Information on EC 3.1.1.11 - pectinesterase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.1.1.11
-
RECOMMENDED NAME
GeneOntology No.
pectinesterase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pectin + n H2O = n methanol + pectate
show the reaction diagram
-
-
-
-
pectin + n H2O = n methanol + pectate
show the reaction diagram
mechanism
-
pectin + n H2O = n methanol + pectate
show the reaction diagram
mechanism
-
pectin + n H2O = n methanol + pectate
show the reaction diagram
reaction mechanism
-
pectin + n H2O = n methanol + pectate
show the reaction diagram
reaction mechanism
-
pectin + n H2O = n methanol + pectate
show the reaction diagram
reaction mechanism, D157, stabilized by a hydrogen bond to R225, performs a nucleophilic attack on the ester bond of the carboxymethyl group of HGA
-
pectin + n H2O = n methanol + pectate
show the reaction diagram
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
-
pectin + n H2O = n methanol + pectate
show the reaction diagram
the catalytic residues Gln151, Gln173, Asp174, Asp195, and Arg253 are conserved in Sal k 1
Q17ST3
pectin + n H2O = n methanol + pectate
show the reaction diagram
two conserved aspartates are the nucleophile and general acid-base in the reaction mechanism, respectively, the catalytic site is formed by the conserved resisues Asp178, Asp199, and Arg267, molecular basis of the processive action of the enzyme, overview
Erwinia chrysanthemi
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
homogalacturonan degradation
-
-
Metabolic pathways
-
-
pectin degradation II
-
-
pectin degradation III
-
-
Pentose and glucuronate interconversions
-
-
Starch and sucrose metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
pectin pectylhydrolase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P65
-
-
-
-
PE
-
-
-
-
pectase
-
-
-
-
pectin demethoxylase
-
-
-
-
pectin methoxylase
-
-
-
-
pectin methyl esterase
-
-
-
-
pectin methylesterase
-
-
-
-
pectinoesterase
-
-
-
-
pectofoetidin
-
-
-
-
PME
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9025-98-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acrocylindrium sp.
-
-
-
Manually annotated by BRENDA team
i.e. onion
-
-
Manually annotated by BRENDA team
diverse isozymes, overview
-
-
Manually annotated by BRENDA team
ecotype Col-0
-
-
Manually annotated by BRENDA team
ecotype Columbia-0
-
-
Manually annotated by BRENDA team
Aspergillus niger 71
71
-
-
Manually annotated by BRENDA team
Aspergillus oryzae A-3
A-3
-
-
Manually annotated by BRENDA team
Aspergillus oryzae KBN616
KBN616
-
-
Manually annotated by BRENDA team
IFO 6146
-
-
Manually annotated by BRENDA team
LV 10, two pectin hydrolases: I and II
-
-
Manually annotated by BRENDA team
i.e. oat
-
-
Manually annotated by BRENDA team
subspecies Brassica napus oleifera, winter oil-seed rape
-
-
Manually annotated by BRENDA team
i.e. cauliflower
-
-
Manually annotated by BRENDA team
i.e. paprika
-
-
Manually annotated by BRENDA team
Jalapeno chili pepper
-
-
Manually annotated by BRENDA team
; different varieties
-
-
Manually annotated by BRENDA team
Castilleja indivisa
Indian paintbrush
-
-
Manually annotated by BRENDA team
Cercosporella herpotrichoides
-
-
-
Manually annotated by BRENDA team
cv. Nausica and Arancha, highest enzyme activity at the beginning of the season
-
-
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
cultivars Verna and Primofiori
-
-
Manually annotated by BRENDA team
i.e. mandarin
-
-
Manually annotated by BRENDA team
cultivars Marisol, Clemenules, Ortanique and Clemenvilla
-
-
Manually annotated by BRENDA team
cv. Nules and Marisol
-
-
Manually annotated by BRENDA team
Citrus reticulata Citrus sinensis
-
-
-
Manually annotated by BRENDA team
; cultivar Valencia
-
-
Manually annotated by BRENDA team
cultivar Valencia
-
-
Manually annotated by BRENDA team
cultivars Navelina, Salustiana, and Navelate
-
-
Manually annotated by BRENDA team
cv. Pera-Rio
-
-
Manually annotated by BRENDA team
i.e. orange, shamouti and valencia varieties
-
-
Manually annotated by BRENDA team
isoform PME3
UniProt
Manually annotated by BRENDA team
isoform PME4
UniProt
Manually annotated by BRENDA team
orange
-
-
Manually annotated by BRENDA team
Tarocco, Moro, Sanguinello, and Navel
-
-
Manually annotated by BRENDA team
valencia
-
-
Manually annotated by BRENDA team
Valencia orange
-
-
Manually annotated by BRENDA team
var. Valencia, heat stable activity assayed after heating samples for 2 min (chromatography samples) or 10 min (plant material) to 80C
-
-
Manually annotated by BRENDA team
var. Valencia, orange
-
-
Manually annotated by BRENDA team
Citrus sp.
-
-
-
Manually annotated by BRENDA team
i.e. grapefruit
-
-
Manually annotated by BRENDA team
Marsh grapefruit
-
-
Manually annotated by BRENDA team
variety star ruby
-
-
Manually annotated by BRENDA team
Citrus x paradisi Marsh grapefruit
Marsh grapefruit
-
-
Manually annotated by BRENDA team
Clostridium multifermentans
-
-
-
Manually annotated by BRENDA team
cranberry
-
-
-
Manually annotated by BRENDA team
Cucumis sativa
Pepino Almerica
-
-
Manually annotated by BRENDA team
i.e. cucumber
-
-
Manually annotated by BRENDA team
cv. Tiptop
SwissProt
Manually annotated by BRENDA team
i.e. carrot
-
-
Manually annotated by BRENDA team
var. Alister, Killer, and Oslo, high activity in hyperhydrated leaves
-
-
Manually annotated by BRENDA team
Diospyros sp.
persimmon
-
-
Manually annotated by BRENDA team
Erwinia chrysanthemi
-
-
-
Manually annotated by BRENDA team
Erwinia chrysanthemi
-
Uniprot
Manually annotated by BRENDA team
Erwinia chrysanthemi
a plant pathogen, strain B374
-
-
Manually annotated by BRENDA team
Erwinia chrysanthemi
also known as Dickeya dadantii
-
-
Manually annotated by BRENDA team
Erwinia chrysanthemi
strain 3937
-
-
Manually annotated by BRENDA team
Erwinia chrysanthemi
strain B374
-
-
Manually annotated by BRENDA team
Erwinia chrysanthemi 3937
strain 3937
-
-
Manually annotated by BRENDA team
Erwinia chrysanthemi B374
strain B374
-
-
Manually annotated by BRENDA team
jelly fig Makino
-
-
Manually annotated by BRENDA team
Fragaria sp.
strawberry
-
-
Manually annotated by BRENDA team
cultivar Elsanta
-
-
Manually annotated by BRENDA team
cv. Elsanta, strawberry
-
-
Manually annotated by BRENDA team
strawberry, cv. Elsanta
-
-
Manually annotated by BRENDA team
Fusarium roseum
-
-
-
Manually annotated by BRENDA team
Gibberella sp.
-
-
-
Manually annotated by BRENDA team
cultivar Kaohsiung No. 8
-
-
Manually annotated by BRENDA team
i.e. artichoke
-
-
Manually annotated by BRENDA team
var. Luchistaya, Prozrachnaya
-
-
Manually annotated by BRENDA team
i.e. barley
-
-
Manually annotated by BRENDA team
cells cultured in the presence of PME from orange peel
-
-
Manually annotated by BRENDA team
luPME1; cv. Ariane, flax
SwissProt
Manually annotated by BRENDA team
luPME3; cv. Ariane, flax
SwissProt
Manually annotated by BRENDA team
luPME5; cv. Ariane, flax
SwissProt
Manually annotated by BRENDA team
Macrosporium cladosporioides
-
-
-
Manually annotated by BRENDA team
i.e. Malpighia punicifolia, two isozymes PME1 and PME2
-
-
Manually annotated by BRENDA team
cultivar Fuji
-
-
Manually annotated by BRENDA team
i.e. apple
-
-
Manually annotated by BRENDA team
alfalfa
-
-
Manually annotated by BRENDA team
Monilia fructicola
-
-
-
Manually annotated by BRENDA team
banana, cv. Cavendish and Chiquita
-
-
Manually annotated by BRENDA team
cv. Canendish, banana
-
-
Manually annotated by BRENDA team
i.e. banana
-
-
Manually annotated by BRENDA team
Musa domestica
cv. Canendish, banana
-
-
Manually annotated by BRENDA team
cells cultured in the presence of PME from orange peel
-
-
Manually annotated by BRENDA team
cultivar Samsun NN
-
-
Manually annotated by BRENDA team
i.e. tobacco
-
-
Manually annotated by BRENDA team
Oospora sp.
-
-
-
Manually annotated by BRENDA team
Ophiobolus graminis
-
-
-
Manually annotated by BRENDA team
Pellicularia filamentosa
-
-
-
Manually annotated by BRENDA team
Penicillium oxalicum SX6
-
-
-
Manually annotated by BRENDA team
i.e. avocado
-
-
Manually annotated by BRENDA team
; green bean
-
-
Manually annotated by BRENDA team
; i.e. french bean
-
-
Manually annotated by BRENDA team
Physalospora sp.
