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 ACCESSION NO.
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
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
-
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
reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
hydrolysis of carboxylic ester
Q12535
de-esterification
hydrolysis of carboxylic ester
-
de-esterification
PATHWAY
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 ACCESSION NO.
COMMENTARY
LITERATURE
luPME
Q9FVF9
-
Nicotiana tabacum pollen tube PME1
-
expression of the described pre-pro-PME is restricted to pollen and pollen tubes
Novoshape
-
carbohydrate esterase family 8, commercial preparation
Novoshape
-
commercial preparation
Ole e 11
-
-
Ole e 11.0101
D8VPP5
isoform
Ole e 11.0102
B2VPR8
isoform
P65
-
-
-
-
PE
-
-
-
-
pectase
-
-
-
-
pectin demethoxylase
-
-
-
-
pectin esterase
-
-
pectin esterase
Q1PAH6
-
pectin methoxylase
-
-
-
-
pectin methyl esterase
-
-
-
-
pectin methyl esterase
-
-
pectin methyl esterase
-
-
pectin methyl esterase
-
-
pectin methyl esterase
Castilleja indivisa
-
-
pectin methyl esterase
-
-
pectin methyl esterase
Citrus sp.
-
-
pectin methyl esterase
-
-
pectin methyl esterase
-
-
pectin methyl esterase
-
-
pectin methyl esterase
-
-
pectin methyl esterase
Q9FY03
-
pectin methyl esterase
-
-
pectin methyl esterase
-
-
pectin methylesterase
-
-
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6
-
pectin methylesterase
-
-
pectin methylesterase
Q12535
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
Q1PAH6
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
Citrus reticulata Citrus sinensis
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
-, B2VPR8, D8VPP5
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
-
pectin methylesterase
Phytophthora capsici SD33
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
-
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
P14280
-
pectin methylesterase
-
-
pectin methylesterase
-
-
pectin methylesterase
Q94B16 and Q9XGT5
-
pectin methylesterase
-
-
pectin methylesterase 3
-
-
pectine methylesterase
Q17ST3
-
pectinesterase
-
-
pectinmethylesterase
-
-
pectinmethylesterase
-
-
pectinmethylesterase
-
-
pectinmethylesterase
-
-
pectinoesterase
-
-
-
-
pectofoetidin
-
-
-
-
PME
-
-
-
-
PME
O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6
-
PME
Castilleja indivisa
-
-
PME
Citrus sp.
-
-
PME
-
-
PME
-, B2VPR8, D8VPP5
-
PME
Q17ST3
-
PME
Q94B16 and Q9XGT5
-
PME I
Q1PAH6
isozyme
PME II
Q1PAH6
isozyme
PME III
Q1PAH6
isozyme
PME1
-
isoform
PME1
G2XK68
isoform
PME1
Phytophthora capsici SD33
G2XK68
isoform
-
PME2
-
isoform
PME2
G2XKU9
isoform
PME2
Phytophthora capsici SD33
G2XKU9
isoform
-
PME3
P83948
isoform
PME3
G2XKV0
isoform
PME3
Phytophthora capsici SD33
G2XKV0
isoform
-
PME4
Q8GS16
isoform
PME4
G2XKV1
isoform
PME4
Phytophthora capsici SD33
G2XKV1
isoform
-
PME5
G2XKV2
isoform
PME5
Phytophthora capsici SD33
G2XKV2
isoform
-
PME6
F4MIB0
isoform
PME6
Phytophthora capsici SD33
F4MIB0
isoform
-
PME7
G2XKV3
isoform
PME7
Phytophthora capsici SD33
G2XKV3
isoform
-
PME8
G2XKV4
isoform
PME8
Phytophthora capsici SD33
G2XKV4
isoform
-
PME9
G2XKV5
isoform
PME9
Phytophthora capsici SD33
G2XKV5
isoform
-
PMEU1
Q43143
-
pollen specific PME
-
-
RIP
-
the RIP purified is identified as a mature form of pectin methylesterase, the purified native protein shows both pectin methylesterase and ribosome-inactivating protein activity
Sal k 1
Q17ST3
-
thermally tolerant pectin methylesterase
-
-
thermolabile pectin methylesterase
-, P83948, Q8GS16
-
TL-PME
-, P83948, Q8GS16
-
additional information
Q17ST3
the enzyme belongs to the plant pectin methylesterase family
CAS REGISTRY NUMBER
COMMENTARY
9025-98-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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
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
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
a plant pathogen, strain B374
-
-
Manually annotated by BRENDA team
strain 3937
-
-
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
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
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
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
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 ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
the number of adventitious roots is 30% increased in the pme3-1 mutant
metabolism
-
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
-
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
-
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
-
although foliar pectin methylesterase activity is related to methanol emission, other factors must also be considered when predicting methanol emission
physiological function
-
isoform PME3 plays a role in adventitious rooting
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
-
hydrolyzes pectin from citrus and sugar beet
-
-
?
