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Information on EC 3.2.1.15 - endo-polygalacturonase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P47180
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3.2.1.15 endo-polygalacturonaseIUBMB 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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Word Map
- 3.2.1.15
- aspergillus
- pepsinogen
- polygalacturonic
- niger
-
galacturonic
- tomato
- pylori
-
ripening
- citrus
- helicobacter
- gastritis
- fusarium
-
polygalacturonase-inhibiting
-
pgips
-
methylesterase
- pectinases
- botrytis
- homogalacturonan
- cinerea
- alternaria
- peach
-
macer
- sclerotiorum
- rhamnogalacturonans
-
softening
- exopolygalacturonase
-
sclerotinia
-
ripe
- moniliforme
-
pectolytic
- oligogalacturonates
- carotovora
- marxianus
-
methylesterified
- food industry
-
wall-degrading
-
pylori-positive
- purpureum
- lindemuthianum
-
methylesterification
- stereum
- cochliobolus
- pectinesterase
- polyuronides
-
de-esterification
-
pectin-degrading
- agriculture
-
lycopersici
- nutrition
- medicine
- industry
- analysis
- degradation
- paper production
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pg ii, endopolygalacturonase, endo-polygalacturonase, endo-pg, endopg, endopolygalacturonases, exo-pg, pgase, exo-polygalacturonase, endopg i, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-galacturonase
-
-
-
-
endo-D-galacturonanase
-
-
-
-
endo-D-galacturonase
-
-
-
-
endo-polygalacturonase
-
-
-
-
endogalacturonase
-
-
-
-
endopectinase
-
-
-
-
endopolygalacturonase
endopolygalacturonate lyase
-
-
-
-
EPG
-
-
-
-
liquifying polygalacturonase
-
-
-
-
P1/P3
-
-
-
-
P2C
-
-
-
-
pectic depolymerase
-
-
-
-
pectic hydrolase
-
-
-
-
pectin depolymerase
-
-
-
-
pectin hydrolase
-
-
-
-
pectin polygalacturonase
-
-
-
-
pectinase
-
-
-
-
pectinase SS
-
-
-
-
pectolase
-
-
-
-
pectozyme
-
-
-
-
PG-2A
-
-
-
-
PGA
-
-
-
-
PGase SM
-
-
-
-
PGC
-
-
-
-
PGL
-
-
-
-
phylendonase
-
-
-
-
poly-alpha-1,4-galacturonide glycanohydrolase
-
-
-
-
remanase
-
-
-
-
endopolygalacturonase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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
9032-75-1
-
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
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
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
3.5 - 4.5
79% of maximal activity at pH 3.5, maximal activity at pH 4.5
4 - 7
-
pH 4.0: about 35% of maximal activity, pH 7.0: about 80% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
30% of maximal activity at 25°C, maximal activity at 45°C
20 - 60
-
20°C: about 40% of maximal activity, 60°C: about 25% of maximal activity
30 - 55
-
30°C: about 55% of maximal activity, 55°C: about 60% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
comparison of endo-polygalacturonase from Saccharomyces cerevisiae with the enzyme from Saccharomyces paradoxus after overexpression in Saccharomyces cerevisiae under wine production conditions, overview. The higher activity of Saccharomyces paradoxus strains under laboratory conditions might be due to a different regulation mechanism rather than to a different sequence of gene PGU1. ScPgu1 displayed higher Km and Vmax than SpPgu1 thereby showing a slightly lower affinity for the substrate but a twofold stronger activity under optimal conditions
additional information
-
comparison of endo-polygalacturonase from Saccharomyces cerevisiae with the enzyme from Saccharomyces paradoxus after overexpression in Saccharomyces cerevisiae under wine production conditions, overview. The higher activity of Saccharomyces paradoxus strains under laboratory conditions might be due to a different regulation mechanism rather than to a different sequence of gene PGU1. ScPgu1 displayed higher Km and Vmax than SpPgu1 thereby showing a slightly lower affinity for the substrate but a twofold stronger activity under optimal conditions
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
two potential glycosylation points at residues 318 and 330
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Saccharomyces cerevisiae strain VIN13, which is itself completely devoid of endo-polygalacturonase activity, and secretion to the medium
expressed in Saccharomyces cerevisiae strains UCLMS-1, -3 and -4, while strains Collection Cepage Cabernet and L2226 do not show any transcription of the gene after integration
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the activation of transcription of endopolygalacturonase encoded by the PGU1 gene by galactose is strain specific independent of the strain being an industrial or a domesticated one
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirose, N.; Kishida, M.; Kawasaki, H.; Sakai, T.
Purification and characterization of an endo-polygalacturonase from a mutant of Saccharomyces cerevisiae
Biosci. Biotechnol. Biochem.
63
1100-1103
1999
Saccharomyces cerevisiae, Kluyveromyces marxianus, Saccharomyces cerevisiae SSM52
Gainvors, A.; Nedjaoum, N.; Gognies, S.; Muzart, M.; Nedjma, M.; Belarbi, A.
Purification and characterization of acidic endo-polygalacturonase encoded by the PGL1-1 gene from Saccharomyces cerevisiae
FEMS Microbiol. Lett.
183
131-135
2000
Saccharomyces cerevisiae
Blanco, P.; Sieiro, N.M.; Reboredo, N.M.; Villa, T.G.
Cloning, molecular characterization, and expression of an endo-polygalacturonase-encoding gene from Saccharomyces cerevisiae IM1-8b
FEMS Microbiol. Lett.
164
249-255
1998
Saccharomyces cerevisiae, Saccharomyces cerevisiae IM1-8b
Blanco, P.; Sieiro, C.; Diaz, A.; Villa, T.G.
Production and partial characterization of an endopolygalacturonase from Saccharomyces cerevisiae
Can. J. Microbiol.
40
974-977
1994
Saccharomyces cerevisiae, Saccharomyces cerevisiae CECT1389
Louw, C.; Young, P.R.; van Rensburg, P.; Divol, B.
Regulation of endo-polygalacturonase activity in Saccharomyces cerevisiae
FEMS Yeast Res.
10
44-57
2010
Saccharomyces cerevisiae
van Wyk, H.; Divol, B.
Recovery of endo-polygalacturonase activity in wine yeast and its effect on wine aroma
FEMS Yeast Res.
10
58-71
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae L2323
Eschstruth, A.; Divol, B.
Comparative characterization of endo-polygalacturonase (Pgu1) from Saccharomyces cerevisiae and Saccharomyces paradoxus under winemaking conditions
Appl. Microbiol. Biotechnol.
91
623-634
2011
Saccharomyces paradoxus (F5B9B9), Saccharomyces paradoxus, Saccharomyces cerevisiae (P47180), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742 (P47180), Saccharomyces paradoxus RO88 (F5B9B9)
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