-
-
-
Manually annotated by BRENDA team
isoform PME1
UniProt
Manually annotated by BRENDA team
isoform PME2
UniProt
Manually annotated by BRENDA team
isoform PME3
UniProt
Manually annotated by BRENDA team
isoform PME4
UniProt
Manually annotated by BRENDA team
isoform PME5
UniProt
Manually annotated by BRENDA team
isoform PME6
UniProt
Manually annotated by BRENDA team
isoform PME7
UniProt
Manually annotated by BRENDA team
isoform PME8
UniProt
Manually annotated by BRENDA team
isoform PME9
UniProt
Manually annotated by BRENDA team
Phytophthora capsici SD33
isoform PME1
UniProt
Manually annotated by BRENDA team
Phytophthora capsici SD33
isoform PME2
UniProt
Manually annotated by BRENDA team
Phytophthora capsici SD33
isoform PME3
UniProt
Manually annotated by BRENDA team
Phytophthora capsici SD33
isoform PME4
UniProt
Manually annotated by BRENDA team
Phytophthora capsici SD33
isoform PME5
UniProt
Manually annotated by BRENDA team
Phytophthora capsici SD33
isoform PME6
UniProt
Manually annotated by BRENDA team
Phytophthora capsici SD33
isoform PME7
UniProt
Manually annotated by BRENDA team
Phytophthora capsici SD33
isoform PME8
UniProt
Manually annotated by BRENDA team
Phytophthora capsici SD33
isoform PME9
UniProt
Manually annotated by BRENDA team
cultivar Alaska
UniProt
Manually annotated by BRENDA team
apricot
-
-
Manually annotated by BRENDA team
Malatya apricot
-
-
Manually annotated by BRENDA team
sweet cherry
-
-
Manually annotated by BRENDA team
i.e. peach
-
-
Manually annotated by BRENDA team
Prunus sp.
i.e. plum
-
-
Manually annotated by BRENDA team
cultivar Paluma
-
-
Manually annotated by BRENDA team
cultivar Predilecta
-
-
Manually annotated by BRENDA team
i.e. guave
-
-
Manually annotated by BRENDA team
i.e. pear
-
-
Manually annotated by BRENDA team
i.e. radish
-
-
Manually annotated by BRENDA team
Ribes sp.
i.e. gooseberry
-
-
Manually annotated by BRENDA team
i.e. raspberry
-
-
Manually annotated by BRENDA team
frgament
UniProt
Manually annotated by BRENDA team
Sclerotinia libertiana
-
-
-
Manually annotated by BRENDA team
i.e. rye
-
-
Manually annotated by BRENDA team
cultivar Micro Tom
-
-
Manually annotated by BRENDA team
cultivar Micro Tom
UniProt
Manually annotated by BRENDA team
cultivar Rutgers
-
-
Manually annotated by BRENDA team
Flandria prince
-
-
Manually annotated by BRENDA team
four isozymes
-
-
Manually annotated by BRENDA team
PMEU1 precursor; i.e. Solanum lycopersicum, gene Pmeu1, salt-dependent isozyme
SwissProt
Manually annotated by BRENDA team
var. Flandria Prince
-
-
Manually annotated by BRENDA team
cultivars Desiree, Montrose, and Pentland Dell
-
-
Manually annotated by BRENDA team
cultivars Mayan Gold and Inca Sun
-
-
Manually annotated by BRENDA team
i.e. potato
-
-
Manually annotated by BRENDA team
sugar cane weevil
UniProt
Manually annotated by BRENDA team
i.e. lilac
-
-
Manually annotated by BRENDA team
i.e. cacao
-
-
Manually annotated by BRENDA team
Torulopsis candida
-
-
-
Manually annotated by BRENDA team
i.e. wheat
-
-
Manually annotated by BRENDA team
isoform PEalpha; mung bean
SwissProt
Manually annotated by BRENDA team
isoform PEgamma; mung bean
SwissProt
Manually annotated by BRENDA team
i.e. grape
-
-
Manually annotated by BRENDA team
fragment; cultivar Cabernet Sauvignon
Q94B16 and Q9XGT5
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
the number of adventitious roots is 30% increased in the pme3-1 mutant
malfunction
-
loss-of-function mutant alleles of pectin methylesterase35 show a pendant stem phenotype and an increased deformation rate of the stem
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
metabolism
Erwinia chrysanthemi, Citrus sinensis, Aspergillus sp.
-
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
physiological function
-
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
-
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
-
although foliar pectin methylesterase activity is related to methanol emission, other factors must also be considered when predicting methanol emission
physiological function
-
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
-
isoform PME3 plays a role in adventitious rooting
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
-
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
-
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
-
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
-
isoform PME35-mediated demethylesterification of the primary cell wall directly regulates the mechanical strength of the supporting tissue
physiological function
Q9FVF9
the enzyme catalyzes the de-methylesterification of pectin in plant cell walls during cell elongation
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
anhydrogalacturonate + H2O
?
show the reaction diagram
Erwinia chrysanthemi, Erwinia chrysanthemi B374
-
-
-
-
?
citrus pectin + H2O
methanol + citrus pectate
show the reaction diagram
-
-
-
?
citrus pectin + H2O
methanol + citrus pectate
show the reaction diagram
Q94FS5, Q94FS6, Q9FVF9
-
-
?
citrus pectin + H2O
methanol + citrus pectate
show the reaction diagram
Erwinia chrysanthemi, Erwinia chrysanthemi 3937
-
highest activity with pectin with an esterification degree of 50%
-
?
citrus pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
citrus pectin + H2O
methanol + pectate
show the reaction diagram
-
best substrate
-
-
?
citrus pectin + H2O
methanol + pectate
show the reaction diagram
-
hydrolyzes pectin from citrus and sugar beet
-
-
?
citrus pectin + H2O
methanol + pectate
show the reaction diagram
Penicillium oxalicum SX6
-
-
-
-
?
cyano-acetate + H2O
?
show the reaction diagram
Solanum lycopersicum, Citrus sp., Cuscuta pentagona, Castilleja indivisa
-
-
-
-
?
high methoxyl pectin + H2O
?
show the reaction diagram
-
-
-
-
?
homogalacturonan + H2O
?
show the reaction diagram
-
-
-
-
?
homogalacturonan + H2O
?
show the reaction diagram
Q9FY03
PME removes methyl ester groups from homogalacturonan, overview
-
-
?
homogalacturonan + n H2O
?
show the reaction diagram
-
-
-
?
methyl pectate + H2O
?
show the reaction diagram
-
high molecular weight methyl pectate
-
-
?
methyl-esterfied oligogalacturonides + H2O
?
show the reaction diagram
-
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.
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Kluyveromyces marxianus, Torulopsis candida
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Erwinia chrysanthemi
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Erwinia chrysanthemi
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Erwinia chrysanthemi
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Erwinia chrysanthemi
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Citrus sp.
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
P83948, Q8GS16
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Acrocylindrium sp.
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Acrocylindrium sp.
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Clostridium multifermentans
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Lasiodiplodia theobromae, Epicoccum nigrum, Fusarium sp., Gibberella sp., Gilbertella persicaria, Macrosporium cladosporioides, Monilia fructicola, Nigrospora sphaerica, Oospora sp., Ophiobolus graminis, Pellicularia filamentosa, Alternaria infectoria, Physalospora sp., Physalospora obtusa, Gymnascella dankaliensis, Thanatephorus cucumeris, Sclerotinia libertiana, Pleospora tarda, Citrus reticulata
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
B2VPR8, D8VPP5
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
P85076
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
P83218
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q9FVF9
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
P14280
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q43143
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q9FY03
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Citrus reticulata Citrus sinensis
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q1PAH6
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q94B16 and Q9XGT5
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Castilleja indivisa
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q12535
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
S5YAB5
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
V9Q624
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
P09607
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
citrus pectin
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
citrus pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
apple pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
pectin B
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
no activity if the degree of esterification is below 31%
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q43234, Q9M5J0
the lower the degree of esterification, the higher the enzyme affinity to the substrate
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
P14280
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
show the reaction diagram
-
involved in the regulation of the cell wall rigidity
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, important for the control of hyperhydricity
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
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
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
low-temperature blanching of vegetables activates PME, which demethylates cell wall pectins and improves tissue firmness
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
Erwinia chrysanthemi
-
the enzyme catalyses the essential first step in bacterial invasion of plant tissues
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q43143
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
show the reaction diagram
Erwinia chrysanthemi
-
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
show the reaction diagram
-
highly methylated citrus pectin
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
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
show the reaction diagram
-
86% anhydrous galacturonic acid, 94% degree of methylation, containing minor amounts of galactose
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
a medium methylated pectin of 46% degree of methylation is used
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q12535
a medium methylated pectin of 46% degree of methylation is used
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
degree of methylation of 90%
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Erwinia chrysanthemi
-
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
show the reaction diagram
Aspergillus oryzae KBN616
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Aspergillus niger 71
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Citrus x paradisi Marsh grapefruit
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Phytophthora capsici SD33
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Aspergillus japonicus mutant
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Erwinia chrysanthemi B374
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Erwinia chrysanthemi B374
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Aspergillus oryzae A-3
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Aspergillus oryzae A-3
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
?
show the reaction diagram
Erwinia chrysanthemi, Citrus sinensis, Aspergillus sp.
-
-
-
-
?
pectin + H2O
?
show the reaction diagram
-
-
-
-
?
pectin + H2O
?
show the reaction diagram
-
constitutive enzyme
-
-
-
pectin + H2O
?
show the reaction diagram
-
the enzyme allows pectin hydrolysis during cell growth
-
-
-
pectin + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
Erwinia chrysanthemi
-
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
?
show the reaction diagram
-
maximum enzyme production is obtained after 4 days of batch growth
-
-
-
pectin + H2O
?
show the reaction diagram
-
the enzyme builds up the Donnan potential at the cell surface, this response may be cooperative with respect to pH
-
-
-
pectin + H2O
?
show the reaction diagram
-
the enzyme deesterifies methoxylated pectin in the plant cell wall
-
-
-
sisal fibre + H2O
?
show the reaction diagram
Penicillium oxalicum, Penicillium oxalicum SX6
-
-
-
-
?
methylated oligogalacturonides + H2O
?
show the reaction diagram
Erwinia chrysanthemi
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
Erwinia chrysanthemi
-
substrate specificity, overview
-
-
-
additional information
?
-
-
immobilized enzymes show about 7.5% of the activity of the free enzyme
-
-
-
additional information
?
-
-
enzyme immobilized on CNBr-Sepharose 4B show about 11.5% of the activity of the free enzyme, enzyme immobilized on polyethylene terephthalate shows 23.1% of the activity of the free enzyme
-
-
-
additional information
?
