectin methylesterase activity is related to methanol emission, other factors must also be considered when predicting methanol emission
physiological function
-
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PME1_SOLLC
546
1
60066
Swiss-Prot
Secretory Pathway (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
no loss of activity at atmospheric pressure and at pressures up to 700 MPa
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
60
60 - 80
-
maximal thermostability in citrate buffer, pH 4.5, supplemented with 50% glycerol, addition of sucrose and trehalose increase thermal stability
65
-
20 min, complete loss of activity of the soluble enzyme, about 50% loss of activity of the immobilized enzyme
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
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
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
60
-
20 min, about 50% loss of activity of the soluble enzyme, about 20% loss of activity of the immobilized enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is very pressure resistant, inactivation at 900 MPa is slower as compared at atmospheric pressure
-
purified enzyme is more heat-stable than enzyme in fruit juice, enzyme is pressure-stable between 550 and 700 Mpa
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and DEAE cellulose column chromatography
-
native enzyme partially from fruits by ammonium sulfate fractionation and dialysis
-
native isozymes about 12fold by ammonium sulfate fractionation, PME inhibitor PMEI affinity chromatography, and cation exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression under the control of the CaMV 35S promoter in transgenic Nicotiana tabacum
-
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
in the tomato genome, there exists 79 PMEs with temporally and spatially regulated expression, quantitative realtime PCR expression analysis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
food industry
-
destabilizes pectinaceous materials in fruit juices and concentrates and modifies the texture of fruit and vegetable products
food industry
-
pectin methylesterase can positively or negatively affect structural quality of plant-based foods (cloud stability, viscosity, texture)
food industry
-
the enzyme enhances the pectin degradation process in apple juice clarification
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Markovic, O.; Jrnvall, H.
Pectinesterase. The primary structure of the tomato enzyme
Eur. J. Biochem.
158
455-462
1986
Solanum lycopersicum
Markovic, O.; Machova, E.
Immobilization of pectin esterase from tomatoes and Aspergillus foetidus on various supports
Collect. Czech. Chem. Commun.
50
2021-2027
1985
Aspergillus foetidus, Solanum lycopersicum
-
Versteeg, C.
Pectinesterases from the orange fruit - their purification, general characteristics and juice cloud destabilizating properties
Agric. Res. Rep. (Versl. Landbouwkd. Onderz.)
892
1-109
1979
Acrocylindrium sp., Allium cepa, Alternaria humicola, Alternaria infectoria, Aspergillus carbonarius, Aspergillus japonicus, Aspergillus niger, Athelia rolfsii, Avena sativa, Botrytis cinerea, Brassica oleracea, Capsicum annuum, Carica papaya, Chaetomium globosum, Citrus aurantiifolia, Citrus limon, Citrus nobilis, Citrus reticulata, Citrus sinensis, Citrus x paradisi, Clostridium aurantibutyricum, Clostridium multifermentans, Colletotrichum gloeosporioides, Colletotrichum trifolii, Coniella diplodiella, Corynebacterium sp., cranberry, Cucumis sativus, Curvularia lunata, Daucus carota, Diospyros sp., Epicoccum nigrum, Erwinia sp., Fragaria sp., Fusarium oxysporum, Fusarium sambucinum, Fusarium sp., Gaeumannomyces graminis, Gilbertella persicaria, Gymnoascus dankaliensis, Helianthus tuberosus, Hordeum vulgare, Kluyveromyces marxianus, Lasiodiplodia theobromae, Macrosporium cladosporioides, Malus sp., Medicago sativa, Monilinia fructicola, Musa acuminata, Neofusicoccum ribis, Nicotiana tabacum, Nigrospora sphaerica, Oculimacula yallundae, Oospora sp., Paecilomyces fulvus, Pellicularia filamentosa, Penicillium chrysogenum, Penicillium sp., Persea americana, Phaseolus vulgaris, Physalospora obtusa, Physalospora sp., Phytophthora infestans, Prunus armeniaca, Prunus avium, Prunus persica, Prunus sp., Psidium guajava, Pyrus communis, Ralstonia solanacearum, Raphanus sativus, Ribes sp., Rubus idaeus, Sclerotinia libertiana, Sclerotinia sclerotiorum, Secale cereale, Solanum lycopersicum, Solanum tuberosum, Stemphylium botryosum, Vicia faba, Syringa vulgaris, Thanatephorus cucumeris, Theobroma cacao, Torulopsis candida, Trichoderma viride, Trichothecium roseum, Triticum aestivum, Vitis sp., Xanthomonas citri pv. malvacearum
-
Markovic, O.