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
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
-
-
-
?
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
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
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
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
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, Lewia 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
B2VPR8, D8VPP5, -
-
-
-
?
pectin + H2O
methanol + pectate
show the reaction diagram
P85076
-
-
-
?
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
-
-
-
-
?
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
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
-
-
-
-
?
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
-
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
-
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
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
?
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
-
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
-
-
-
methylated oligogalacturonides + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
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 ACCESSION NO.
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
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
-
-
-
-
?
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
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
-
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
?
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
-
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
-
-
-
?
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 ACCESSION NO.
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
specific activity is higher in the presence than in the absence of 5 mM Ca2+
Ca2+
-
specific activity is higher in the presence than in the absence of 5 mM Ca2+
CaCl2
-
activates with increasing temperature to a maximal value
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
Li+
Acrocylindrium sp.
-
-
Li+
Acrocylindrium sp.
-
LiCl, activates
Mg2+
-
stimulates
Mg2+
Acrocylindrium sp.
-
activates
Mg2+
-
activates
Mg2+
-
stimulates
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
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
NH4Cl
-
activates
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
ZnSO4
-
activates
Mg2+
-
highest activity at 15 mM Mg2+, further increase in concentration results in the decline of the enzyme activity
additional information
Q43143
PMEU1 is a salt-dependent isozyme
additional information
-
the enzyme does not require salt for activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
Acrocylindrium sp.
-
-
(NH4)Cl
Acrocylindrium sp.
-
-
Ca2+
-
60 mM Ca2+ decreases enzyme activity at atmospheric pressure and 45-60C, but increases activity at elevated pressure up to 300 MPa
D-galacturonate
-
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
gallocatechin gallate
Castilleja indivisa, Citrus sp., Cuscuta pentagona, Solanum lycopersicum
-
-
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
-
-
Lauryl sulfate
-
-
NaCl
-
activity decreases in the presence of 0.1 M NaCl and is 4times lower in 0.5 M NaCl
pectate
-
-
-
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
-
competitive
Polygalacturonate
-
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
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
-
0.1% complete inactivation
Silver nitrate
-
-
sodium carbonate
-
-
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
-
mutant V198A, pH 7.0, 30C
-
0.08
-
Pectin
-
pH 8.3, 50C, isozyme PME2
-
0.13
-
Pectin
-
wild-type enzyme, pH 7.0, 30C
-
0.22
-
Pectin
-
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
-
mutant M306A, pH 7.0, 30C
-
0.71
-
Pectin
-
immobilized enzyme, at 20C
-
0.77
-
Pectin
-
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
-
mutant Q153A, pH 7.0, 30C
-
additional information
-
citrus pectin
-
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
-
steady-state kinetics, kinetic mechanism
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
40
-
Pectin
-
mutant Q177A, pH 7.0, 30C
-
59
-
Pectin
-
mutant M306A, pH 7.0, 30C
-
68
-
Pectin
-
mutant V198A, pH 7.0, 30C
-
232
-
Pectin
-
mutant Q153A, pH 7.0, 30C
-
425
-
Pectin
-
mutant T272A, pH 7.0, 30C
-
450
-
Pectin
-
wild-type enzyme, pH 7.0, 30C
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
