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EC Tree
IUBMB Comments The enzyme catalyses the eliminative cleavage of an unsaturated disaccharide from the reducing end of homogalacturonan (the backbone of smooth regions of pectate, also known as de-esterified pectin).
The enzyme appears in viruses and cellular organisms
Synonyms
exopolygalacturonase, exo-pectate lyase, exopectate lyase, exopolygalacturonate lyase, exopl, exopolygalacturonate lyase x, exopectate lyase w,
more
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exocleaving pectate lyase
exopectic acid transeliminase
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Exopolygalacturonate lyase
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exopolygalacturonate lyase X
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exopolymethylgalacturonate lyase
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lyase, exopolygalacturonate
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PECI
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extracellular pectinase
poly (1,4-alpha-D-galacturonide) exolyase
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poly(1,4-alpha-D-galacturonide) exo-lyase
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exocleaving pectate lyase
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exocleaving pectate lyase
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exopectate lyase
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exopectate pectate lyase
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exopectate pectate lyase
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PelW
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PelX
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(1,4-alpha-D-galacturonosyl)n = (1,4-alpha-D-galacturonosyl)n-2 + 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate
(1,4-alpha-D-galacturonosyl)n = (1,4-alpha-D-galacturonosyl)n-2 + 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate
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(1,4-alpha-D-galacturonosyl)n = (1,4-alpha-D-galacturonosyl)n-2 + 4-(4-deoxy-alpha-D-galact-4-enuronosyl)-D-galacturonate
trans-elimination mechanism
Clostridium multifermentans
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elimination
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(1->4)-alpha-D-galacturonan reducing-end-disaccharide-lyase
The enzyme catalyses the eliminative cleavage of an unsaturated disaccharide from the reducing end of homogalacturonan (the backbone of smooth regions of pectate, also known as de-esterified pectin).
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1-methyl-di-D-galacturonate
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alpha-(1-4)-linked, 36% of the activity with di-D-galacturonate
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?
1-methyl-tri-D-galacturonate
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2-methyl-di-D-galacturonate
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alpha-(1-4)-linked, 35% of the activity with di-D-galacturonate
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?
2-methyl-tri-D-galacturonate
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alpha-(1-4)-linked, 19% of the activity with tri-D-galacturonate or 1-methyl-tri-D-galacturonate
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?
3-methyl-tri-D-galacturonate
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DELTA4,5-unsaturated tri-D-galacturonate
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alpha-(1-4)-linked, low activity with PelX
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?
di-D-galacturonate
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alpha-(1-4)-linked
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?
galacturonic acid
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?
heptagalacturonate
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better substrate than polygalacturonate
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?
oligogalacturonate
?
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-
?
pectic acid
4,5-unsaturated digalacturonic acid
poly-D-galacturonic acid
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pectin from citrus
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?
polygalacturonate
unsaturated digalacturonate
polygalacturonate I
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?
polygalacturonate II
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?
additional information
?
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1-methyl-tri-D-galacturonate
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best substrate, alpha-(1-4)-linked
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?
1-methyl-tri-D-galacturonate
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alpha-(1-4)-linked
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?
3-methyl-tri-D-galacturonate
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alpha-(1-4)-linked, 18% of the activity with tri-D-galacturonate or 1-methyl-tri-D-galacturonate
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?
3-methyl-tri-D-galacturonate
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poor substrate only for PelW, not for PelX
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?
hexagalacturonic acid
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better substrate than polygalacturonate
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?
hexagalacturonic acid
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51% of the activity with low molecular polygalacturonic acid
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?
pectic acid
4,5-unsaturated digalacturonic acid
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acid-soluble pectic acid and acid-insoluble pectic acid
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?
pectic acid
4,5-unsaturated digalacturonic acid
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acid-soluble pectic acid and acid-insoluble pectic acid
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?
pectic acid
4,5-unsaturated digalacturonic acid
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?
pentagalacturonic acid
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better substrate than polygalacturonate
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?
pentagalacturonic acid
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better substrate than polygalacturonate
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?
pentagalacturonic acid
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60% of the activity with low molecular polygalacturonic acid
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?
polygalacturonate
unsaturated digalacturonate
Clostridium multifermentans
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?
