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Information on EC 3.2.1.15 - endo-polygalacturonase and Organism(s) Aspergillus niger and UniProt Accession P26213

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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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Aspergillus niger
UNIPROT: P26213
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The taxonomic range for the selected organisms is: Aspergillus niger
The enzyme appears in selected viruses and cellular organisms
Synonyms
pg ii, endopolygalacturonase, endo-polygalacturonase, endo-pg, endopg, endopolygalacturonases, exo-pg, pgase, exo-polygalacturonase, endopg i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endopolygalacturonase
-
poly [1, 4-alpha-D-galacturonide] glycano-hydrolase
-
D-galacturonase
-
-
-
-
endo-D-galacturonanase
-
-
-
-
endo-D-galacturonase
-
-
-
-
endo-polygalacturonase
endo-polygalacturonase A
-
-
endo-polygalacturonase C
-
-
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
-
-
-
-
PGase SM
-
-
-
-
PGL
-
-
-
-
phylendonase
-
-
-
-
poly [1, 4-alpha-D-galacturonide] glycano-hydrolase
-
poly-alpha-1,4-galacturonide glycanohydrolase
-
-
-
-
polygalacturonase inhibiting protein 1
-
-
remanase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
9032-75-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pectin + H2O
?
show the reaction diagram
endopolygalacturonases hydrolyse the 1-4 linkages between two alpha-D-galacturonic acids of the smooth homogalacturonan regions of pectin. Isozyme PGI is not only the most potent but also the most tolerant enzyme to hydrolyse acetylated pectin
-
-
?
polygalacturonate + H2O
oligogalacturonates
show the reaction diagram
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
D-galacturonic acid
show the reaction diagram
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
digalacturonic acid + galacturonate
show the reaction diagram
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + D-galacturonate
show the reaction diagram
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
show the reaction diagram
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
show the reaction diagram
-
-
-
-
?
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate + H2O
?
show the reaction diagram
-
-
-
-
?
amylopectin + H2O
?
show the reaction diagram
-
-
-
-
?
dextrose agar + H2O
?
show the reaction diagram
-
potato dextrose agar, low activity
-
-
?
galacturonosyl-galactonic acid + H2O
?
show the reaction diagram
-
-
-
-
?
homogalacturonan + H2O
oligogalacturonide
show the reaction diagram
-
-
-
-
?
methyl digalacturonoside + H2O
?
show the reaction diagram
-
-
-
-
?
pectic acid + H2O
galacturonic acid oligomers
show the reaction diagram
-
-
-
-
?
pectin + H2O
?
show the reaction diagram
pectin + H2O
galacturonic acid + digalacturonic acid + trigalacturonic acid
show the reaction diagram
-
-
-
?
pectin + H2O
galacturonic acid oligomers
show the reaction diagram
-
-
-
-
?
polygalacturonate + H2O
oligogalacturonates
show the reaction diagram
polygalacturonic acid + H2O
?
show the reaction diagram
-
-
-
-
?
polygalacturonic acid + H2O
galacturonic acid
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
polygalacturonate + H2O
oligogalacturonates
show the reaction diagram
-
-
-
?
pectin + H2O
?
show the reaction diagram
-
citrus or apple pectin
-
-
?