16
-
Polygalacturonate
-
-
4.2
-
polygalacturonic acid
Q43234, Q9M5J0
pH 5.6
additional information
-
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.246
-
-
crude extract
0.82
-
-
crude extract
1.1
-
Q1PAH6
crude homogenate
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
5.83
-
-
crude extract, at 20C
6.5
-
-
after 7.93fold purification
7.59
-
Q12535
in the presence of 5 mM Ca2+, pH 6.0, 30C
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
70.92
-
-
after 12.2fold purification, at 20C
115
-
-
-
124
-
-
isoenzyme PE I
206
-
-
purified isozyme PME1
242.5
-
-
purified enzyme, pH 7.0, 22C
834
847
-
purified isozymes
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
-
-
-
additional information
-
Citrus reticulata, Citrus reticulata Citrus sinensis, Citrus sinensis
-
activity in different cultivars, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
5.5
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
-
-
assay at
7
-
-
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, Citrus sinensis, Solanum lycopersicum
-
-
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
7.9
-
-
-
8
8.5
-
two pH optima
8
8.5
-
in phosphate buffer
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
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
4.5
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
-
about 55% activity at pH 5-6
5
9
-
pH 5: 58% of maximal activity, pH 9: 64% of maximal activity, isoenzyme PE I
5.2
7.6
-
pH 5.2: about 75% of maximal activity, pH 7.6: about 70% of maximal activity
5.6
7.6
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
7.5
11
-
pH 7.5: about 50% of maximal activity, pH 11.0: about 85% of maximal activity
7.5
9.5
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
Citrus reticulata, Citrus reticulata Citrus sinensis, Citrus sinensis
-
assay at
22
-
-
assay at
22.5
-
-
assay at
24
-
-
assay at room temperature
25
35
Clostridium multifermentans
-
-
30
-
Cucumis sativa
-
assay at
30
-
-
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
40
-
-
soluble enzyme
40
-
Acrocylindrium sp., Aspergillus japonicus, Athelia rolfsii, Cercosporella herpotrichoides
-
-
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
-
-
assay at
50
-
-
immobilized enzyme
52
-
-
enzyme immobilized on polyethylene terephthalate
52.5
55
-
at pH 7, sharp optimum
55
-
Fragaria sp.
-
-
55
-
-
at atmospheric pressure
60
65
-
at 100-200 MPa
60
-
-
free 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+
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
70
-
50% of activity at 30C, 30% of activity at 70C
30
70
-
PME activity during isobaric-isothermal treatment, overview
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
80
-
-
no activity
additional information
-
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
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
-
P83218
isoelectric focusing
9.8
-
-
isoelectric focusing
9.8
-
-
calculated from amino acid sequence
10.1
-
-
isoelectric focusing
additional information
-
-
acidic and alkaline isoforms detected in both varieties
additional information
-
-
acidic isoelectric pH
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
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
-
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; 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
Citrus reticulata, Citrus reticulata Citrus sinensis, Citrus sinensis
-
juice
Manually annotated by BRENDA team
Q43143
young developing, isozyme profile, expression analysis, overview
Manually annotated by BRENDA team
-
PME activity increases with fruit maturation
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
P83948, Q8GS16
isoform PME1 is a minor citrus fruit thermolabile pectin methylesterase; isoform PME2 is the major thermolabile pectin methylesterase isoenzyme accumulated in citrus pulp tissue
Manually annotated by BRENDA team
-
isoenzyme B and C in comparable amounts
Manually annotated by BRENDA team
Q43234, Q9M5J0
-
Manually annotated by BRENDA team
Q94FS5, Q94FS6, Q9FVF9
-
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
Citrus reticulata, Citrus reticulata Citrus sinensis
-
-
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
-
photosynthetic active and vascular tissues
Manually annotated by BRENDA team
Q43143
isozyme profile, expression analysis, overview
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