polygalacturonate
unsaturated digalacturonate
Clostridium multifermentans
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the major end product is O-(4-deoxy-beta-L-threo-hexopyranos-4-enyluronic acid)-(1,4)-D-galacturonic acid
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polygalacturonate
unsaturated digalacturonate
Clostridium multifermentans
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plus one molecule of digalacturonate originating from the nonreducing end of the chain
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polygalacturonate
unsaturated digalacturonate
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?
polygalacturonate
unsaturated digalacturonate
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?
polygalacturonate
unsaturated digalacturonate
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?
polygalacturonate
unsaturated digalacturonate
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?
polygalacturonate
unsaturated digalacturonate
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?
polygalacturonate
unsaturated digalacturonate
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4,5-unsaturated digalacturonic acid
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polygalacturonate
unsaturated digalacturonate
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low molecular polygalacturonic acid, very low activity with high molecular polygalacturonic acid
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?
polygalacturonate
unsaturated digalacturonate
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tetragalacturonic acid
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?
tetragalacturonic acid
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maximal activity, better substrate than polygalacturonate
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tetragalacturonic acid
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tetragalacturonic acid
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maximal activity, better substrate than polygalacturonate
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tetragalacturonic acid
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maximal activity, better substrate than polygalacturonate
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tetragalacturonic acid
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maximal activity, better substrate than polygalacturonate
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tetragalacturonic acid
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52% of the activity with low molecular polygalacturonic acid
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tri-D-galacturonate
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alpha-(1-4)-linked
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tri-D-galacturonate
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alpha-(1-4)-linked, best substrate for both enzyme types
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trigalacturonic acid
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trigalacturonic acid
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poor substrate
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trigalacturonic acid
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trigalacturonic acid
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poor substrate
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trigalacturonic acid
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trigalacturonic acid
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trigalacturonic acid
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trigalacturonic acid
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248% of the activity with low molecular polygalacturonic acid
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?
additional information
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Clostridium multifermentans
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no activity with pectin of high methoxyl content
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?
additional information
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Clostridium multifermentans
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inducible
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?
additional information
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does not cleave digalacturonate
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additional information
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does not cleave digalacturonate
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additional information
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substrate specificity, overview, no activity for both enzyme types with monomethyl-esterified digalacturonate substrates and with 2-methyl-tri-G-galacturonate
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?
additional information
?
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does not cleave digalacturonate
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?
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additional information
?
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Clostridium multifermentans
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inducible
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?
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Ba2+
Clostridium multifermentans
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stimulates
Fe2+
activates, 85% of maximal activity in 0.1 M TES, pH 7.4, 0.1 mM Fe2+
Ca2+
Clostridium multifermentans
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stimulates
Ca2+
Clostridium multifermentans
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greatest stimulation of divalent cations tested, Km: 0.06 mM
Ca2+
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required, optimal concentration is 0.5 mM
Co2+
weak activation
Mg2+
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no effect
Mg2+
Clostridium multifermentans
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stimulates
Mn2+
Clostridium multifermentans
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stimulates
Mn2+
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50% of the stimulation with Ca2+
Na+
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strong activation
Sr2+
Clostridium multifermentans
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stimulates
Sr2+
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50% of the stimulation with Ca2+
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1-ethyl-3-(3-dimethylamino-propyl) carbodiimide
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weak inhibitor
diethylenetriaminepentaacetate
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hydroxyethylenediaminetriacetate
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mixed type inhibition
N-bromosuccinimide
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complete inhibition
trans-1,2-cyclohexanediaminetetraacetate
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Cu2+
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inhibitory
EDTA
Clostridium multifermentans
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Hg2+
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2,2'-dithiodipyridine
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5,5-dithio-bis 2-nitrobenzoic acid
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PelN
presence of PelN has an synergistic effect on PelX activity