polygalacturonate + H2O
oligogalacturonates
show the reaction diagram
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the hydrolytic cleavage of the polygalacturonic acid chain
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
about 125% activity at 1 mM
Fe2+
about 115% activity at 1 mM
K+
about 115% activity at 1 mM
Li+
about 110% activity at 1 mM
Na+
about 120% activity at 1 mM
Zn2+
about 115% activity at 1 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
-
-
auxin
-
either in tobacco PG or wild-type plants treated with oligogalacturonides, resistance to fungal infection is suppressed by exogenous auxin, whereas sensitivity to auxin of PG plants is reduced in different bioassays. Altered auxin sensitivity in PG plants may be due to an increased accumulation of oligogalacturonides and subsequent antagonism of auxin action
Ba2+
about 92% residual activity at 1 mM
chlorogenic acid
-
-
Cinnamic acid
-
-
Co2+
about 75% residual activity at 1 mM
diethyl dicarbonate
-
at pH 6, only enzyme form E2 is protected from inhibition by 2% w/v polygalacturonate
ferulic acid
-
-
L-cystine
-
-
Mercuric chloride
-
-
Ni2+
about 82% residual activity at 1 mM
p-coumaric acid
-
-
Pb2+
about 38% residual activity at 1 mM
polygalacturonase-inhibiting protein
-
polygalacturonase-inhibiting protein 1 of Chorispora bungeana
-
-
-
protein PPGIP2
-
polygalacturonase-inhibiting protein 2 from Phaseolus vulgaris, is an efficient inhibitor of fungal polygalacturonases. Overall sequence conservation of PGIP2 and minor variation at specific sites is necessary for high-affinity recognition of different fungal polygalacturonases
-
salicylic acid
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
apple or peach lipid transfer proteins significantly increase PG activity (more than 2fold) and heat stability
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.67 - 12.5
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
1.82 - 3.31
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
0.89 - 1.85
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
0.7
alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonosyl-(1,4)-O-alpha-D-galacturonate
-
-
0.0196
pectate
-
-
0.155
Pectin
-
pH 4.5, 50°C
0.34
polygalacturonic acid
-
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
246
-
partially purified enzyme, pH 4.5, 40°C
43.9
-
enzyme form E2
54.3
-
determined as micromol/ml/mg protein, purified enzyme, pH 4.8, 45°C, substrate polygalacturonic acid
80.8
-
enzyme form E1
83.06
-
partially purified enzyme, pH 4.5, 50°C
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.4 - 5.2
more than 30% of maximal activity from pH 2.4 to 5.2
3 - 6
more than 60% activity between pH 3.0 and 6.0
3.5 - 6
-
pH 3.5: about 30% of maximal activity, pH 6.0: about 30% of maximal activity
3.5 - 6.5
-
over 50% of maximal acitivity at pH 3.5-6.0, 32% at pH 6.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
-
activity range, profile, overview. 55% of maximal activity at 20°C, 70% at 70°C
30 - 60
more than 60% activity between 30 and 60°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
solid-state fermentation in double-surface bioreactor, fermentation method optimization, overview
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PGLR1_ASPNG
368
0
38108
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
106000
-
native PAGE
34000
-
1 * 34000 + 1 * 69000, SDS-PAGE
35000
-
x * 35000, SDS-PAGE
36000
-
MALDI-TOF MS, PGA lacking N-glycan modification
36200
-
MALDI-TOF MS, deglycosylated PGA
37000
-
x * 37000, SDS-PAGE
37230
-
MALDI-TOF MS, recombinant PGA
39600
-
MALDI-TOF MS
46000
-
gel filtration
50788
x * 50788, calculation from nucleotide sequence
69000
-
1 * 34000 + 1 * 69000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
-
1 * 34000 + 1 * 69000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
at least two polypeptide chains with different glycosylation patterns. The component with the higher electrophoretic mobility is a high mannose or hybrid-type glycoprotein. The other component may contain O-glycosidically linked mannose, N-acetylglucosamine or glucose
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D180E
-
0.01% of wild type activity, Km-values change minimally
D180N
-
0.08% of wild type activity, Km-values change minimally
D201E
-
0.01% of wild type activity, Km-values change minimally
D201N
D202E
-
0.6% of wild type activity, Km-values change minimally