-
-
role of enzyme in juice clarification
-
-
-
additional information
?
-
-
the immobilized enzyme, unlike the free pectin esterase, does not act on pectin showing a higher esterification degree
-
-
-
additional information
?
-
Q94FS5, Q94FS6, Q9FVF9
involved in cell wall stiffening
-
?
additional information
?
-
Q43234, Q9M5J0
role in cell wall stiffening
-
?
additional information
?
-
Q9FY03
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
?
-
Q17ST3
the mildly basic and polymorphic protein causes allergic reactions in humans determined by secific IgE production
-
-
-
additional information
?
-
O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6
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 pectinmethylesterase catalyzes pectin de-esterification accelerates by increasing pressure up to 200 MPa in presence of tomato polygalacturonase
-
-
-
additional information
?
-
-
PME suppressed tobacco mosaic virus reproduction, including short- and long-distance virus movement in plants
-
-
-
additional information
?
-
-
the overall PME activity greatly decreases with a pectic substrate with a degree of methylation of 60%
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
P83218
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q9FVF9
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q9FY03
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Citrus reticulata Citrus sinensis
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q12535
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
S5YAB5
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
V9Q624
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
P09607
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
P14280
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
show the reaction diagram
-
involved in the regulation of the cell wall rigidity
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, important for the control of hyperhydricity
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
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
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
involved in the regulation of the cell wall rigidity, key role in process of fruit ripening
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
low-temperature blanching of vegetables activates PME, which demethylates cell wall pectins and improves tissue firmness
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
Erwinia chrysanthemi
-
the enzyme catalyses the essential first step in bacterial invasion of plant tissues
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Q43143
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
show the reaction diagram
Erwinia chrysanthemi
-
the enzyme catalyzes the hydrolysis of methylester groups from the galacturonic acid residues of homogalacturonan chains, the major component of pectin
-
-
?
pectin + H2O
?
show the reaction diagram
-
constitutive enzyme
-
-
-
pectin + H2O
?
show the reaction diagram
-
the enzyme allows pectin hydrolysis during cell growth
-
-
-
pectin + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
Erwinia chrysanthemi
-
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
?
show the reaction diagram
-
maximum enzyme production is obtained after 4 days of batch growth
-
-
-
pectin + H2O
?
show the reaction diagram
-
the enzyme builds up the Donnan potential at the cell surface, this response may be cooperative with respect to pH
-
-
-
pectin + H2O
?
show the reaction diagram
-
the enzyme deesterifies methoxylated pectin in the plant cell wall
-
-
-
pectin + H2O
methanol + pectate
show the reaction diagram
Citrus x paradisi Marsh grapefruit
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
Aspergillus japonicus mutant
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
-
-
-
-
?
citrus pectin + H2O
methanol + pectate
show the reaction diagram
-
best substrate
-
-
?
additional information
?
-
Q94FS5, Q94FS6, Q9FVF9
involved in cell wall stiffening
-
?
additional information
?
-
Q43234, Q9M5J0
role in cell wall stiffening
-
?
additional information
?
-
Q9FY03
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
?
-
Q17ST3
the mildly basic and polymorphic protein causes allergic reactions in humans determined by secific IgE production
-
-
-
additional information
?
-
-
PME suppressed tobacco mosaic virus reproduction, including short- and long-distance virus movement in plants
-
-
-
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
Ca2+
-
CaCl2, stimulates, optimal concentration is 0.1 M
Ca2+
-
CaCl2, isoenzyme PE I is stimulated to a higher degree than isoenzyme PE II; stimulates, optimal concentration is 0.01 M
Ca2+
-
activates
Ca2+
-
optimal concentration: 0.05 M
Ca2+
-
activates
Ca2+
-
activates
Ca2+
Acrocylindrium sp.
-
CaCl2, activates
Ca2+
-
activates
Ca2+
-
60 mM Ca2+ increases activity at elevated pressure up to 300 MPa, but decreases enzyme activity at atmospheric pressure and 45-60C
Ca2+
-
activates; activating
Ca2+
-
the highest PME activity occurrs at 20 mM of Ca2+, further increase in concentration results in the decline of the enzyme activity
Ca2+
Q12535
Ca2+ strongly stimulates activity at 5 mM; specific activity is higher in the presence than in the absence of 5 mM Ca2+
Ca2+
-
Ca2+ slightly stimulates activity at 5 mM; specific activity is higher in the presence than in the absence of 5 mM Ca2+
Ca2+
-
313.2% activity at 1 mM
CaCl2
-
activates with increasing temperature to a maximal value
Co2+
-
351.2% activity at 1 mM
Cr3+
-
216.5% activity at 1 mM
Cu2+
-
104.5% activity at 1 mM
EDTA
-
229% activity at 1 mM
Fe3+
-
107.1% activity at 1 mM
K+
Acrocylindrium sp.
-
KCl, activates
K+
-
stimulates
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+
-
stimulates
Mg2+
Acrocylindrium sp.
-
activates
Mg2+
-
activates
Mg2+
-
stimulates
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
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
-
stimulates, optimal concentration is 0.1 M
NaCl
-
activates, optimal concentration 0.1-0.15 mM
NaCl
-
isoenzyme PE I is stimulated to a higher degree than the enzyme PE II; stimulates, optimal concentration is 0.1 M
NaCl
-
dependent on NaCl, 0.2 M
NaCl
-
enzyme is not affected by NaCl from 0.1 M to 0.5 M concentrations
NaCl
-
optimal concentration: 0.2 M
NaCl
-
activates
NaCl
-
activates; optimal concentration: 0.18 M
NaCl
-
activates
NaCl
Acrocylindrium sp.
-
activates
NaCl
-
activates
NaCl
-
activates
NaCl
-
optimal concentration: 0.3-0.5 M
NaCl
-
highest activity at 0.15 M
NaCl
-
maximum activity at 2 M
NaCl
-
0.13 M NaCl required for optimum activity
NaCl
-
activating at 100 mM, especially at pH under 7.0
NaCl
-
activating at 100 mM at pH under 7.0
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
NH4Cl
-
activates
Ni2+
-
331.8% activity at 1 mM
Pb2+
-
139.2% activity at 1 mM
SDS
-
105.9% activity at 1 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
ZnSO4
-
activates
Mn2+
-
369.9% activity at 1 mM
additional information
Q43143
PMEU1 is a salt-dependent isozyme
additional information
-
the enzyme does not require salt for activity
additional information
-
not affected by Na+
additional information
-
no metal ions required for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-epigallocatechin
-
82% residual activity at 20 mg/ml
(NH4)2SO4
Acrocylindrium sp.
-
-
(NH4)Cl
Acrocylindrium sp.
-
-
beta-mercaptoethanol
-
96% residual activity at 1 mM
Ca2+
-
60 mM Ca2+ decreases enzyme activity at atmospheric pressure and 45-60C, 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
D-galacturonate
Erwinia chrysanthemi
-
slight
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 4C
-
EDTA
-
partial inhibition at 10 mM; slight inhibition
EGTA
-
EGTA treatment reduces PME activity, but the addition of Ca2+ with EGTA reinstates the activity in response to heat shock
epigallocatechin gallate
Castilleja indivisa, Citrus sp., Cuscuta pentagona, Solanum lycopersicum
-
natural inhibitor for pectin methyl esterase, acts as a non-specific pan-inhibitor for PME
epigallocatechin gallate
-
47% residual activity at 20 mg/ml
gallic acid
-
80% residual activity at 20 mg/ml
gallocatechin gallate
Castilleja indivisa, Citrus sp., Cuscuta pentagona, Solanum lycopersicum
-
-
Hg(CH3COO)2
-
-
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
iodoacetic acid
-
-
iodoacetic acid
-
-
K+
-
73% residual activity at 100 mM
Lauryl sulfate
-
-
Li2SO4
-
-
Mg2+
-
86% residual activity at 100 mM
Na2SO4
-
-
NaCl
-
activity decreases in the presence of 0.1 M NaCl and is 4times lower in 0.5 M NaCl
Ni2+
-
47% residual activity at 100 mM
NiCl2
-
-
Pectin
-
inhibits hydrolysis of p-nitrophenyl acetate
pectin methylesterase inhibitor
P85076
PMEI
-
PMEI
-
PME inhibitor
-
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
-
-
Polygalacturonate
Erwinia chrysanthemi
-
competitive
Polygalacturonate
Erwinia chrysanthemi
-
completely deesterified pectin, a competitive inhibitor of PME
polygalacturonic acid
Q43234, Q9M5J0
; competitive inhibitor, inhibits the alpha isoform at pH 5.6 and the gamma isoform at pH 5.6 and pH 7.6
polygalacturonic acid
-
end-product inhibition
PP60
Castilleja indivisa, Citrus sp., Cuscuta pentagona, Solanum lycopersicum
-
concentration-dependent inhibition
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
P14280
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
-
PMEI, isolated from kiwi fruit (Actinidia chinensis cv. Hayward), competitive, medium 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
Erwinia chrysanthemi
-
0.1% complete inactivation
SDS
-
78% residual activity at 10 mg/ml SDS
Silver nitrate
-
-
sodium carbonate
-
-
Sucrose
-
-
Tannic acid
-
10 mg/ml tannic acid completely inhibits the enzyme
ZnCl2
-
-
