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Information on EC 3.1.1.11 - pectinesterase and Organism(s) Daucus carota and UniProt Accession P83218
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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: Daucus carota
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 methylesterase
-
-
-
-
PME
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pectin + n H2O = n methanol + pectate
reaction mechanism, the active site contains two aspartic acid residues D136 and D157 at the centre, which are distinguishing features of aspartyl esterases, two glutamines Q113 and Q135 and one arginine residue R225
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
pectin pectylhydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9025-98-3
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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
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
-
-
?
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
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
proteinaceous pectin methylesterase inhibitor
-
PMEI, isolated from kiwi fruit (Actinidia chinensis cv. Hayward), competitive, medium inhibition
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). PME_DAUCA
319
0
34254
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the enzyme contains a pro-region, role of the PRO region in PME targeting and function
proteolytic modification
-
the inactive enzyme precursor, Pro-PME, is activated to the mature soluble enzyme, which is excreted to the cell wall
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
-
enzyme is known to be responsible for cloud loss in juice processing and storage
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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Markovic, O.; Cederlund, E.; Griffiths, W.J.; Lipka, T.; Jornvall, H.
Characterization of carrot pectin methylesterase
Cell. Mol. Life Sci.
59
513-518
2002
Daucus carota (P83218), Daucus carota
Johansson, K.; El-Ahmad, M.; Friemann, R.; Jornvall, H.; Markovic, O.; Eklund, H.
Crystal structure of plant pectin methylesterase
FEBS Lett.
514
243-249
2002
Daucus carota (P83218)
Ly-Nguyen, B.; Van Loey, A.M.; Smout, C.; Verlent, I.; Duvetter, T.; Hendrickx, M.E.
Effect of intrinsic and extrinsic factors on the interaction of plant pectin methylesterase and its proteinaceous inhibitor from kiwi fruit
J. Agric. Food Chem.
52
8144-8150
2004
Musa acuminata, Daucus carota, Fragaria x ananassa
Rico, D.; Martin-Diana, A.B.; Barry-Ryan, C.; Henehan, G.T.; Frias, J.M.
Simultaneous modelling of the thermal degradation kinetics of pectin methylesterase in lettuce (Lactuca sativa L.) and carrot (Daucus carota L.) extracts: analysis of seasonal variation and tissue type
Biosci. Biotechnol. Biochem.
71
2383-2392
2007
Daucus carota, Lactuca sativa
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