Tomato pectin esterase - characterization of one of its multiple forms
Collect. Czech. Chem. Commun.
39
908-913
1974
Solanum lycopersicum
-
Warrilow, A.G.S.; Turner, R.J.; Jones, M.G.
A novel form of pectinesterase in tomato
Phytochemistry
35
863-868
1994
Solanum lycopersicum
Gaffe, J.; Tiznado, M.E.; Handa, A.K.
Characterization and functional expression of a ubiquitously expressed tomato pectin methylesterase
Plant Physiol.
114
1547-1556
1997
Solanum lycopersicum
Markovic, O.; Jrnvall, H.
Disulfide bridges in tomato pectinesterase: variations from pectinesterases of other species; conservation of possible active site segments
Protein Sci.
1
1288-1292
1992
Solanum lycopersicum
Terefe, N.S.; Hendrickx, M.
Kinetics of the pectin methylesterase catalyzed de-esterification of pectin in frozen food model systems
Biotechnol. Prog.
18
221-228
2002
Solanum lycopersicum
Fachin, D.; Van Loey, A.M.; Nguyen, B.L.; Verlent, I.; Indrawati; Hendrickx, M.E.
Comparative Study of the inactivation kinetics of pectin methylesterase in tomato juice and purified form
Biotechnol. Prog.
18
739-744
2002
Solanum lycopersicum
Terefe, N.S.; Nhan, M.T.; Vallejo, D.; Van Loey, A.; Hendrickx, M.
Modeling the kinetics of the pectin methylesterase catalyzed de-esterfication of pectin in frozen systems
Biotechnol. Prog.
20
480-490
2004
Solanum lycopersicum
Guiavarc'h, Y.; Sila, D.; Duvetter, T.; Van Loey, A.; Hendrickx, M.
Influence of sugars and polyols on the thermal stability of purified tomato and cucumber pectinmethylesterases: a basis for TTI development
Enzyme Microb. Technol.
33
544-555
2003
Solanum lycopersicum, Cucumis sativa
-
Van Den Broeck, I.; Ludikhuyze, L.R.; Van Loey, A.M.; Hendrickx, M.E.
Effect of temperature and/or pressure on tomato pectinesterase activity
J. Agric. Food Chem.
48
551-558
2000
Solanum lycopersicum
Lee, C.W.; Wu, M.C.; Lee, B.H.; Jiang, C.M.; Chang, H.M.
Changes in molecular weight of transacylated pectin catalyzed by tomato and citrus pectinesterases as determined by gel permeation chromatography
J. Agric. Food Chem.
51
5455-5461
2003
Citrus sinensis, Solanum lycopersicum
Terefe, N.S.; Delele, M.A.; Van Loey, A.; Hendrickx, M.
Effects of cryostabilizers, low temperature, and freezing on the kinetics of the pectin methylesterase-catalyzed de-esterification of pectin
J. Agric. Food Chem.
53
2282-2288
2005
Solanum lycopersicum
Anthon, G.E.; Barrett, D.M.
Characterization of the temperature activation of pectin methylesterase in green beans and tomatoes
J. Agric. Food Chem.
54
204-211
2006
Solanum lycopersicum, Phaseolus vulgaris
Verlent, I.; van Loey, A.; Smout, C.; Duvetter, T.; Nguyen, B.L.; Hendrickx, M.E.
Changes in purified tomato pectinmethylesterase activity during thermal and high pressure treatment
J. Sci. Food Agric.
84
1839-1847
2004
Solanum lycopersicum
Di Matteo, A.; Giovane, A.; Raiola, A.; Camardella, L.; Bonivento, D.; De Lorenzo, G.; Cervone, F.; Bellincampi, D.; Tsernoglou, D.
Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein
Plant Cell
17
849-858
2005
Solanum lycopersicum (P14280), Solanum lycopersicum
Verlent, I.; Hendrickx, M.; Verbeyst, L.; Van Loey, A.
Effect of temperature and pressure on the combined action of purified tomato pectinmethylesterase and polygalacturonase in presence of pectin
Enzyme Microb. Technol.