Mn2+
-
61% residual activity at 100 mM
additional information
-
no inhibition by up to 10 mM spermidine at 30C
-
additional information
-
no inhibition by proteinaceous pectin methylesterase inhibitor isolated from kiwi fruit
-
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
-
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
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
-
-
KCl
-
highest activity at 0.05-0.10 M
Na2SO4
-
highest activity at 0.02-0.05 M
NaCl
-
highest activity at 50 mM NaCl
NaCl
-
highest activity at 0.15 M
NaCl
Q1PAH6
a 10% increase of activity is observed at 0.1 M NaCl in all the three isoforms, then the activity decreases almost linearly with salt concentration increase for the PME I, while PME II and PME III show little increase of activity when salt concentration reaches 0.35 M
NaCl
-
activity is highest in the presence of 0.3 M NaCl in 50 mM borate-acetate, pH 8.3
NaCl
-
40-80 mM required for maximal activity
NH4Cl
-
highest activity at 0.05 M
spermidine
-
activates with increasing temperature to a maximal value at 45C
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
-
additional information
-
effects of hormones and stresses on isozyme expression, overview
-
additional information
-
plant acclimation in the cold (2C) is associated with the increases in leaf tensile stiffness, cell wall and pectin contents, pectin methylesterase activity and the low-methylated pectin content
-
additional information
-
PME activity increases with fruit maturation
-
additional information
-
transcriptional activation of light-inducible psbO is accompanied by elevated transcription of the PME gene
-
additional information
-
PME3 activity is increased in cellulose binding protein-overexpressing plants
-
additional information
-
overexpression of cellulose binding protein from Heterodera schachtii increases PME3 activity and leads to increased susceptibility to Heterodera schachtii potentially targeting this enzyme to aid cyst nematode parasitism
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
citrus pectin
Q94FS5, Q94FS6, Q9FVF9
pH 7.5, basic isoform
-
0.031
citrus pectin
Q94FS5, Q94FS6, Q9FVF9
pH 7.5, very basic isoform, i.e. luPME5
-
0.06
Pectin
Erwinia chrysanthemi
-
mutant V198A, pH 7.0, 30C
0.08
Pectin
-
pH 8.3, 50C, isozyme PME2
0.13
Pectin
Erwinia chrysanthemi
-
wild-type enzyme, pH 7.0, 30C
0.22
Pectin
Erwinia chrysanthemi
-
mutant Q177A, pH 7.0, 30C
0.51
Pectin
-
immobilized enzyme, Vmax: 14.6 micromol/min/mg, no difference between free and immobilized enzyme in Km but in Vmax (8.4fold higher value)
0.53
Pectin
Erwinia chrysanthemi
-
mutant M306A, pH 7.0, 30C
0.71
Pectin
-
immobilized enzyme, at 20C
0.77
Pectin
Erwinia chrysanthemi
-
mutant T272A, pH 7.0, 30C
0.77
Pectin
-
free enzyme, at 20C
0.77
Pectin
-
-
0.94
Pectin
-
pH 8.3, 50C, isozyme PME1
2.2
Pectin
Erwinia chrysanthemi
-
mutant Q153A, pH 7.0, 30C
additional information
citrus pectin
Erwinia chrysanthemi
-
pH 6 and pH 7.6
-
0.21
citrus pectin
Q94FS5, Q94FS6, Q9FVF9
pH 7.5, neutral isoform
-
additional information
additional information
-
-
-
additional information
additional information
Erwinia chrysanthemi
-
steady-state kinetics, kinetic mechanism
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
47.6
citrus pectin
-
at pH 5.0 and 50C
-
40
Pectin
Erwinia chrysanthemi
-
mutant Q177A, pH 7.0, 30C
59
Pectin
Erwinia chrysanthemi
-
mutant M306A, pH 7.0, 30C
68
Pectin
Erwinia chrysanthemi
-
mutant V198A, pH 7.0, 30C
232
Pectin
Erwinia chrysanthemi
-
mutant Q153A, pH 7.0, 30C
425
Pectin
Erwinia chrysanthemi
-
mutant T272A, pH 7.0, 30C
450
Pectin
Erwinia chrysanthemi
-
wild-type enzyme, pH 7.0, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16
Polygalacturonate
Erwinia chrysanthemi
-
-
4.2
polygalacturonic acid
Q43234, Q9M5J0
pH 5.6
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.246
-
crude extract
0.82
-
crude extract
1.1
Q1PAH6
crude homogenate
1.19
Erwinia chrysanthemi
-
-
1.29
-
pH 8.0, no NaCl added
1.82
-
pH 8.0, 0.15 M NaCl
1.91
-
in the absence of Ca2+, pH 6.0, 30C
2.26
Q12535
in the absence of Ca2+, pH 6.0, 30C
2.54
-
in the presence of 5 mM Ca2+, pH 6.0, 30C
5.7
-
crude enzyme, at pH 5.0 and 30C
5.83
-
crude extract, at 20C
5.9
-
cell wall extract, at pH 7.0 and 30C
6.5
-
after 7.93fold purification
7.59
Q12535
in the presence of 5 mM Ca2+, pH 6.0, 30C
9.67
-
supernatant, at pH 4.7 and 50C
11.98
-
purified enzyme
15.67
-
partially purified enzyme, pH 8., 50C
26.6
-
pH 8.0, purified enzyme
26.96
-
partially purified enzyme, at pH 7.0, 22C
66
-
purified isozyme PME2
68.6
-
at pH 5.0 and 50C
70.92
-
after 12.2fold purification, at 20C
124
-
isoenzyme PE I
194
-
after 34fold purification, at pH 5.0 and 30C
206
-
purified isozyme PME1
242.5
-
purified enzyme, pH 7.0, 22C
342
-
after 35.4fold purification, at pH 4.7 and 50C
834 - 847
-
purified isozymes
963
-
after 163fold purification, at pH 7.0 and 30C
1350
-
pH 8.0, 20C, 100 mM NaCl
1950
-
pH 8.0, 20C, no added NaCl
2253
Q1PAH6
isozyme PME I after purification
2297
Q1PAH6
isozyme PME II after purification
2333
Q1PAH6
isozyme PME III after purification
2450
-
pH 8.0, 20C, 100 mM NaCl
2702
-
purified enzyme immobilized onto porous glass beads, at 20C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
Acrocylindrium sp.
-
-
additional information
-
method for determination of a low level of pectin methylesterase activity from vegetable products
additional information
-
-
additional information
-
-
additional information
Erwinia chrysanthemi
-
-
additional information
Citrus reticulata, Citrus reticulata Citrus sinensis, Citrus sinensis
-
activity in different cultivars, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
-
pectin hydrolase II, at 50C
4.6
-
enzyme immobilized on CNBr-Sepharose 4B or polyethylenen terephthalate
4.8
-
soluble enzyme
5
Sclerotinia libertiana
-
-
5
Erwinia chrysanthemi
-
-
5.5 - 6
B2VPR8, D8VPP5
-
5.5 - 6
P83948, Q8GS16
in the presence of 1.2% NaCl; in the presence of 1.2% NaCl; in the presence of 1.2% NaCl
5.5 - 7
Q94FS5, Q94FS6, Q9FVF9
neutral isoform
5.5 - 7.5
-
activity increases with increasing pH up to 45C
5.5
-
pectin hydrolase I, at 50C
5.5
-
-
6
-
presence of 1.2% NaCl
6
-
two pH optima
6
-
native and recombinant protein
6.5 - 7
-
two pH optima
6.5 - 9
-
isoenzyme PE I from pod
6.8
-
assay at
7 - 7.5
Acrocylindrium sp.
-
-
7 - 8
-
isoenzyme II
7 - 9
-
isoenzyme PE II from seed hull
7
-
isoenzyme PE I or PE II
7
-
isoenzyme PE I
7
Erwinia chrysanthemi
-
assay at
7
Q1PAH6
isozyme PME II, at 0.1 M NaCl isozyme PME III shows two maxima at pH 7.0 and 9.0
7.2
-
at atmospheric pressure and 55C
7.3
-
-
7.5
-
soluble and immobilized enzyme
7.5
Acrocylindrium sp., Cercosporella herpotrichoides
-
-
7.5
Erwinia chrysanthemi
-
-
7.5
-
at 0.1-0.2 M NaCl
7.5
-
at 22C
7.5
-
assay at
7.5
Q1PAH6
isozyme PME I
7.6
-
isoenzyme I
7.8
P83218
-
7.8
Citrus reticulata, Citrus reticulata Citrus sinensis, Citrus sinensis
-
assay at
8 - 8.5
-
two pH optima
8 - 8.5
-
in phosphate buffer
8 - 9
Erwinia chrysanthemi
-
-
8
-
isoenzyme II
8
-
isoenzyme PME I and PME II
8
-
two pH optima
8
-
immobilized enzyme
8.3
-
assay at
8.5 - 9
Q94FS5, Q94FS6, Q9FVF9
very basic isoform, i.e. luPME5
8.5 - 9.5
-
at 50 mM NaCl
8.5
Q94FS5, Q94FS6, Q9FVF9
basic isoform
9
Citrus nobilis, Clostridium multifermentans
-
-
9
-
around
9
-
absence of NaCl
9
Q1PAH6
isozyme PME III, at 0.35 M NaCl only one maximum is observed at pH 9.0
9
-
free enzyme
9
-
around pH 9 in glycine buffer
additional information
-
acidic pH optimum
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 - 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 - 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 - 9.5
-
-
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
-
pH-dependent activity pattern, pH-profile, overview
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
4.5 - 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
4.5 - 9.5
Q1PAH6
-
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 - 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
-
less than 50% of activity at pH 5 and 10
5 - 6
Erwinia chrysanthemi
-
about 55% activity at pH 5-6
5 - 8.5
-
-
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
Q43234, Q9M5J0
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
-
pH 6.0: about 40% of maximal activity, pH 9.0: about 70% of maximal activity
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
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
7.5 - 11
-
pH 7.5: about 50% of maximal activity, pH 11.0: about 85% of maximal activity
7.5 - 9.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
Citrus reticulata, Citrus reticulata Citrus sinensis, Citrus sinensis
-
assay at
22.5
-
assay at
24
-
assay at room temperature
25 - 35
Clostridium multifermentans
-
-
27.5
Aspergillus sp., Citrus sinensis, Erwinia chrysanthemi
-
assay at
30
Cucumis sativa
-
assay at
30
Erwinia chrysanthemi
-
assay at
30
-
assay at
35
-
isoenzyme PME I and PME II
35
-
at pH 4.4 and normal pressure, temperature optimum shifted to higher temperatures at higher pressure
37
Aspergillus sp., Citrus sinensis, Erwinia chrysanthemi
-
assay at
40
-
soluble enzyme
40
Acrocylindrium sp., Aspergillus japonicus, Athelia rolfsii, Cercosporella herpotrichoides
-
-
40
Erwinia chrysanthemi
-
-
45
-
at pH 8 and normal pressure, temperature optimum shifted to higher temperatures at higher pressure
50 - 55
-
isoenzyme PE I and PE II
50 - 60
-
at atmospheric pressure to 300 MPa
50
-
CNBr-Sepharose 4B immobilized enzyme
50
-
soluble enzyme
50
Erwinia chrysanthemi
-
-
50
-
assay at
50
-
immobilized enzyme
52
-
enzyme immobilized on polyethylene terephthalate
52.5 - 55
-
at pH 7, sharp optimum
55 - 60
-
-
55
Fragaria sp.
