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Information on EC 3.1.1.11 - pectinesterase and Organism(s) Dickeya chrysanthemi and UniProt Accession P0C1A8
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3.1.1.11 pectinesteraseSpecify your search results
Word Map
- 3.1.1.11
- polygalacturonase
- juice
- tomato
- orange
-
ripening
-
firmness
- citrus
-
softening
-
pectic
- pmeis
-
texture
- esterification
- pectate
- cellulase
-
methylesterification
-
postharvest
- pulp
- homogalacturonans
-
de-esterification
-
shelf
-
galacturonic
- hemicellulose
-
pectinolytic
- pectinases
-
cloud
-
de-esterified
-
pasteurization
- carrot
- valencia
-
kiwi
- xyloglucan
-
expansins
- food industry
-
methoxylated
- endo-polygalacturonase
- chrysanthemi
- oligogalacturonides
-
pollen-specific
-
blanch
-
ripening-related
-
wall-modifying
- ficus
-
pectin-degrading
- mango
- 1-methylcyclopropene
-
methyl-esterified
- endo-pg
- grapefruit
- rhamnogalacturonan
- achene
-
wall-degrading
- industry
- diagnostics
The taxonomic range for the selected organisms is: Dickeya chrysanthemi
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
pectin methylesterase, pectinesterase, pectin methyl esterase, pectinmethylesterase, pectin esterase, pme i, sal k 1, atpme3, hms-1, pmeu1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
P65
-
-
-
-
PE
-
-
-
-
pectase
-
-
-
-
pectin demethoxylase
-
-
-
-
pectin methoxylase
-
-
-
-
pectin methyl esterase
pectin methylesterase
pectinoesterase
-
-
-
-
pectofoetidin
-
-
-
-
PME
pectin methyl esterase
-
-
-
-
pectin methylesterase
-
-
-
-
PME
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pectin + n H2O = n methanol + pectate
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
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
pectin pectylhydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9025-98-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
citrus pectin + H2O
methanol + citrus pectate
-
highest activity with pectin with an esterification degree of 50%
-
?
pectin + H2O
?
-
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
methanol + pectate
-
the enzyme catalyses the essential first step in bacterial invasion of plant tissues
-
-
?
pectin + H2O
methanol + pectate
-
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
-
the enzyme catalyzes the hydrolysis of methylester groups from the galacturonic acid residues of homogalacturonan chains, the major component of pectin
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pectin + H2O
?
-
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
methanol + pectate
-
the enzyme catalyses the essential first step in bacterial invasion of plant tissues
-
-
?
pectin + H2O
methanol + pectate
-
the enzyme catalyzes the hydrolysis of methylester groups from the galacturonic acid residues of homogalacturonan chains, the major component of pectin
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not inhibited by proteinaceous pectin methylesterase inhibitor from kiwi fruit
-
Polygalacturonate
-
completely deesterified pectin, a competitive inhibitor of PME
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
steady-state kinetics, kinetic mechanism
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 65
-
0°C: about 20% of maximal activity, 65°C: 10% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme possesses a parallel beta-helix architecture, three dimensional structure of PME, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M306A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q153A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q177A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T272A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V198A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
50
60
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freezing and thawing results in a substantial loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli strain NM522
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
-
exogenous pectin methylesterase is applied in texture engineering of thermally processed intact fruits and vegetables, for example, via enzyme infusion
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heikinheimo, R.; Hemil, H.; Pakkanen, R.; Palva, I.
Production of pectin methylesterase from Erwinia chrysanthemi B374 in Bacillus subtilis
Appl. Microbiol. Biotechnol.
35
51-55
1991
Dickeya chrysanthemi, Dickeya chrysanthemi B374
Pitknen, K.; Heikinheimo, R.; Pakkanen, R.
Purification and characterization of Erwinia chrysanthemi B374 pectin methylesterase produced by Bacillus subtilis
Enzyme Microb. Technol.
14
832-836
1992
Dickeya chrysanthemi, Dickeya chrysanthemi B374
-
Shevchik, V.E.; Condemine, G.; Hugouvieux-Cotte-Pattat, N.; Robert-Baudouy, J.
Characterization of pectin methylesterase B, an outer membrane lipoprotein of Erwinia chrysanthemi 3937
Mol. Microbiol.
19
455-466
1996
Dickeya chrysanthemi
Laurent, F.; Kotoujansky, A.; Bertheau, Y.
Overproduction in Escherichia coli of the pectin methylesterase A from Erwinia chrysanthemi 3937: one-step purification, biochemical characterization, and production of polyclonal antibodies
Can. J. Microbiol.
46
474-480
2000
Dickeya chrysanthemi, Dickeya chrysanthemi 3937
Jenkins, J.; Mayans, O.; Smith, D.; Worboys, K.; Pickersgill, R.W.
Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site
J. Mol. Biol.
305
951-960
2001
Dickeya chrysanthemi (P0C1A8), Dickeya chrysanthemi
Fries, M.; Ihrig, J.; Brocklehurst, K.; Shevchik, V.E.; Pickersgill, R.W.
Molecular basis of the activity of the phytopathogen pectin methylesterase
EMBO J.
26
3879-3887
2007
Dickeya chrysanthemi
Bruhn, D.; Mikkelsen, T.N.; Obro, J.; Willats, W.G.; Ambus, P.
Effects of temperature, ultraviolet radiation and pectin methyl esterase on aerobic methane release from plant material
Plant Biol.
11 Suppl 1
43-48
2009
Aspergillus sp., Citrus sinensis, Dickeya chrysanthemi
Jolie, R.P.; Duvetter, T.; Van Loey, A.M.; Hendrickx, M.E.
Pectin methylesterase and its proteinaceous inhibitor: a review
Carbohydr. Res.
345
2583-2595
2010
Aspergillus aculeatus, Aspergillus niger, Dickeya chrysanthemi, Solanum lycopersicum, Daucus carota subsp. sativus
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