O23447, O80722, Q5MFV6, Q5MFV8, Q84WM7, Q8GXA1, Q8L7Q7, Q9LSP1, Q9LY18, Q9LY19, Q9SMY6
tube, the enzyme belongs to the group II of pectinesterases in Arabidopsis thaliana pollen; tube, the enzyme belongs to the group II of pectinesterases in Arabidopsis thaliana pollen; tube, the enzyme belongs to the group II of pectinesterases in Arabidopsis thaliana pollen; tube, the enzyme belongs to the group II of pectinesterases in Arabidopsis thaliana pollen; tube, the enzyme belongs to the group II of pectinesterases in Arabidopsis thaliana pollen; tube, the enzyme belongs to the group II of pectinesterases in Arabidopsis thaliana pollen; tube, the enzyme belongs to the group II of pectinesterases in Arabidopsis thaliana pollen; tube, the enzyme belongs to the group I of pectinesterases in Arabidopsis thaliana pollen; tube, the enzyme belongs to the group I of pectinesterases in Arabidopsis thaliana pollen; tube, the enzyme belongs to the group I of pectinesterases in Arabidopsis thaliana pollen; tube, the enzyme belongs to the group I of pectinesterases in Arabidopsis thaliana pollen
Manually annotated by BRENDA team
B2VPR8, D8VPP5, -
-
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
additional information
-
isoform PME3 is ubiquitously expressed in Arabidopsis thaliana, particularly in vascular tissues
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5200
-
-
isozyme PME2, gel filtration
13000
-
-
bands of 37000, 27000, and 13000 Da are detected in crude PME extract, SDS-PAGE
25100
-
-
isozyme PME1, gel filtration
27000
-
-
-
27000
-
-
bands of 37000, 27000, and 13000 Da are detected in crude PME extract, SDS-PAGE
27500
27800
-
-
28000
-
-
-
28500
-
-
isoenzyme PE II from seed hull, gel filtration
30000
-
-
isoenzyme PE II from pod, gel filtration
33000
-
P83218
SDS-PAGE
33000
-
-
SDS-PAGE
33500
-
-
two bands: 33500 Da and 43000 Da, SDS-PAGE
33500
-
-
SDS-PAGE
33600
-
-
SDS-PAGE
34000
-
-
gel filtration
34000
-
-
SDS-PAGE
35000
37000
-
isoenzyme PE II, gel filtration
35000
-
-
SDS-PAGE
35400
-
P85076
calculated from amino acid sequence
36000
-
-
bands of 37000, 27000, and 13000 Da are detected in crude PME extract, SDS-PAGE
36200
-
-
isoenzyme I and II, gel filtration
37000
-
-
gel filtration
37000
-
-
gel filtration
37000
-
-
gel filtration
37000
-
-
gel filtration
37000
-
-
SDS-PAGE
38000
-
Q94FS5, Q94FS6, Q9FVF9
gel filtration, very basic isoform, i.e. luPME5
40100
-
-
gel filtration
41000
-
-
SDS-PAGE
42000
-
Q1PAH6
the three PME isoforms show the same molecular weight of 42000 Da, SDS-PAGE
43000
-
-
two bands: 33500 Da and 43000 Da, SDS-PAGE
44000
-
-
isoenzyme PE I from seed hull, gel filtration
45000
-
-
isoenzyme PE I, gel filtration
46000
-
-
isoenzyme PE I from pod, gel filtration
46000
-
-
isoform I, SDS-PAGE
47000
-
-
isoform II, SDS-PAGE
50000
-
-
gel filtration
50000
-
P85076
purified enzyme, SDS-PAGE
53000
-
-
gel filtration
57000
-
-
guava PME contains two isoforms, one with 57000 Da molecular mass, SDS-PAGE
99000
-
-
guava PME contains two isoforms, one with 99000 Da molecular mass, SDS-PAGE
100000
-
-
isoenzyme I, gel filtration
110000
-
-
isoenzyme II, gel filtration
110000
-
Q94FS5, Q94FS6, Q9FVF9
gel filtration, neutral and basic isoform
141300
-
-
gel filtration
158000
-
-
SDS-PAGE
400000
-
Clostridium multifermentans
-
-
additional information
-
-
primary structure
additional information
-
-
-
additional information
-
-
linear arrangement of disulfide bridges along the polypeptide chain with two consecutive disulfide bridges, disulfide bridges connect Cys98 with Cys125 and Cys166 with Cys200
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 36200, SDS-PAGE
?
-
x * 43000, isoenzyme I, SDS-PAGE
?
-
x * 35900, isoenzyme A, SDS-PAGE; x * 40300, isoenzyme B, SDS-PAGE; x * 43200, isoenzyme C, SDS-PAGE
?
-
x * 38000, SDS-PAGE
?
-
x * 33792, calculation from nucleotide sequence
?
-
three different isoforms with molecular weights of 75000, 83000, and 91000 detected in SDS-PAGE
?
-
x * 41000, 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 * 40800, SDS-PAGE
?
-
x * 38000, SDS-PAGE, protein from host; x * 45000, SDS-PAGE, recombinant protein
?
-
x * 39000-41500, calculated from the deduced amino acid sequence for the mature protein; x * 40000, SDS-PAGE; x * 60300, calculated from the deduced amino acid sequence of the pre-pro-protein
?
Q17ST3
x * 40000, native enzyme, SDS-PAGE, x * 37214, native glycosylated enzyme, mass spectrometry
?