40
1141-1146
2007
Solanum lycopersicum
-
Duvetter, T.; Fraeye, I.; Sila, D.N.; Verlent, I.; Smout, C.; Hendrickx, M.; Van Loey, A.
Mode of de-esterification of alkaline and acidic pectin methyl esterases at different pH conditions
J. Agric. Food Chem.
54
7825-7831
2006
Aspergillus aculeatus, Solanum lycopersicum
Plaza, L.; Duvetter, T.; Monfort, S.; Clynen, E.; Schoofs, L.; Van Loey, A.M.; Hendrickx, M.E.
Purification and thermal and high-pressure inactivation of pectinmethylesterase isoenzymes from tomatoes (Lycopersicon esculentum): a novel pressure labile isoenzyme
J. Agric. Food Chem.
55
9259-9265
2007
Solanum lycopersicum
Phan, T.D.; Bo, W.; West, G.; Lycett, G.W.; Tucker, G.A.
Silencing of the major salt-dependent isoform of pectinesterase in tomato alters fruit softening
Plant Physiol.
144
1960-1967
2007
Solanum lycopersicum (Q43143), Solanum lycopersicum
Lewis, K.C.; Selzer, T.; Shahar, C.; Udi, Y.; Tworowski, D.; Sagi, I.
Inhibition of pectin methyl esterase activity by green tea catechins
Phytochemistry
69
2586-2592
2008
Citrus sp., Solanum lycopersicum, Cuscuta pentagona, Castilleja indivisa
Jolie, R.P.; Duvetter, T.; Van Loey, A.M.; Hendrickx, M.E.
Pectin methylesterase and its proteinaceous inhibitor: a review
Carbohydr. Res.
345
2583-2595
2010
Aspergillus aculeatus, Aspergillus niger, Dickeya chrysanthemi, Solanum lycopersicum, Daucus carota subsp. sativus
Oikawa, P.Y.; Giebel, B.M.; da Silveira Lobo OReilly Sternberg, L.; Li, L.; Timko, M.P.; Swart, P.K.; Riemer, D.D.; Mak, J.E.; Lerdau, M.T.
Leaf and root pectin methylesterase activity and 13C/12C stable isotopic ratio measurements of methanol emissions give insight into methanol production in Lycopersicon esculentum
New Phytol.
191
1031-1040
2011
Solanum lycopersicum
Spelbrink, R.E.; Giuseppin, M.L.
Large-scale single step partial purification of potato pectin methylesterase that enables the use in major food applications
Appl. Biochem. Biotechnol.
174
1998-2006
2014
Solanum lycopersicum
Vandevenne, E.; Van Buggenhout, S.; Peeters, M.; Compernolle, G.; Declerck, P.; Hendrickx, M.; Van Loey, A.; Gils, A.
Development of an immunological toolbox to detect endogenous and exogenous pectin methylesterase in plant-based food products
Food Res. Int.
44
931-939
2011
Aspergillus aculeatus, Solanum lycopersicum
de Freitas, S.T.; Handa, A.K.; Wu, Q.; Park, S.; Mitcham, E.J.
Role of pectin methylesterases in cellular calcium distribution and blossom-end rot development in tomato fruit
Plant J.
71
824-835
2012
Solanum lycopersicum
Hyodo, H.; Terao, A.; Furukawa, J.; Sakamoto, N.; Yurimoto, H.; Satoh, S.; Iwai, H.
Tissue specific localization of pectin-Ca2+ cross-linkages and pectin methyl-esterification during fruit ripening in tomato (Solanum lycopersicum)
PLoS ONE
8
e78949
2013
Solanum lycopersicum (P09607), Solanum lycopersicum
Kant, S.; Gupta, R.
Purification of pectin methylesterase from Lycopersicon esculentum and its application
Protein Pept. Lett.
19
1205-1211
2012
Solanum lycopersicum
Jeong, H.Y.; Nguyen, H.P.; Eom, S.H.; Lee, C.
Integrative analysis of pectin methylesterase (PME) and PME inhibitors in tomato (Solanum lycopersicum) identification, tissue-specific expression, and biochemical characterization
Plant Physiol. Biochem.
132
557-565
2018
Solanum lycopersicum
EXTERNAL LINKS (specific for EC-Number 3.1.1.11)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