D202N
-
0.01% of wild type activity, Km-values change minimally
H223A
-
enzyme has only 0.5% of wild type activity, no effect of Km-value
K258N
-
0.8% of wild type activity, 10fold decrease in Km-values
N178D
-
has an activity approximately 20fold lower than the native Aspergillus niger PGII
R256N
-
14% of wild type activity, 10fold decrease in Km-values
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.8
-
2 h, about 60% loss of activity
135824
3 - 6
the enzyme shows good stability within the pH range of 3.0-6.0 for different incubation times and over 65% of activity is retained
751303
3.5
-
2 h, about 25% loss of activity
135824
4 - 5.5
-
purified enzyme, 1 h, stable at
730876
5
-
2 h, stable
135824
6
-
2 h, about 10% loss of activity
135824
7
-
2 h, about 40% loss of activity
135824
8
-
2 h, about 70% loss of activity
135824
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
-
stable up to, 90-100% activity remaining after 120 min
25
-
purified enzyme, half-life is 3 h
35 - 70
the enzyme retains more than 50% of its activity after incubation at 35-70°C for 60 min, but no activity remains after incubation at 70°C for 2 h
4
-
purified enzyme, half-life is 104 h
50
-
50% activity remaining after 120 min
60 - 70
-
inactivation within 12 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
operational stability of a membrane reactor with pectinases
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography using polygalacturonic acid as ligand. Good results with silanized porous glass or keratin coated silica gel supports
-
ammonium sulfate precipitation and ENrich SEC 650 gel filtration
by thiol chromatography
-
native enzyme 6.5fold by ethanol precipitation and gel filtration to homogeneity
-
native enzyme 9fold by ultrafiltration, ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
-
native enzyme partially 7fold by gel filtration
-
to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain EBY100
generation of transgenic Arabidopsis thaliana Ws and Nicotiana tabacum Petit Havana-SR1 plants expressing PG with the point mutation N178D. Arabidopsis line PG201 expressing PGII with the point mutation D201N
-
highly conserved region in the C-terminal region of the enzyme probably comprising the elements of substrate binding and the catalytic centre
-
homologously overexpressed
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
PG plants exhibit enhanced resistance to the necrotrophic fungal pathogen Botrytis cinerea and to the virulent bacterial pathogen Pseudomonas syringae and have constitutively activated defense responses by releasing oligogalacturonides
food industry
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lobarzewski, J.; Fiedurek, J.; Ginalska, G.; Wolski, T.
New matrices for the purification of pectinases by affinity chromatography
Biochem. Biophys. Res. Commun.
131
666-674
1985
Aspergillus niger
Manually annotated by BRENDA team
Schejter, A.; Marcus, L.
Isozymes of pectinesterase and polygalacturonase from Botrytis cinerea Pers.
Methods Enzymol.
161
366-373
1988
Aspergillus japonicus, Aspergillus niger, Botrytis cinerea, Burkholderia cepacia, Pectobacterium carotovorum, Fusarium oxysporum, Solanum lycopersicum, Rhizoctonia fragariae, Rhizopus arrhizus, Saccharomyces fragilis, Trichoderma koningii, Verticillium albo-atrum, Botrytis cinerea Pers.
-
Manually annotated by BRENDA team
Cervone, F.; de Lorenzo, G.; Degra, L.; Salvi, G.; Bergami, M.
Purification and characterization of a polygalacturonase-inhibiting protein from Phaseolus vulgaris L.
Plant Physiol.
85
631-637
1987
Aspergillus niger, Colletotrichum lindemuthianum, Fusarium verticillioides
Manually annotated by BRENDA team
Heinrichova, K.; Dzurova, M.
Purification, characterization and mode of effect of another endo-D-galacturonase from Aspergillus niger
Collect. Czech. Chem. Commun.
46
3145-3156
1981
Aspergillus niger
-
Manually annotated by BRENDA team
Heinrichova, K.; Rexova-Benkova, L.
Purification and characterization of another D-galacturonase from Aspergillus niger
Collect. Czech. Chem. Commun.
42
2569-2576
1977
Aspergillus niger
-
Manually annotated by BRENDA team
Cooke, R.D.; Ferber, C.E.M.; Kanagasabapathy, L.
Purification and characterisation of polygalacturonases from a commercial Aspergillus niger preparation
Biochim. Biophys. Acta
452
440-451
1976
Aspergillus niger
Manually annotated by BRENDA team
Deuel, H.; Stutz, E.