-
x * 34500-35000, four isozymes, SDS-PAGE
?
B2VPR8, D8VPP5, -
x * 37386, isoform Ole e 11.0101, calculated from amino acid sequence; x * 39647, recombinant enzyme, calculated from amino acid sequence; x * 40000, recombinant enzyme, SDS-PAGE
?
P83948, Q8GS16
x * 34341, isoform PME4, MALDI-TOF mass spectrometry; x * 34467, isoform PME2, MALDI-TOF mass spectrometry; x * 34485, isoform PME1, MALDI-TOF mass spectrometry; x * 35000, isoform PME2, SDS-PAGE
?
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
x * 36200, isoform PME3, calculated from amino acid sequence; x * 36900, isoform PME2, calculated from amino acid sequence; x * 37700, isoform PME1, calculated from amino acid sequence; x * 37700, isoform PME7, calculated from amino acid sequence; x * 37700, isoform PME9, calculated from amino acid sequence; x * 37800, isoform PME8, calculated from amino acid sequence; x * 37900, isoform PME5, calculated from amino acid sequence; x * 38100, isoform PME4, calculated from amino acid sequence; x * 38200, isoform PME6, calculated from amino acid sequence
?
-
x * 33300, mature enzyme, estimated from SDS-PAGE
?
Aspergillus oryzae KBN616
-
x * 33792, calculation from nucleotide sequence
-
?
Phytophthora capsici SD33
-
x * 36200, isoform PME3, calculated from amino acid sequence; x * 36900, isoform PME2, calculated from amino acid sequence; x * 37700, isoform PME1, calculated from amino acid sequence; x * 37700, isoform PME7, calculated from amino acid sequence; x * 37700, isoform PME9, calculated from amino acid sequence; x * 37800, isoform PME8, calculated from amino acid sequence; x * 37900, isoform PME5, calculated from amino acid sequence; x * 38100, isoform PME4, calculated from amino acid sequence; x * 38200, isoform PME6, calculated from amino acid sequence
-
dimer
Q94FS5, Q94FS6, Q9FVF9
isoform luPME1: 2 * 56000, SDS-PAGE, isoform luPME3: 2 * 58000, SDS-PAGE
monomer
-
1 * 40000, isoenzyme PE II, SDS-PAGE; 1 * 45000-48000, isoenzyme PE I, SDS-PAGE
monomer
-
1 * 37000, SDS-PAGE
monomer
-
1 * 38000, gel filtration
monomer
-
1 * 32400, gel filtration
monomer
Q94FS5, Q94FS6, Q9FVF9
isoform luPME5, 1 * 34000-40000, SDS-PAGE
monomer
-
1 * 50000, SDS-PAGE, native mass by gel filtration
monomer
-
1 * 37000, SDS-PAGE, native mass by gel filtration
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
-
the enzyme possesses a parallel beta-helix architecture, three dimensional structure of PME, overview
additional information
-
primary structures of isozymes, structural and processing motifs, three-dimensional structure analysis, overview
additional information
-
three-dimensional structure analysis, overview
additional information
-
structural and processing motifs, three-dimensional structure analysis, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
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
no modification
-
-
no modification
-
probably not a glycoprotein
side-chain modification
-
glycoprotein
glycoprotein
-
-
no modification
-
no glycoprotein
side-chain modification
-
N-linked glycoprotein
proteolytic modification
-
the inactive enzyme precursor, Pro-PME, is activated to the mature soluble enzyme, which is excreted to the cell wall
proteolytic modification
-
the enzyme contains a pro-region, role of the PRO region in PME targeting and function
side-chain modification
-
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
B2VPR8, D8VPP5, -
-
proteolytic modification
-
the enzyme contains a pro-region, role of the PRO region in PME targeting and function
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
no modification
-
no glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method
-
hanging drop vapor diffusion method
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
-
complex between enzyme and PMEI, vapor diffusion technique
P14280
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.1
10
-
stable
1.1
-
-
5C, 72 h, stable
3
7
-
isoenzyme PE I is stable
4
7
-
stable
4
8.5
Acrocylindrium sp.