-
-
55
-
at atmospheric pressure
60 - 65
-
at 100-200 MPa
60
-
free enzyme
60
-
longer exposure to this optimum temperatures resulted in inactivation of the enzyme
61
-
enzyme immobilized on polyethylene terephthalate
62
-
enzyme immobilized on pectin esterase
63
-
-
65 - 70
-
at 200-300 MPa, optimal reaction conditions in the presence of Ca2+
75 - 85
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-10
-
sharp increase in reaction rate as the temperature approaches the melting temperature, fructose, maltodextrin and sucrose enhance this effect
-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
0 - 65
Erwinia chrysanthemi
-
0C: about 20% of maximal activity, 65C: 10% of maximal activity
10 - 60
-
10C: about 45% of maximal activity, 60C: about 25% of maximal activity
20 - 70
-
rapid increase of activity between 30 and 40C, rapid loss of activity above 55C
23
-
no methanol production in whole green beans
25 - 65
-
activity increases with increasing temperature up to 65C
25 - 65
-
activity increases with increasing temperature up to 45C and decreases above
25 - 65
-
the rate of de-esterification increases substantially with increasing temperature
30 - 50
-
about 50% of maximal activity at 30C and at 50C
30 - 65
-
the enzyme activity is slightly increased at temperatures above 30C, but peaks at 55C. At temperatures above 55C, the activity drops rapidly, and no activity is detected at 65C
30 - 70
-
50% of activity at 30C, 30% of activity at 70C
30 - 70
-
PME activity during isobaric-isothermal treatment, overview
35 - 60
-
90-100% activity from 35-50C, about 30% activity at 55C, no activity at 60C
35 - 65
-
about 45% of maximal activity at 35C and at 65C, pectin hydrolase I
35 - 65
-
highest activity detected at 65C
40 - 65
-
40C: about 20% of maximal activity, 65C: about 25% of maximal activity
42 - 56
-
42C: about 80% of maximal activity, 56C: about 45% of maximal activity, hydrolase II
45 - 65
-
very low activity below 45C
50
-
heating intact beans to 50C causes PME activation and enzyme remains active even at 23C
60 - 90
-
maximum activity is observed at 60C after that activity decreases sharply up to almost zero at 90C
60 - 90
-
maximum activity is observed at 60C. The activity decreases sharply up to almost zero at 90C
80
-
no activity
additional information
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8
-
isoelectric focusing
5
-
isoelectric focusing, isoform 3
5.2
-
isoelectric focusing, isoform 2
5.3
-
at least 7 isoforms, isoelectric focusing, pH gradient 3.5-10
5.5
-
at least 7 isoforms, isoelectric focusing, pH gradient 3.5-10
5.9
-
at least 7 isoforms, isoelectric focusing, pH gradient 3.5-10
6 - 9.3
-
isoelectric focusing, several bands with pI values of 6.1, 6.3, 7.5, 7.9, and >9.3 detected
6.3 - 6.8
-
at least 7 isoforms, isoelectric focusing, pH gradient 3.5-10
6.7 - 7.8
Q17ST3
due to heterogenities
6.7
-
isoelectric focusing
6.8
S5YAB5
calculated from amino acid sequence
7
Q94FS5, Q94FS6, Q9FVF9
isoelectric focusing, pH gradient 3-10, neutral isoform
7.2
-
isoelectric focusing, isoform 1
7.3 - 7.4
-
at least 7 isoforms, isoelectric focusing, pH gradient 3.5-10
7.3
-
isoelectric focusing
7.8
B2VPR8, D8VPP5
calculated from amino acid sequence
8.3
Q94FS5, Q94FS6, Q9FVF9
isoelectric focusing, pH gradient 3-10, basic isoform
8.5
-
at least 7 isoforms, isoelectric focusing, pH gradient 3.5-10
8.5
-
isoelectric focusing
8.6
-
calculated from the deduced amino acid sequence for the mature protein
9
-
pI above 9, isoelectric focusing, pH range pH 3-9
9.1
-
at least 7 isoforms, isoelectric focusing, pH gradient 3.5-10
9.2
-
isoelectric focusing
9.3
-
above, isoelectric focusing pH range pH 3-10
9.31
-
isoelectric focusing
9.6
Q94FS5, Q94FS6, Q9FVF9
isoelectric focusing, pH gradient 3-10, very basic isoform, i.e. luPME5
9.6
-
isoelectric focusing
9.8
-
isoelectric focusing
9.8
-
calculated from amino acid sequence
9.8
Q9FVF9
isoelectric focusing
10.1
-
isoelectric focusing
additional information
-
acidic and alkaline isoforms detected in both varieties
additional information
-
acidic isoelectric pH
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
low activity
Manually annotated by BRENDA team
Q94B16 and Q9XGT5
pectin methylesterase activity is present before the onset of veraison and increases during skin maturation
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
Citrus sinensis, Citrus reticulata, Citrus reticulata Citrus sinensis
-
juice
Manually annotated by BRENDA team
-
isoenzyme A is the predominant enzyme form
Manually annotated by BRENDA team
-
Easy Pick and Hard Pick fruits with different states of pectin polymerization, higher activity in immature than in mature fruits
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Q43143
young developing, isozyme profile, expression analysis, overview
Manually annotated by BRENDA team
-
maximum PME activity is detected in green fruits and steadily decreases to reach a minimum in senescent fruits
Manually annotated by BRENDA team
-
PME activity increases with fruit maturation
Manually annotated by BRENDA team
P83948, Q8GS16
isoform PME1 is a minor citrus fruit thermolabile pectin methylesterase
Manually annotated by BRENDA team
P83948, Q8GS16
isoform PME2 is the major thermolabile pectin methylesterase isoenzyme accumulated in citrus pulp tissue
Manually annotated by BRENDA team
Q94FS5, Q94FS6, Q9FVF9
-
Manually annotated by BRENDA team
Q43234, Q9M5J0
-
Manually annotated by BRENDA team
-
isoenzyme B and C in comparable amounts
Manually annotated by BRENDA team
Citrus reticulata Citrus sinensis
-
-
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Q43143
isozyme profile, expression analysis, overview
Manually annotated by BRENDA team
-
photosynthetic active and vascular tissues
Manually annotated by BRENDA team
-
pollen specific PME detected exclusively in mature pollen and not in any other tissue examined, high activity in pollen tube
Manually annotated by BRENDA team
-
tube, the enzyme belongs to the group I of pectinesterases in Arabidopsis thaliana pollen
Manually annotated by BRENDA team
-
tube, the enzyme belongs to the group II of pectinesterases in Arabidopsis thaliana pollen
Manually annotated by BRENDA team
S5YAB5
the enzyme is expressed in pollen grains from 4 days before anthesis till anther dehiscence and in pollinated carpels
Manually annotated by BRENDA team
-
higher activity in pulp than in juice, relatively low activity in Navel oranges compared with the other strains
Manually annotated by BRENDA team
Citrus x paradisi Marsh grapefruit
-
-
-
Manually annotated by BRENDA team
-
isoenzyme C is the predominant enzyme form
Manually annotated by BRENDA team
Q9FY03
tissues active in secondary growth and during dormancy, PME1 expression patterns, overview
Manually annotated by BRENDA team
-
highest expression in the basal part of the inflorescence stem
Manually annotated by BRENDA team
additional information
-
isoform PME3 is ubiquitously expressed in Arabidopsis thaliana, particularly in vascular tissues
Manually annotated by BRENDA team
additional information
P09607
isoform PE2 expression is not detected in tissues surrounding seeds, such as locular tissue, seed, placenta, and core
Manually annotated by BRENDA team
additional information
S5YAB5
no expression is located in other vegetative or floral tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Citrus sp.