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triethylenetetramine
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activates
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0.0032
oligogalacturonate
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0.0013
polygalacturonate I
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0.0016
polygalacturonate II
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0.0054
trigalacturonate
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additional information
additional information
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additional information
additional information
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additional information
additional information
Clostridium multifermentans
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additional information
additional information
Clostridium multifermentans
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Km for polygalacturonate is 0.114% on the basis of dry, ash-free polygalacturonic acid, in presence of 0.5 mM CaCl2
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1.311
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fractionated enzyme in supernatant fluid, no activity in crude cell extract
additional information
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substrate specificity
additional information
Clostridium multifermentans
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additional information
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additional information
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substrate specificity
additional information
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7.4
85% of maximal activity in 0.1 M TES, pH 7.4, 0.1 mM Fe2+
8
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8.5
Clostridium multifermentans
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6 - 8.5
Clostridium multifermentans
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pH 5: no activity, pH 6.0: 15% of maximal activity, pH 7.0: 40% of maximal activity, pH 8.5: maximal activity
7 - 9
Clostridium multifermentans
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pH 7: about 40% of maximal activity, pH 9: about 85% of maximal activity
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brenda
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brenda
Clostridium multifermentans
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brenda
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brenda
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brenda
rumen bacterium, strain ATCC 19207
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brenda
subsp. carotovora
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brenda
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brenda
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brenda
2 different enzyme types: exopolygalacturonate lyase X, i.e. Pel X, and exopectate lyase W, i.e. PelW
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brenda
3937
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brenda
3937
Uniprot
brenda
3937
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brenda
3937
Uniprot
brenda
gene pelW; i.e. Erwinia chrysanthemi, gene pelW
UniProt
brenda
gene pelX; i.e. Erwinia chrysanthemi, gene pelX
UniProt
brenda
i.e. Erwinia chrysanthemi, gene pelW
UniProt
brenda
gene pelW; i.e. Erwinia chrysanthemi, gene pelW
UniProt
brenda
gene pelX; i.e. Erwinia chrysanthemi, gene pelX
UniProt
brenda
i.e. Erwinia chrysanthemi, gene pelW
UniProt
brenda
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Clostridium multifermentans
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brenda
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brenda
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brenda
PelW
brenda
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PelW
brenda
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brenda
PelX
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brenda
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PelX
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brenda
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evolution
PelX belongs to the PL9 family
evolution
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PelX belongs to the PL9 family
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32400
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equilibrium centrifugation
35000
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SDS-PAGE, mass spectrometry
38000
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1 * 38000, SDS-PAGE
76000
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x * 76000, SDS-PAGE
76938
x * 76938, calculation from nucleotide sequence
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?
x * 76938, calculation from nucleotide sequence
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x * 76938, calculation from nucleotide sequence
monomer
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monomer
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1 * 54000, SDS-PAGE
monomer
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1 * 38000, SDS-PAGE
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side-chain modification
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contains about 13% carbohydrate
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3 - 10
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2°C, 72 h, relatively stable
34115
5 - 9
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at 50-55°C
669558
6
Clostridium multifermentans
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38°C, most stable at
34111
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50
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pH 7.0, 10 min, stable below
60
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pH 7.0, 10 min, 85% loss of activity
45
5 min, 50% loss of activity
45
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Mn2+ or Co2+ increases half-life from 4 min to 15 min
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Ca2+ stablizes
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Ca2+ stablizes
Clostridium multifermentans
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Mn2+ stablizes
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Mn2+ stablizes
Clostridium multifermentans
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partial
Clostridium multifermentans
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ultrafiltration and three-step chromatographic procedures, Sephacryl S-100 column, DEAE-Sepharose ion-exchange column, Sephadex G-50 column chromatography
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Clostridium multifermentans
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industry
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degumming and retting of fiber crops and pre-treatment of pectic waste water from fruit juice industries
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Shevchik, V.E.; Condemine, G.; Robert-Baudouy, J.; Hugouvieux-Cotte-Pattat, N.
The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937
J. Bacteriol.
181
3912-3919
1999
Dickeya chrysanthemi, Dickeya chrysanthemi 3937
brenda
Macmillan, J.D.; Phaff, H.J.
Exopolygalacturonate lyase from Clostridium multifermentans. II. Further purification and exopolygalacturonate lyase and pectinesterase from Clostridium multifermentans
Methods Enzymol.
8
632-635
1966
Clostridium multifermentans
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brenda
Miller, L.; Macmillan, J.D.