-
24 h, 30C, stable
4
9
-
40C, 30 min, stable
4
9
-
isoenzyme PE II is stable
4
-
-
pectinesterase I is stable, complete loss of activity of pectinesterase II after 6 h
5
7
-
at both sides of this pH range the stability decreases slightly
7
-
-
pectinesterase I and II, stable for at least 24 h
9
-
-
no activity at pH 9
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
55
-
incubation at 30C has little but significant effect on enzyme activity, the incubation at 55C abolishes over 95% of enzyme activity
30
-
Acrocylindrium sp., Athelia rolfsii
-
-
30
-
-
pectinesterase II is labile
30
-
-
57% loss of activity after 20 h at pH 1.1, 23% loss of activity after 20 h at pH 2.0
30
-
Acrocylindrium sp.
-
24 h, pH 4.0-8.5, quite stable
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
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
35
-
-
10 min, stable
38
-
Clostridium multifermentans
-
5-15 min, inactivation
40
50
-
stable
40
-
-
30 min, pH 4.0-9.0, isoenzyme PE II is stable
40
-
-
16 min, in absence of substrate, stable up to
40
-
-
5 h, stable
40
-
-
no loss of activity at atmospheric pressure and at pressures up to 700 MPa
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
45
-
-
10 min, 45% loss of maximal activity
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
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.
50
98
-
no loss of activity within 60 min
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
50
-
-
10 min, 50% loss of activity
50
-
-
60 min, 20% loss of activity
50
-
-
pH 8.0, stable up to
50
-
-
stable up to
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
50
-
-
pH 6.0, 16 min, 50% loss of activity
50
-
-
half-life: 10 min
50
-
-
no loss of activity after 20 min
50
-
-
43% loss of activity within 15 min at atmospheric pressure
50
-
-
no loss of activity within 2 h
50
-
-
90% of activity remaining after 50 min
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
54
63
-
inactivation rate constants increase with increasing temperature
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
55
70
-
PME thermal degradation kinetics, modeling, overview
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
55
-
Acrocylindrium sp.
-
-
55
-
-
5-15 min, inactivation
55
-
-
10 min, pH 4.0, inactivation; pH 4.0, inactivation
55
-
Acrocylindrium sp.
-
stable
55
-
-
stable up to, sharp inactivation above
55
-
-
50% loss of activity after 5 min
55
-
-
almost 50% loss of activity after 5 min
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
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
55
-
-
75% of activity after 60 min
55
-
-
rapid inactivation at temperatures above 55C
60
80
Cucumis sativa
-
maximal thermostability in Bis-Tris buffer, pH 6.7, supplemented with 60% glycerol and 1.25 M NaCl
60
80
-
maximal thermostability in citrate buffer, pH 4.5, supplemented with 50% glycerol, addition of sucrose and trehalose increase thermal stability
60
90
-
kinetic model for thermal inactivation of multiple PME, kinetics, at pH 3.5-4.5, overview
60
-
-
10 min, inactivation
60
-
-
20 min, about 50% loss of activity of the soluble enzyme, about 20% loss of activity of the immobilized enzyme
60
-
-
complete loss of activity after 5 min
60
-
-
complete loss of activity after 2 min
60
-
-
inactivation at atmospheric pressure
60
-
-
50% of activity lost within 5 min
60
-
-
15 min stable, loss of activity after 15 min
60
-
-
45% of activity remaining after 8 min
60
-
-
5 min, thermolabile isozyme, complete inactivation
62
-
-
1 min, 50% inactivation
63
91
Citrus reticulata Citrus sinensis, Citrus reticulata, Citrus sinensis
-
thermostability of the enzyme from juice of different cultivars, overview
64
-
-
inactivation above at atmospheric pressure
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
65
-
-
20 min, about 75% loss of activity of the soluble enzyme, about 20% loss of activity of the immobilized enzyme
65
-
-
20 min, complete loss of activity of the soluble enzyme, about 50% loss of activity of the immobilized enzyme
65
-
-
complete loss of activity after 5 min
65
-
-
progressive loss of activity even at high pressure conditions
65
-
-
native enzyme stable for 30 min, 60% of activity remaining after 2 h
68
-
-
more than 90% of activity lost within 5 min
70
90
-
z-values for thermal inactivation range from 15 to 24 C, purified enzyme, z-value: temperature increase necessary to obtain a 10fold decrease of the time needed for 90% reduction of enzyme activity
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
70
-
Acrocylindrium sp., Cucumis sativus
-
-
70
-
-
5-15 min, inactivation
70
-
Acrocylindrium sp.