-
-
Manually annotated by BRENDA team
Castilleja indivisa
-
-
Manually annotated by BRENDA team
-
ionically bound to cell wall
Manually annotated by BRENDA team
-
mature part of the protein
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Dickeya dadantii (strain 3937)
Dickeya dadantii (strain 3937)
Dickeya dadantii (strain 3937)
Dickeya dadantii (strain 3937)
Dickeya dadantii (strain 3937)
Dickeya dadantii (strain 3937)
Dickeya dadantii (strain 3937)
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5200
-
isozyme PME2, gel filtration
681639
13000
-
bands of 37000, 27000, and 13000 Da are detected in crude PME extract, SDS-PAGE
693877
25100
-
isozyme PME1, gel filtration
681639
27000
-
-
114108
27000
-
bands of 37000, 27000, and 13000 Da are detected in crude PME extract, SDS-PAGE
693877
27500 - 27800
-
-
114108
28000
-
-
114108
28500
-
isoenzyme PE II from seed hull, gel filtration
114121
30000
-
isoenzyme PE II from pod, gel filtration
114121
33000
P83218
SDS-PAGE
650804
33000
-
SDS-PAGE
651294
33500
-
two bands: 33500 Da and 43000 Da, SDS-PAGE
650676
33500
-
SDS-PAGE
651560
33600
-
SDS-PAGE
650703
34000
-
gel filtration
114105
34000
-
SDS-PAGE
651558
35000 - 37000
-
isoenzyme PE II, gel filtration
114095, 114102
35000
-
SDS-PAGE
683188
35400
P85076
calculated from amino acid sequence
695057
36000
-
bands of 37000, 27000, and 13000 Da are detected in crude PME extract, SDS-PAGE
693877
36200
-
isoenzyme I and II, gel filtration
114108
37000
-
gel filtration
114108
37000
-
gel filtration
114109
37000
-
gel filtration
114130
37000
-
gel filtration
674087
37000
-
SDS-PAGE
694782
38000
-
SDS-PAGE
651557
38000
Q94FS5, Q94FS6, Q9FVF9
gel filtration, very basic isoform, i.e. luPME5
653562
40100
-
gel filtration
114123
41000
-
SDS-PAGE
692427
42000
Q1PAH6
the three PME isoforms show the same molecular weight of 42000 Da, SDS-PAGE
692425
43000
-
two bands: 33500 Da and 43000 Da, SDS-PAGE
650676
44000
-
isoenzyme PE I from seed hull, gel filtration
114121
45000
-
isoenzyme PE I, gel filtration
114095, 114102
46000
-
isoenzyme PE I from pod, gel filtration
114121
46000
-
isoform I, SDS-PAGE
650276
47000
-
isoform II, SDS-PAGE
650276
50000
-
gel filtration
674087
50000
P85076
purified enzyme, SDS-PAGE
695057
53000
-
gel filtration
114104
57000
-
guava PME contains two isoforms, one with 57000 Da molecular mass, SDS-PAGE
692672
99000
-
guava PME contains two isoforms, one with 99000 Da molecular mass, SDS-PAGE
692672
100000
-
isoenzyme I, gel filtration
114113
110000
-
isoenzyme II, gel filtration
114113
110000
Q94FS5, Q94FS6, Q9FVF9
gel filtration, neutral and basic isoform
653562
141300
-
gel filtration
690308
158000
-
SDS-PAGE
653572
400000
Clostridium multifermentans
-
-
114108
additional information
-
primary structure
114096
additional information
-
-
114108
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
114124
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 38000, SDS-PAGE
?
V9Q624
x * 50000, SDS-PAGE
?
-
x * 45000, SDS-PAGE
?
-
x * 55000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
?
-
x * 40000, SDS-PAGE
?
-
x * 41000, SDS-PAGE
?
-
x * 34000, SDS-PAGE
?
Q9FVF9
x * 34000, SDS-PAGE
?
-
x * 33792, calculation from nucleotide sequence
?
-
x * 35900, isoenzyme A, SDS-PAGE
?
-
x * 43000, isoenzyme I, SDS-PAGE
?
-
x * 43200, isoenzyme C, SDS-PAGE
?
-
x * 36200, SDS-PAGE
?
-
x * 40300, isoenzyme B, SDS-PAGE
?
-
x * 37500, SDS-PAGE
?
-
x * 40800, SDS-PAGE
?
B2VPR8, D8VPP5
x * 40000, recombinant enzyme, SDS-PAGE
?
-
three different isoforms with molecular weights of 75000, 83000, and 91000 detected in 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 * 38000, SDS-PAGE, protein from host
?
-
x * 39000-41500, calculated from the deduced amino acid sequence for the mature protein
?
-
x * 45000, SDS-PAGE, recombinant protein
?
-
x * 60300, calculated from the deduced amino acid sequence of the pre-pro-protein
?
-
x * 34500-35000, four isozymes, SDS-PAGE
?
Q17ST3
x * 40000, native enzyme, SDS-PAGE, x * 37214, native glycosylated enzyme, mass spectrometry
?
-
x * 33300, mature enzyme, estimated from SDS-PAGE
?
P83948, Q8GS16
x * 34341, isoform PME4, MALDI-TOF mass spectrometry
?
P83948, Q8GS16
x * 34467, isoform PME2, MALDI-TOF mass spectrometry
?
P83948, Q8GS16
x * 34485, isoform PME1, MALDI-TOF mass spectrometry
?
P83948, Q8GS16
x * 35000, isoform PME2, SDS-PAGE
?
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
x * 36200, isoform PME3, calculated from amino acid sequence
?
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
x * 36900, isoform PME2, calculated from amino acid sequence
?
B2VPR8, D8VPP5
x * 37386, isoform Ole e 11.0101, calculated from amino acid sequence
?
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
x * 37700, isoform PME1, calculated from amino acid sequence
?
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
x * 37700, isoform PME7, calculated from amino acid sequence
?
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
x * 37700, isoform PME9, calculated from amino acid sequence
?
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
x * 37800, isoform PME8, calculated from amino acid sequence
?
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
x * 37900, isoform PME5, calculated from amino acid sequence
?
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
x * 38100, isoform PME4, calculated from amino acid sequence
?
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
x * 38200, isoform PME6, calculated from amino acid sequence
?
B2VPR8, D8VPP5
x * 39647, recombinant enzyme, calculated from amino acid sequence
?
-
x * 38100, calculated from amino acid sequence
?
-
x * 47900, one of two principal glycoisoforms, MALDI-TOF mass spectrometry, x * 53000, one of two principal glycoisoforms, MALDI-TOF mass spectrometry
?
S5YAB5
x * 65570, calculated from amino acid sequence
?
Penicillium oxalicum SX6
-
x * 55000, SDS-PAGE, x * 38100, calculated from amino acid sequence
-
?
Aspergillus oryzae KBN616
-
x * 33792, calculation from nucleotide sequence
-
?
Phytophthora capsici SD33
-
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 * 40000, SDS-PAGE
-
dimer
Q94FS5, Q94FS6, Q9FVF9
isoform luPME1: 2 * 56000, SDS-PAGE, isoform luPME3: 2 * 58000, SDS-PAGE
monomer
-
1 * 37000, SDS-PAGE
monomer
-
1 * 40000, isoenzyme PE II, SDS-PAGE, 1 * 45000-48000, isoenzyme PE I, SDS-PAGE
monomer
-
1 * 32400, gel filtration
monomer
-
1 * 38000, gel filtration
monomer
Q94FS5, Q94FS6, Q9FVF9
isoform luPME5, 1 * 34000-40000, SDS-PAGE
monomer
-
1 * 37000, SDS-PAGE, native mass by gel filtration
monomer
-
1 * 50000, SDS-PAGE, native mass by gel filtration
additional information
-
three-dimensional structure analysis, overview
additional information
Q17ST3
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
-
primary structures of isozymes, structural and processing motifs, three-dimensional structure analysis, overview
additional information
-
structural and processing motifs, three-dimensional structure analysis, overview
additional information
Erwinia chrysanthemi
-
the enzyme possesses a parallel beta-helix architecture, three dimensional structure of PME, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
possible glycosylation concluded from the relatively high mass of the kiwi enzyme compared with other plant PMEs
glycoprotein
P85076
-
proteolytic modification
-
the enzyme contains a pro-region, role of the PRO region in PME targeting and function
glycoprotein
-
-
glycoprotein
-
-
no modification
-
-
no modification
-
probably not a glycoprotein
side-chain modification
-
glycoprotein
glycoprotein
-
-
glycoprotein
-
the enzyme forms exhibits two principal glycoisoforms
no modification
-
no glycoprotein
side-chain modification
-
N-linked glycoprotein
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
side-chain modification
Erwinia chrysanthemi
-
lipoprotein
glycoprotein
-
N-linked glycoprotein, consists of 22 hexoses including 16 mannose, 4 N-acetylglucosamine and 2 glalactose residues
glycoprotein
-
native protein has about 10% carbohydrates, recombinant protein appears to be hyperglycosylated
proteolytic modification
-
the inactive enzyme precursor, Pro-PME, is activated to the mature soluble enzyme, which is excreted to the cell wall
proteolytic modification
Q94FS5, Q94FS6, Q9FVF9
cleavage between Ala29 and Thr30 removes the signal peptide from the pro-protein
proteolytic modification
-
the gene encoding PME has an N-terminal extension encoding the pro-sequence
glycoprotein
-
-
proteolytic modification
-
the enzyme contains a pro-region, role of the PRO region in PME targeting and function
glycoprotein
-
-
glycoprotein
Penicillium oxalicum SX6
-
-
-
side-chain modification
-
glycoprotein
glycoprotein
Q9FY03
PME1 contains two potential N-linked glycosylation sites, specified by the sequence Asn-X-Ser/Thr in the N-terminal Pro region
proteolytic modification
-
the enzyme contains a pro-region, role of the PRO region in PME targeting and function
glycoprotein
Q17ST3
carbohydrate detection, overview
glycoprotein
-
-
no modification
-
no glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
-
hanging drop vapor diffusion method
Erwinia chrysanthemi
P0C1A8
the inactive D178A PME mutant in complex with specifically methylated hexagalacturonates, 3 mg/ml protein, crystallization solutions contain 0.1 M MES, pH 6.5, 10% dioxane and 1.6 M ammonium sulfate, and dilutions of that crystallisation buffer with H2O, or 0.1 M MES, pH 6.5, and 12% w/v PEG 20000, X-ray diffraction structure determination and anaylsis at 1.7-1.9 A resolution
Erwinia chrysanthemi
-
complex between enzyme and PMEI, vapor diffusion technique
P14280
sitting drop vapor diffusion method, using 25% (w/v) PEG 3350, 0.1 M citric acid pH 3.5
V9Q624
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.1 - 10
-
stable
114109
1.1
-
5C, 72 h, stable
114109
3 - 7
-
isoenzyme PE I is stable
114106
4 - 7
-
stable
114119
4 - 8.5
Acrocylindrium sp.
-
24 h, 30C, stable
114112
4 - 9
-
40C, 30 min, stable
114105
4 - 9
-
isoenzyme PE II is stable
114106
4
-
pectinesterase I is stable, complete loss of activity of pectinesterase II after 6 h
114108
5 - 7
-
at both sides of this pH range the stability decreases slightly
692427
7
-
pectinesterase I and II, stable for at least 24 h
114108
9
-
no activity at pH 9
683188
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 50
-
the enzyme is very stable at 4C. At 50C the enzyme is stable up to 2 h as it retains 70% of its activity
730888
30 - 55
-
incubation at 30C has little but significant effect on enzyme activity, the incubation at 55C abolishes over 95% of enzyme activity
694782
30
Acrocylindrium sp., Athelia rolfsii
-
-
114108
30
-
pectinesterase II is labile
114108
30
-
57% loss of activity after 20 h at pH 1.1, 23% loss of activity after 20 h at pH 2.0
114109
30
Acrocylindrium sp.
