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Information on EC 3.2.1.15 - endo-polygalacturonase

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EC Tree
IUBMB Comments
The enzyme catalyses the random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans. Different forms of the enzyme have different tolerances to methyl esterification of the substrate.
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UNIPROT: B9JUR9
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
pg ii, endopolygalacturonase, endo-polygalacturonase, endopg, endo-pg, endopolygalacturonases, exo-pg, pgase, exo-polygalacturonase, endopg i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-galacturonase
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-
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endo-D-galacturonanase
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endo-D-galacturonase
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endo-polygalacturonase
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endogalacturonase
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endopectinase
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endopolygalacturonase
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endopolygalacturonate lyase
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EPG
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-
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liquifying polygalacturonase
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-
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P1/P3
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-
-
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P2C
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-
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pectic depolymerase
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-
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pectic hydrolase
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pectin depolymerase
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pectin hydrolase
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pectin polygalacturonase
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-
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pectinase
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pectinase SS
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-
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pectolase
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-
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pectozyme
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PG-2A
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-
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PGA
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-
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PGase SM
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-
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PGC
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PGL
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phylendonase
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poly-alpha-1,4-galacturonide glycanohydrolase
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remanase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
(1->4)-alpha-D-galacturonan glycanohydrolase (endo-cleaving)
The enzyme catalyses the random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans. Different forms of the enzyme have different tolerances to methyl esterification of the substrate.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-75-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
B9JUR9_AGRVS
Agrobacterium vitis (strain S4 / ATCC BAA-846)
544
0
57223
TrEMBL
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by hanging-drop vapour-diffusion method. Crystals belong to space group P21, with unit-cell parameters a=52.387, b=62.738, c=149.165 A, beta=89.98, to 1.59 A resolution, crystals contain two molecules per asymmetric unit, a right-handed parallel beta-helix fold
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity by a two-step chromatography procedure
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the expression vector pBAD24 and transformed into Escherichia coli strain TOP10
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vordtriede, P.B.; Yoder, M.D.
Crystallization, X-ray diffraction analysis and preliminary structure determination of the polygalacturonase PehA from Agrobacterium vitis
Acta Crystallogr. Sect. F
64
645-647
2008
Agrobacterium vitis (B9JUR9)
Manually annotated by BRENDA team