-
10 min, complete inactivation
70
-
-
complete loss of activity within 5 min
70
-
-
20% of activity remaining after 2 h
70
-
-
5 min, thermostable isozyme, complete inactivation
70
-
-
activity decreases at temperatures above 70C
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
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
75
-
-
increase in activity after 30 min of incubation
75
-
-
10% of activity after 60 min
80
-
-
1 min, complete loss of activity
80
-
-
5-15 min, complete inactivation
80
-
-
5-15 min, complete inactivation
80
-
-
2 min, 17% loss of activity
80
-
-
7.6% of activity remaining after 1 min
80
-
-
5 min, purified enzyme, inactivation
80
-
-
5 min, partially purified enzyme, inactivation
85
95
-
5% of activity after 5 min
85
-
-
5-15 min, inactivation
85
-
-
more than 50% of activity remaining after 1 min treatment, less than 10% of activity remaining after 3 min treatment
90
-
Sclerotinia libertiana, Vitis sp.
-
5-15 min, inactivation
90
-
-
slight loss of activity within the first 4 h of incubation, then activity increases and remains high until at least 8 h of total incubation time
90
-
-
complete inactivation within 1 min
95
-
-
no inactivation after 30 s, 51% loss of activity after 60 s
98
-
-
purified PME1 specific activity increases by 9.63% after 60 min incubation at 98C, while purified PME2 retains 66% of its specific activity
100
-
cranberry
-
5-15 min, complete inactivation
106
125
-
only slight loss of activity when incubated for 5 min
additional information
-
-
-
additional information
-
-
activity not completely abolished after pasteurization
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
additional information
-
-
immobilization stabilzes the enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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
-
significant loss of activity after freezing and thawing
-
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 ACCESSION NO.
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
-
4C, stable for at least 1 week
-
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
two isoforms, homogeneity
-
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
-
from fruit rag tissue
-
Hi-Trap SP column chromatography and heparin affinity column chromatography
-
pectinesterase I and II
-
-
Cucumis sativa
-
homogeneity, one-step purification
-
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, -
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
-
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
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
overexpression under control of the Aspergilus oryzae TEF1 promoter
-
DNA sequence anaylsis, overview
-
expressed in Escherichia coli
-
expression in Bacillus subtilis
-
expression of wild-type and mutant enzymes in Escherichia coli strain NM522
-
overexpression in Escherichia coli
-
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
-
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
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
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; 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; 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; 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; 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; 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; 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; 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; 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
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
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; 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; 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; 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; 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; 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; 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; 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; 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
F4MIB0, G2XK68, G2XKU9, G2XKV0, G2XKV1, G2XKV2, G2XKV3, G2XKV4, G2XKV5
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; 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; 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; 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; 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; 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; 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; 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; 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
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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; 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; 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; 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; 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; 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; 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; 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; 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
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pectin methylesterase expression decreases during the color change period in fruit ripening
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pectin methylesterase expression increases at the end of fruit ripening
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pectin methylesterase expression is positively regulated by cAMP receptor protein-like protein and RpfF
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D178A
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site-directed mutagenesis, inactive mutant
D199A
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site-directed mutagenesis, inactive mutant
M306A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q153A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q177A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R267A
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site-directed mutagenesis, inactive mutant
T272A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V198A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W269A
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site-directed mutagenesis, inactive mutant
additional information
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the degree of methylesterification of galacturonic acids is affected in the pme3-1 mutant enzyme
395A396A
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an enzymatically inactive proPME mutant
additional information
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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 ACCESSION NO.
COMMENTARY
LITERATURE
food industry
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responsible for phase separation and cloud loss in fruit juice manufacturing
food industry
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used for various applications in fruit processing e.g. texture improvement of fruit pieces, juice extraction, concentration and clarification of fruit juices
food industry
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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
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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
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exogenous pectin methylesterase is applied in texture engineering of thermally processed intact fruits and vegetables, for example, via enzyme infusion
food industry
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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
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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
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used for juice clarification and gelation of frozen concentrates, destabilizing agent for pectin material in fruit juices and concentrates
food industry
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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
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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
-
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
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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
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destabilizes pectinaceous materials in fruit juices and concentrates and modifies the texture of fruit and vegetable products
food industry
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pectin methylesterase can positively or negatively affect structural quality of plant-based foods (cloud stability, viscosity, texture)