-
24 h, pH 4.0-8.5, quite stable
114112
30
-
the optimum temperature for the activity of pectimethylesterase is 30C, 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
690308
35 - 45
-
the residual activity of apple pectin methyl esterase under atmospheric pressure exhibits some fluctuations after mild heat at 35, 45, and 55C, it seems that apple pectin methyl esterase is activated at 35 or 45C, 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 55C 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
692725
35
-
10 min, stable
114103
38
Clostridium multifermentans
-
5-15 min, inactivation
114108
40 - 50
-
stable
650276
40
-
30 min, pH 4.0-9.0, isoenzyme PE II is stable
114105
40
Erwinia chrysanthemi
-
16 min, in absence of substrate, stable up to
114125
40
Erwinia chrysanthemi
-
5 h, stable
114129
40
-
no loss of activity at atmospheric pressure and at pressures up to 700 MPa
651555
40
-
the enzyme remains stable for 1 h at 40C
729080
42 - 62
-
freshly squeezed orange juices processed at temperatures of 62C or above are characterized by minor residual enzyme activities, the juice processed at 52C 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 42C rapid clarification occurs within the first 8 days consistent with undetectable enzyme deactivation
692728
45
-
10 min, 45% loss of maximal activity
114103
50 - 60
-
thermal inactivation at 50C 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 60C for 30 s
692146
50 - 91
-
In the case of orange pectin methyl esterase no inactivation is achieved below 50C and around 8% remaining activity is found at 83C. As for inactivation of purified orange PME around 6% remaining activity is found at 72.5C. In orange juice-milk based beverages from 65 to 72.5C only the labile pectin methyl esterase fraction is inactivated whereas the stable fraction does not inactivate. It is necessary to increase the temperature to 90C 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 63C for 5 min and around 3.5% remaining activity is found at 91C.
693428
50 - 98
-
no loss of activity within 60 min
673778
50 - 98
-
guava PME retains 96.8% of activity after 300 min in 90C, retains 101.85% of its specific activity after 60 min of incubation at 50C, the PME enzyme retains 75.4%, 86.2% and 90.4% of its specific activity after 60 min of incubation, respectively, at 80C, 90C, and 98C
692672
50
-
10 min, 50% loss of activity
114103
50
-
60 min, 20% loss of activity
114104
50
-
pH 8.0, stable up to
114105
50
-
stable up to
114106
50
-
10 min, pH 3.0 or 10.0, complete inactivation; 10 min, pH 8.0, about 45% loss of activity; 240 min, pH 5.0, 1 h, 50% loss of activity
114111
50
Erwinia chrysanthemi
-
pH 6.0, 16 min, 50% loss of activity
114125
50
Erwinia chrysanthemi
-
half-life: 10 min
114129
50
Erwinia chrysanthemi
-
no loss of activity after 20 min
650755
50
-
43% loss of activity within 15 min at atmospheric pressure
671841
50
-
no loss of activity within 2 h
674101
50
-
90% of activity remaining after 50 min
675163
52 - 92
-
total pectin methylesterase activity rapidly declines between 52 and 72C after 12 s incubation. Heating at temperatures above 72C for 12 s inactivates the thermo-labile pectin methylesterase isoenzymes almost completely
714883
54 - 63
-
inactivation rate constants increase with increasing temperature
650676
55 - 60
-
at pH 5.0 and a high ionic strength (0.5 M), the enzyme shows a high thermostability (inactivation at temperatures above 60C), an enhancement of its heat stability is observed at pH 7.0 and temperatures above 55C, 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 65C and no increase of stability at temperatures above 65C, adding sugars and adding polyols has a positive effect on heat stability
692427
55 - 70
-
PME thermal degradation kinetics, modeling, overview
678803
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
650703
55
Acrocylindrium sp.
-
-
114108
55
-
5-15 min, inactivation
114108
55
-
10 min, pH 4.0, inactivation; pH 4.0, inactivation
114109
55
Acrocylindrium sp.
-
stable
114112
55
-
stable up to, sharp inactivation above
114119
55
Erwinia chrysanthemi
-
50% loss of activity after 5 min
650755
55
-
almost 50% loss of activity after 5 min
651558
55
-
97% loss of activity within 15 min at atmospheric pressure, no inactivation at pressures above 200 MPa up to at least 700 MPa; no inactivation at pressures above 400 MPa up to at least 700 MPa
671841
55
-
incubation at 55C, 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
673377
55
-
75% of activity after 60 min
673784
55
-
rapid inactivation at temperatures above 55C
674086
60 - 80
Cucumis sativa
-
maximal thermostability in Bis-Tris buffer, pH 6.7, supplemented with 60% glycerol and 1.25 M NaCl
651029
60 - 80
-
maximal thermostability in citrate buffer, pH 4.5, supplemented with 50% glycerol, addition of sucrose and trehalose increase thermal stability
651029
60 - 80
-
the enzyme retains more than 90% activity at 60C for 60 min. At 70C, the enzyme loses 46 and 61% activity in 30 and 60 min, respectively. Activity is completely abolished at 80C after 5 min of incubation
730650
60 - 90
-
kinetic model for thermal inactivation of multiple PME, kinetics, at pH 3.5-4.5, overview
681635
60
-
10 min, inactivation
114095
60
-
20 min, about 50% loss of activity of the soluble enzyme, about 20% loss of activity of the immobilized enzyme
114099
60
Erwinia chrysanthemi
-
complete loss of activity after 5 min
114129
60
Erwinia chrysanthemi
-
complete loss of activity after 2 min
650755
60
-
inactivation at atmospheric pressure
651555
60
-
50% of activity lost within 5 min
674086
60
-
15 min stable, loss of activity after 15 min
674118
60
-
45% of activity remaining after 8 min
675163
60
-
5 min, thermolabile isozyme, complete inactivation
680321
62
-
1 min, 50% inactivation
114130
63 - 91
Citrus reticulata Citrus sinensis, Citrus reticulata, Citrus sinensis
-
thermostability of the enzyme from juice of different cultivars, overview
679601
64
-
inactivation above at atmospheric pressure
651563
65 - 80
Q1PAH6
PME I and PME III retain about the 80% of their activity after 4 min of incubation at 65C, whereas PME II retains 60% of activity, PME I is more resistant at 80C 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
692425
65
-
20 min, about 75% loss of activity of the soluble enzyme, about 20% loss of activity of the immobilized enzyme
114099
65
-
20 min, complete loss of activity of the soluble enzyme, about 50% loss of activity of the immobilized enzyme
114099
65
-
complete loss of activity after 5 min
651558
65
-
progressive loss of activity even at high pressure conditions
671841
65
-
native enzyme stable for 30 min, 60% of activity remaining after 2 h
674101
68
-
more than 90% of activity lost within 5 min
674086
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
650703
70 - 90
-
the immobilized pectinesterase retains 35% of its optimum activity whereas the free pectinesterase is 85% active at 70C, the free and immobilized pectinesterases retain 40% and 30% of their optimum activities at 80C, free and immobilized pectinesterase enzymes lose about 95% and 80% of their original activities at 90C for 45 min
693695
70
Acrocylindrium sp., Cucumis sativus
-
-
114108
70
-
5-15 min, inactivation
114108
70
Acrocylindrium sp.
-
10 min, complete inactivation
114112
70
-
complete loss of activity within 5 min
674086
70
-
20% of activity remaining after 2 h
674101
70
-
5 min, thermostable isozyme, complete inactivation
680321
70
-
activity decreases at temperatures above 70C
694840
70
P83948, Q8GS16
following heating of a crude pulp tissue cell wall extract at 70C, the activity for the purified isoform PME2 is rapidly lost
715216
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
650703
75
-
increase in activity after 30 min of incubation
673778
75
-
10% of activity after 60 min
673784
80
-
1 min, complete loss of activity
114104
80
-
-
114108
80
-
5-15 min, complete inactivation
114108
80
-
5-15 min, complete inactivation
114108
80
-
2 min, 17% loss of activity
114123
80
-
7.6% of activity remaining after 1 min
675163
80
-
5 min, purified enzyme, inactivation
680286
80
-
5 min, partially purified enzyme, inactivation
680286
85 - 95
-
5% of activity after 5 min
673784
85
-
5-15 min, inactivation
114108
85
-
more than 50% of activity remaining after 1 min treatment, less than 10% of activity remaining after 3 min treatment
673376
90
-
-
114108
90
Sclerotinia libertiana, Vitis sp.
