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Information on EC 3.1.1.11 - pectinesterase and Organism(s) Solanum lycopersicum and UniProt Accession P14280

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     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.11 pectinesterase
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Select one or more organisms in this record: ?
This record set is specific for:
Solanum lycopersicum
UNIPROT: P14280 not found.
Word Map
The taxonomic range for the selected organisms is: Solanum lycopersicum
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pectin methylesterase, pectinesterase, pectin methyl esterase, pectinmethylesterase, pectin esterase, pme i, sal k 1, atpme3, hms-1, bcpme1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P65
-
-
-
0
PE
-
-
-
0
pectase
-
-
-
0
pectin demethoxylase
-
-
-
0
pectin esterase
301630
-
pectin methoxylase
-
-
-
0
pectin methyl esterase
pectin methyl-esterase
301630
-
pectin methylesterase
pectinmethylesterase
1092
-
pectinoesterase
-
-
-
0
pectofoetidin
-
-
-
0
PMEU1
281841
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
0
SYSTEMATIC NAME
IUBMB Comments
pectin pectylhydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-98-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pectin + H2O
methanol + pectate
show the reaction diagram
citrus pectin + H2O
methanol + pectate
show the reaction diagram
-
best substrate
-
-
?
cyano-acetate + H2O
?
show the reaction diagram
-
-
-
-
?
pectin + H2O
?
show the reaction diagram
-
the enzyme deesterifies methoxylated pectin in the plant cell wall
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
pectin + n H2O
n methanol + pectate
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pectin + H2O
methanol + pectate
show the reaction diagram
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
-
-
?
citrus pectin + H2O
methanol + pectate
show the reaction diagram
-
best substrate
-
-
?
pectin + H2O
?
show the reaction diagram
-
the enzyme deesterifies methoxylated pectin in the plant cell wall
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
pectin + n H2O
n methanol + pectate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
coumaric acid
-
-
epigallocatechin gallate
-
natural inhibitor for pectin methyl esterase, acts as a non-specific pan-inhibitor for PME
gallic acid
-
-
gallocatechin gallate
-
-
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
-
PMEI
-
PME inhibitor
-
polygalacturonic acid
-
end-product inhibition
PP60
-
concentration-dependent inhibition
proteinaceous pectin methylesterase inhibitor
-
specific inhibition
-
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 hide
LITERATURE
IMAGE
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26.96
-
partially purified enzyme, at pH 7.0, 22°C
834 - 847
-
purified isozymes
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
-
activity increases with increasing pH up to 45°C
7.2
-
at atmospheric pressure and 55°C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8
-
pH-dependent activity pattern, pH-profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22.5
-
assay at
35
-
at pH 4.4 and normal pressure, temperature optimum shifted to higher temperatures at higher pressure
50 - 60
-
at atmospheric pressure to 300 MPa
60
-
longer exposure to this optimum temperatures resulted in inactivation of the enzyme
60 - 65
-
at 100-200 MPa
61
-
enzyme immobilized on polyethylene terephthalate
62
-
enzyme immobilized on pectin esterase
65 - 70
-
at 200-300 MPa, optimal reaction conditions in the presence of Ca2+
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 65
30 - 70
-
PME activity during isobaric-isothermal treatment, overview
35 - 65
-
highest activity detected at 65°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.3
-
above, isoelectric focusing pH range pH 3-10
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PME1_SOLLC
546
1
60066
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27500 - 27800
-
-
33600
-
SDS-PAGE
34000
-
x * 34000, SDS-PAGE
35900
-
x * 35900, isoenzyme A, SDS-PAGE
40300
-
x * 40300, isoenzyme B, SDS-PAGE
43200
-
x * 43200, isoenzyme C, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
no modification
-
no glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex between enzyme and PMEI, vapor diffusion technique
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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 - 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
-
5 min, thermostable isozyme, complete inactivation
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
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is very pressure resistant, inactivation at 900 MPa is slower as compared at atmospheric pressure
-
increased temperature stability after immobilization
-
loss of activity in concentrated maltodextrin or sucrose solutions
-
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
25°C, purified enzyme, 3 weeks, no significant loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
4 enzyme forms: A, B, C and D
-
ammonium sulfate precipitation and DEAE cellulose column chromatography
-
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
-
partially purified by CS174 EBA resin column 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 hide
LITERATURE
food industry
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Markovic, O.; Jörnvall, H.
Pectinesterase. The primary structure of the tomato enzyme
Eur. J. Biochem.
158
455-462
1986
Solanum lycopersicum
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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, Aspergillus carbonarius, Aspergillus japonicus, Aspergillus niger, Avena sativa, Persea americana, Musa acuminata, Neofusicoccum ribis, Botrytis cinerea, Brassica oleracea, Vicia faba, Byssochlamys fulva, Kluyveromyces marxianus, Capsicum annuum, Carica papaya, Oculimacula yallundae, Chaetomium globosum, Citrus aurantiifolia, Citrus limon, Citrus nobilis, Citrus x paradisi, Citrus reticulata, Citrus sinensis, Clostridium aurantibutyricum, Clostridium multifermentans, Colletotrichum gloeosporioides, Colletotrichum trifolii, Coniella diplodiella, Athelia rolfsii, Corynebacterium sp., cranberry, Cucumis sativus, Curvularia lunata, Daucus carota, Diospyros sp., Lasiodiplodia theobromae, Epicoccum nigrum, Erwinia sp., Penicillium sp., Fragaria sp., Fusarium oxysporum, Fusarium sp., Fusarium roseum, Gaeumannomyces graminis, Gilbertella persicaria, Helianthus tuberosus, Hordeum vulgare, Medicago sativa, Solanum lycopersicum, Macrosporium cladosporioides, Malus sp., Monilia fructicola, Nicotiana tabacum, Nigrospora sphaerica, Oospora sp., Pyrus communis, Pellicularia filamentosa, Penicillium chrysogenum, Phaseolus vulgaris, Physalospora obtusa, Physalospora sp., Phytophthora infestans, Alternaria infectoria, Prunus armeniaca, Prunus avium, Prunus persica, Prunus sp., Gymnoascus dankaliensis, Ralstonia solanacearum, Psidium guajava, Raphanus sativus, Ribes sp., Rubus idaeus, Sclerotinia libertiana, Sclerotinia sclerotiorum, Secale cereale, Solanum tuberosum, Stemphylium botryosum, Syringa vulgaris, Thanatephorus cucumeris, Theobroma cacao, Torulopsis candida, Trichoderma viride, Trichothecium roseum, Triticum aestivum, Vitis sp., Xanthomonas citri pv. malvacearum
-
Manually annotated by BRENDA team
Markovic, O.
Tomato pectin esterase - characterization of one of its multiple forms
Collect. Czech. Chem. Commun.
39
908-913
1974
Solanum lycopersicum
-
Manually annotated by BRENDA team
Warrilow, A.G.S.; Turner, R.J.; Jones, M.G.
A novel form of pectinesterase in tomato
Phytochemistry
35
863-868
1994
Solanum lycopersicum
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Markovic, O.; Jörnvall, 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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kant, S.; Gupta, R.
Purification of pectin methylesterase from Lycopersicon esculentum and its application
Protein Pept. Lett.
19
1205-1211
2012
Solanum lycopersicum
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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