Pectic substances and pectic enzymes
Adv. Enzymol. Relat. Subj. Biochem.
20
341-382
1958
Aspergillus aureus, Aspergillus foetidus, Aspergillus niger, Bacillus pumilus, Bacterium aroideae, Botrytis cinerea, Paecilomyces fulvus, Ophiostoma ulmi, Clostridium felsineum, Fusarium verticillioides, Solanum lycopersicum, Neurospora crassa, Penicillium expansum, Rhizopus arrhizus, Saccharomyces fragilis, Verticillium dahliae
Manually annotated by BRENDA team
Van Santen, Y.; Benen, J.A.E.; Schroer, K.H.; Kalk, K.H.; Armand, S.; Visser, J.; Dijkstra, B.W.
1.68-A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis
J. Biol. Chem.
274
30474-30480
1999
Aspergillus niger
Manually annotated by BRENDA team
Parenicova, L.; Kester, H.C.M.; Benen, J.A.E.; Visser, J.
Characterization of a novel endopolygalacturonase from Aspergillus niger with unique kinetic properties
FEBS Lett.
467
333-336
2000
Aspergillus niger (Q9P4W2), Aspergillus niger
Manually annotated by BRENDA team
Leech, A.; Mattei, B.; Federici, L.; de Lorenzo, G.; Hemmings, A.M.
Preliminary X-ray crystallographic analysis of a plant defence protein, the polygalacturonase-inhibiting protein from Phaseolus vulgaris
Acta Crystallogr. Sect. D
56
98-100
2000
Aspergillus niger
Manually annotated by BRENDA team
Raab, B.
Characterization of endopolygalacturonase (EC 3.2.1.15) from Aspergillus niger as glycoprotein by electrophoretic methods and lectin affino-blotting
Electrophoresis
13
807-808
1992
Aspergillus niger
Manually annotated by BRENDA team
Ruttkowski, E.; Khanh, N.Q.; Wientjes, F.J.; Gottschalk, M.
Characterization of a polygalacturonase gene of Aspergillus niger RH5344
Mol. Microbiol.
5
1353-1361
1991
Aspergillus niger, Aspergillus niger RH5344
Manually annotated by BRENDA team
Rodriguez-Nogales, J.N.; Ortega, N.; perez-mateos, M.; Busto, M.D.
Operational stability and kinetic study of a membrane reactor with pectinases from Aspergillus niger
J. Food Sci.
70
E104-E108
2005
Aspergillus niger
-
Manually annotated by BRENDA team
Oelofse, D.; Dubery, I.A.; Meyer, R.; et.al.
Apple polygalacturonase inhibiting protein 1 expressed in transgenic tobacco inhibits polygalacturonases from fungal pathogens of apple and the anthracnose pathogen of lupins
Phytochemistry
67
255-263
2006
Aspergillus niger, Diaporthe ambigua, Diplodia seriata, Colletotrichum lupini
Manually annotated by BRENDA team
Woosley, B.; Xie, M.; Wells, L.; Orlando, R.; Garrison, D.; King, D.; Bergmann, C.
Comprehensive glycan analysis of recombinant Aspergillus niger endo-polygalacturonase C
Anal. Biochem.
354
43-53
2006
Aspergillus niger
Manually annotated by BRENDA team
Woosley, B.D.; Kim, Y.H.; Kumar Kolli, V.S.; Wells, L.; King, D.; Poe, R.; Orlando, R.; Bergmann, C.
Glycan analysis of recombinant Aspergillus niger endo-polygalacturonase A
Carbohydr. Res.
341
2370-2378
2006
Aspergillus niger
Manually annotated by BRENDA team
Tomassen, M.M.; Barrett, D.M.; van der Valk, H.C.; Woltering, E.J.