-
5-15 min, inactivation
114108
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
673778
90
-
complete inactivation within 1 min
675163
95
-
no inactivation after 30 s, 51% loss of activity after 60 s
114123
98
-
purified PME1 specific activity increases by 9.63% after 60 min incubation at 98C, while purified PME2 retains 66% of its specific activity
681639
100
cranberry
-
5-15 min, complete inactivation
114108
106 - 125
-
only slight loss of activity when incubated for 5 min
673778
additional information
-
-
114108
additional information
-
activity not completely abolished after pasteurization
673376
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
680321
additional information
-
immobilization stabilzes the enzyme
701983, 707325
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
high pressure stabilizes enzyme activity
-
highly pressure stable, no loss of activity upon treatment at 700 MPa for 1 h at 25C
-
pressure increases stability towards thermal inativation
-
very pressure stable, no inactivation up to 700 MPa
-
increased temperature stability after immobilization
-
pressure stable up to 600 MPa, loss of activity at 700 and 800 MPa
-
the highest level of inactivation of PME (96.8%) is obtained using a combination of preheating to 50C and a pulsed electric fields treatment time of 0.1 ms at 40 kV/cm
-
pressure labile enzyme
-
repeated freezing and thawing results in a substantial loss of activity
Erwinia chrysanthemi
-
significant loss of activity after freezing and thawing
Erwinia chrysanthemi
-
extremely pressure stable enzyme
-
at lower pressure of 300-400 MPa and higher temperatures of above 64C an antagonistic effect of pressure and heat is observed, high pressure prevents inactivation
-
pressure and temperature stable enzyme
-
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
-20C, crude extract, several weeks, no significant loss of activity
-
4C, enzyme in freshly squeezed orange juice, 62 days, the total enzyme activity remains nearly constant irrespective of the previous thermal treatment
-
4C, pH 7.5, 0.1 M NaCl, 2 years, less than 15% loss of activity
-
4C, purified enzyme, stable for 1 week
Erwinia chrysanthemi
-
4C, stable for at least 1 week
Erwinia chrysanthemi
-
4C, fully stable for several months
-
room temperature, fully stable for several days
-
4C, enzyme immobilized onto glutaraldehyde-containing amino group functionalized porous glass beads surface, 30 days, retains 50% of its initial activity
-
4C, free enzyme, 30 days, retains 25% of its initial activity
-
25C, purified enzyme, 3 weeks, no significant loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Acrocylindrium sp.
-
DE52 column chromatography, SP-Sepharose column chromatography, Mono-S column chromatography, and Superdex 75 gel filtration
P85076
ammonium sulfate precipitation and Ni-NTA agarose column chromatography
-
Ni-NTA His-bind resin chromatography, DEAE-Sephadex gel filtration, CM-cellulose column chromatography, and Shephacryl SH-100 gel filtration
-
further purification of a commercial preparation by gel filtration
-
Superdex-75 gel filtration
-
ammonium sulfate precipitation, HisTrap column chromatography, and SOURCE 30Q column chromatography
-
two isoforms, homogeneity
-
ammonium sulfate precipitation, HiTrap Q column chromatography, and Resource S column chromatography
-
good results of purification is obtained on silanized CPG or keratin coated silica gel supports
-
isoenzyme PE I and PE II; isoenzyme PE II
-
ammonium sulfate precipitation, Sephadex G-100 gel filtration, and Sephadex C-50 gel filtration
-
isoenzyme PME I and PME II
-
partial
-
heparin-Sepharose column chromatography, S-sepharose column chromatography, and Superdex-75 gel filtration
Q1PAH6
affinity purification with immobilized pectin methylesterase-inhibitor protein; affinity purification with immobilized pectin methylesterase-inhibitor protein; affinity purification with immobilized pectin methylesterase-inhibitor protein
P83948, Q8GS16
ammonium sulfate precipitation and NH-Sepharose 4B PME-inhibitor column chromatography
-
DEAE-Sepharose column chromatography and PME-IP affinity chromatography
-
from fruit rag tissue
-
Hi-Trap SP column chromatography and heparin affinity column chromatography
-
pectinesterase I and II
-
-
Cucumis sativa
-
ammonium sulfate precipitation, Q Sepharose column chromatography, and Superdex 200 gel filtration
-
-
Erwinia chrysanthemi
-
homogeneity, one-step purification
Erwinia chrysanthemi
-
recombinant protein and native protein from host
-
partial
Q94FS5, Q94FS6, Q9FVF9
partial, 3 isoenzymes: I, II and III
-
native isozymes PME1 389fold and PME2 125fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
ammonium sulfate precipitation
-
phenyl Sepharose column chromatography and Sephacryl S100 gel filtration
B2VPR8, D8VPP5
resource Q column chromatography
-
partial, isoenzyme PE I and PE II
-
isoenzyme PE I and isoenzyme PE II
-
ammonium sulfate precipitation, dialysis, and DEAE-Sephadex gel filtration
-
partial purification by ammonium sulfate precipitation and dialysis
-
ammonium sulfate fractionation
-
native enzyme from pollen by gel filtration, anion exchange chromatography and isoelectric focusing
Q17ST3
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
-
Ni-NTA column chromatography
V9Q624
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
diverse isozymes, DNA sequence anaylsis, phylogenetic tree, PME transcriptomes, overview
-
DNA sequence and phylogenetic analysis; DNA sequence and phylogenetic analysis; DNA sequence and phylogenetic analysis; DNA sequence and phylogenetic analysis; DNA sequence and phylogenetic analysis; DNA sequence and phylogenetic analysis; DNA sequence and phylogenetic analysis; DNA sequence and phylogenetic analysis; DNA sequence and phylogenetic analysis; DNA sequence and phylogenetic analysis; DNA sequence and phylogenetic analysis
O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6
expressed in Escherichia coli strain JM101, IPTG induction at 37C instead of 25-28C 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
-
YFP-tagged protein expressed in host
-
expressed in Pichia pastoris
-
expressed in Pichia pastoris strain GS115
-
overexpression under control of the Aspergilus oryzae TEF1 promoter
-
expressed in Escherichia coli Top10F' cells
-
DNA sequence anaylsis, overview
-
expressed in Escherichia coli
Erwinia chrysanthemi
-
expression in Bacillus subtilis
Erwinia chrysanthemi
-
expression of wild-type and mutant enzymes in Escherichia coli strain NM522
Erwinia chrysanthemi
-
overexpression in Escherichia coli
Erwinia chrysanthemi
-
expressed in Escherichia coli
-
expressed in Pichia pastoris as secretory protein
-
luPME5 isoform
Q94FS5, Q94FS6, Q9FVF9
expressed in Nicotiana benthamiana fused with the gene for the green fluorescent protein
-
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
-
expressed as GFP-fusion protein in host strain, overexpression of PME results in reduced pollen tube growth
-
expressed in Nicotiana tabacum fused with the gene for the green fluorescent protein
-
expressed in Pichia pastoris strain KM71
B2VPR8, D8VPP5
DNA sequence anaylsis, phylogenetic tree, overview
-
expressed in Pichia pastoris strain GS115
-
DNA sequence anaylsis,phylogenetic tree, PME transcriptomes, overview
-
DNA and amino acid sequence determination and analysis, expression in Escherichia coli
Q17ST3
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
Q43143
expressed in Pichia pastoris
V9Q624
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform PME3 is induced upon infection with Botrytis cinerea and Pectobacterium carotovorum. The enzyme expression is induced upon herbivore attack as a defense mechanism
-
upon infection, Pectobacterium carotovorum and Botrytis cinerea induce in Arabidopsis a rapid expression of isoform PME3
-
the enzyme is activated in response to heat shock. Pectin methylesterae activity during the 40C treatment (2 h) is higher, by about 2.2fold, than that with the 28C control treatment
-
isoform PME3 is induced upon infection with Botrytis cinerea and Pectobacterium carotovorum. The enzyme expression is induced upon herbivore attack as a defense mechanism
-
most pectin methylesterase genes from Phytophthora capsici present a decreasing trend of expression from 1 to 5 dpi in tomato fruits. In cucumber fruits, expression levels decrease from 5 to 7 dpi
-
the expression levels of the pectin methylesterase genes from Phytophthora capsici increase from 1 to 7 dpi in pepper. In fruits from pepper and tomato fruits, peaks are reached at 7 dpi. In cucumber fruits, each gene shows minor expression levels from 1 to 3 dpi and exhibits definite peaks at 5 dpi
-
most pectin methylesterase genes from Phytophthora capsici present a decreasing trend of expression from 1 to 5 dpi in tomato fruits. In cucumber fruits, expression levels decrease from 5 to 7 dpi
Phytophthora capsici SD33
-
-
the expression levels of the pectin methylesterase genes from Phytophthora capsici increase from 1 to 7 dpi in pepper. In fruits from pepper and tomato fruits, peaks are reached at 7 dpi. In cucumber fruits, each gene shows minor expression levels from 1 to 3 dpi and exhibits definite peaks at 5 dpi
Phytophthora capsici SD33
-
-
isoform PME3 is induced upon infection with Botrytis cinerea and Pectobacterium carotovorum. The enzyme expression is induced upon herbivore attack as a defense mechanism
-
pectin methylesterase expression decreases during the color change period in fruit ripening
-
pectin methylesterase expression increases at the end of fruit ripening
-
pectin methylesterase expression is positively regulated by cAMP receptor protein-like protein and RpfF
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
-
fruit juice industry
D178A
Erwinia chrysanthemi
-
site-directed mutagenesis, inactive mutant
D199A
Erwinia chrysanthemi
-
site-directed mutagenesis, inactive mutant
M306A
Erwinia chrysanthemi
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q153A
Erwinia chrysanthemi
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q177A
Erwinia chrysanthemi
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R267A
Erwinia chrysanthemi
-
site-directed mutagenesis, inactive mutant
T272A
Erwinia chrysanthemi
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V198A
Erwinia chrysanthemi
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W269A
Erwinia chrysanthemi
-
site-directed mutagenesis, inactive mutant
additional information
-
the degree of methylesterification of galacturonic acids is affected in the pme3-1 mutant enzyme
395A396A
-
an enzymatically inactive proPME mutant
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
Q9FY03
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
Q43143
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
-
responsible for phase separation and cloud loss in fruit juice manufacturing
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
-
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 (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
-
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
-
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
-
used for juice clarification and gelation of frozen concentrates, destabilizing agent for pectin material in fruit juices and concentrates
food industry
-
inhibition of pectin methylesterase directly after juice extraction is crucial in the production of storable citrus juice products
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
-
enzyme is known to be responsible for cloud loss in juice processing and storage
food industry
-
pectin methylesterase can positively or negatively affect structural quality of plant-based foods (cloud stability, viscosity, texture)
food industry
-
responsible for phase separation and cloud loss in fruit juice manufacturing
food industry
Erwinia chrysanthemi
-
exogenous pectin methylesterase is applied in texture engineering of thermally processed intact fruits and vegetables, for example, via enzyme infusion
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
diagnostics
Q17ST3
pectin methylesterase is an allergenic marker for the sensitization to Russian thistle, Salsola kali pollen
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