Mode of action of pectic enzymes. II. Further purification of exopolygalacturonate lyase and pectinesterase from Clostridium multifermentans
J. Bacteriol.
102
72-78
1970
Clostridium multifermentans
brenda
Macmillan, J.D.; Vaughn, R.H.
Purification and properties of a polygalacturonic acid-trans-eliminase produced by Clostridium multifermentans
Biochemistry
3
564-572
1964
Clostridium multifermentans
brenda
Sato, M.; Kaji, A.
Further properties of the new type of exopolygalacturonate lyase from Streptomyces nitrosporeus
Agric. Biol. Chem.
43
1547-1551
1979
Streptomyces nitrosporeus
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brenda
Shevchik, V.; Scott, M.; Mayans, O.; Jenkins, J.
Crystallization and preliminary X-ray analysis of a member of a new family of pectate lyases, PeIL from Erwinia chrysanthemi
Acta Crystallogr. Sect. D
54
419-422
1998
Dickeya chrysanthemi, Dickeya chrysanthemi 3937
brenda
Sato, M.; Kaji, A.
Exopolygalacturonate lyase produced by Streptomyces massasporeus
Agric. Biol. Chem.
44
717-721
1980
Streptomyces massasporeus
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brenda
Hatanaka, C.; Ozawa, J.
Exopectic acid transeliminase of an Erwinia
Agric. Biol. Chem.
36
2307-2313
1972
Erwinia sp., Erwinia sp. W2
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brenda
Hatanaka, C.; Ozawa, J.
Effect of metal ions on activity of exopectic acid transeliminase of Erwinia sp.
Agric. Biol. Chem.
37
593-597
1973
Erwinia sp.
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brenda
Shevchik, V.E.; Kester, H.C.M.; Benen, J.A.E.; Visser, J.; Robert-Baudouy, J.; Hugouvieux-Cotte-Pattat, N.
Characterization of the exopolygalacturonate lyase PelX of Erwinia chrysanthemi 3937
J. Bacteriol.
181
1652-1663
1999
Dickeya chrysanthemi (Q9Z5P8), Dickeya chrysanthemi, Dickeya chrysanthemi 3937 (Q9Z5P8)
brenda
Ikeda, S.; Kegoya, Y.; Hatanaka, C.
Effect of chelating agents on exopolygalacturonate lyase of Erwinia carotovora subsp. carotovora
Agric. Biol. Chem.
48
2777-2782
1984
Pectobacterium carotovorum
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brenda
Kegoya, Y.; Setoguchi, M.; Yokohiki, K.; Hatanaka, C.
Affinity chromatography of exopolygalactururonate lyase from Erwinia carotovora subsp. carotovora
Agric. Biol. Chem.
48
1055-1060
1984
Pectobacterium carotovorum
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brenda
Kester, H.C.M.; Magaud, D.; Roy, C.; Anker, D.; Doutheau, A.; Shevchik, V.; Hugouvieux-Cotte-Pattat, N.; Benen, J.A.E.; Visser, J.
Performance of selected microbial pectinases on synthetic monomethyl-esterified di- and trigalacturonates
J. Biol. Chem.
274
37053-37059
1999
Aspergillus tubingensis, Dickeya chrysanthemi
brenda
Duskova, D.; Marounek, M.
Fermentation of pectin and glucose, and activity of pectin-degrading enzymes in the rumen bacterium Lachnospira multiparus
Lett. Appl. Microbiol.
33
159-163
2001
Lachnospira multipara
brenda
Celestino, S.M.; Maria de Freitas, S.; Javier Medrano, F.; Valle de Sousa, M.; Filho, E.X.
Purification and characterization of a novel pectinase from Acrophialophora nainiana with emphasis on its physicochemical properties
J. Biotechnol.
123
33-42
2006
Acrophialophora nainiana
brenda
Hassan, S.; Shevchik, V.E.; Robert, X.; Hugouvieux-Cotte-Pattat, N.
PelN is a new pectate lyase of Dickeya dadantii with unusual characteristics
J. Bacteriol.
195
2197-2206
2013
Dickeya dadantii (E0SDR9), Dickeya dadantii (Q05526), Dickeya dadantii, Dickeya dadantii 3937 (E0SDR9), Dickeya dadantii 3937 (Q05526)
brenda
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