Isolation and characterization of a tomato non-specific lipid transfer protein involved in polygalacturonase-mediated pectin degradation
J. Exp. Bot.
58
1151-1160
2007
Aspergillus niger, Solanum lycopersicum
Manually annotated by BRENDA team
Ferrari, S.; Galletti, R.; Pontiggia, D.; Manfredini, C.; Lionetti, V.; Bellincampi, D.; Cervone, F.; De Lorenzo, G.
Transgenic expression of a fungal endo-polygalacturonase increases plant resistance to pathogens and reduces auxin sensitivity
Plant Physiol.
146
669-681
2008
Aspergillus niger
Manually annotated by BRENDA team
Andre-Leroux, G.; Tessier, D.; Bonnin, E.
Endopolygalacturonases reveal molecular features for processivity pattern and tolerance towards acetylated pectin
Biochim. Biophys. Acta
1794
5-13
2009
Aspergillus niger (P26213), Aspergillus niger (P26214), Aspergillus niger, Fusarium fujikuroi (Q07181)
Manually annotated by BRENDA team
Farina, A.; Rocchi, V.; Janni, M.; Benedettelli, S.; De Lorenzo, G.; DOvidio, R.
The bean polygalacturonase-inhibiting protein 2 (PvPGIP2) is highly conserved in common bean (Phaseolus vulgaris L.) germplasm and related species
Theor. Appl. Genet.
118
1371-1379
2009
Aspergillus niger, Botrytis cinerea, Colletotrichum lupini, Fusarium phyllophilum, Botrytis cinerea B05-10
Manually annotated by BRENDA team
Di, C.; Li, M.; Long, F.; Bai, M.; Liu, Y.; Zheng, X.; Xu, S.; Xiang, Y.; Sun, Z.; An, L.
Molecular cloning, functional analysis and localization of a novel gene encoding polygalacturonase-inhibiting protein in Chorispora bungeana
Planta
231
169-178
2009
Aspergillus niger
Manually annotated by BRENDA team
Buga, M.; Ibrahim, S.; Nok, A.
Physico-chemical characteristics of immobilized polygalacturonase from Aspergillus niger (SA6)
Afr. J. Biotechnol.
9
8934-8943
2010
Aspergillus niger, Aspergillus niger SA6
-
Manually annotated by BRENDA team
Buga, M.; Ibrahim, S.; Nok, A.
Partially purified polygalacturonase from Aspergillus niger (SA6)
Afr. J. Biotechnol.
9
8944-8954
2010
Aspergillus niger, Aspergillus niger SA6
-
Manually annotated by BRENDA team
Hendges, D.; Montanari, Q.; Malvessi, E.; Silveira, M.
Production and characterization of endo-polygalacturonase from Aspergillus niger in solid-state fermentation in double-surface bioreactor
Braz. Arch. Biol. Technol.
54
253-258
2011
Aspergillus niger, Aspergillus niger T0005/007-2
-
Manually annotated by BRENDA team
Dushyantha, D.; Jagadeesh, K.; Krishnaraj, P.; Patil, C.
Purification and kinetic studies of polygalacturonase from Aspergillus niger RBF96
J. Pure Appl. Microbiol.
8
2389-2394
2014
Aspergillus niger, Aspergillus niger RBF96
-
Manually annotated by BRENDA team
Kant, S.; Vohra, A.; Gupta, R.
Purification and physicochemical properties of polygalacturonase from Aspergillus niger MTCC 3323
Protein Expr. Purif.
87
11-16
2013
Aspergillus niger, Aspergillus niger MTCC 3323
Manually annotated by BRENDA team
Zhou, H.; Li, X.; Guo, M.; Xu, Q.; Cao, Y.; Qiao, D.; Cao, Y.; Xu, H.
Secretory expression and characterization of an acidic endo-polygalacturonase gene from Aspergillus niger SC323 in Saccharomyces cerevisiae
J. Microbiol. Biotechnol.
25
999-1006
2015
Aspergillus niger (A0A0B4UL66), Aspergillus niger, Aspergillus niger SC323 (A0A0B4UL66)
Manually annotated by BRENDA team