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Information on EC 3.2.1.164 - galactan endo-1,6-beta-galactosidase
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EC Tree
3.2.1.164 galactan endo-1,6-beta-galactosidaseSpecify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Endohydrolysis of (1->6)-beta-D-galactosidic linkages in arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield galactose and (1->6)-beta-galactobiose as the final products
Synonyms
endo-beta-1,6-galactanase, type ii arabinogalactan-degrading enzyme, beta-1,6-galactanase, beta-(1,6)-galactanase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-1,6-galactanase
endo-beta-(1-6)-galactanase
GAL1
type II arabinogalactan-degrading enzyme
additional information
additional information
-
the enzyme belongs to the glycoside hydrolase family 5
additional information
-
the enzyme belongs to the glycoside hydrolase family 5
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->6)-beta-D-galactosidic linkages in arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield galactose and (1->6)-beta-galactobiose as the final products
Endohydrolysis of (1->6)-beta-D-galactosidic linkages in arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield galactose and (1->6)-beta-galactobiose as the final products
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-
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Endohydrolysis of (1->6)-beta-D-galactosidic linkages in arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield galactose and (1->6)-beta-galactobiose as the final products
mode of action, overview
-
Endohydrolysis of (1->6)-beta-D-galactosidic linkages in arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield galactose and (1->6)-beta-galactobiose as the final products
mode of action, overview
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CAS REGISTRY NUMBER
COMMENTARY
136111-49-4
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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
arabinogalactan-protein + H2O
beta-GlcA-(1->6)-Gal + 4-methyl-beta-GlcA-(1->6)-Gal
the enzyme prefers alpha-L arabinofuranosidase-treated arabinogalactan-proteins from radish roots (151% activity) and radish leaves (87% activity) compared to native ones from radish roots (36% activity) and leaves (28% activity)
-
-
?
beta-(1->6)-galactotriose + H2O
beta-(1->6)-galactobiose + galactose
-
-
-
?
beta-galactan + H2O
?
-
galactan from Prototheca zopfii, which has a high proportion of beta-1,6-linked galactosyl residues, the extent of hydrolysis of the carbohydrate portion of a radish root arabinogalactan-protein AGP increases when alpha-L-arabinofuranosyl residues attached to beta-1,6-linked galactosyl side chains of the AGP are removed in advance, the enzyme releases galactose, beta-1,6-galactobiose, and 4-O-methyl-beta-glucuronosyl-1,6-galactose as major hydrolysis products when allowed to act exhaustively on the modified AGP, overview
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-
?
desarabinosylated grape 3,6-galactan-protein + H2O
?
-
the enzyme liberates beta-1,6-D-galactobiose and galactose
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-
?
arabinogalactan + H2O
oligo-beta-(1->6)-galactans + beta-(1->6)-D-galactobiose
-
-
-
?
arabinogalactan + H2O
oligo-beta-(1->6)-galactans + beta-(1->6)-D-galactobiose
plant type II arabinogalactans consisting of beta-(1,3)- and beta-(1,6)-galactan side chains connected to each other by (1,3)(1,6)-linked branch points. The O-3 and O-6 positions are substituted with terminal arabinosyl residues
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-
?
type II arabinogalactans + H2O
?
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the enzyme preferentially debranches beta-1,6-galactobiose from the substrate, type II arabinogalactans from Western larch
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-
?
type II arabinogalactans + H2O
?
-
the enzyme preferentially debranches beta-1,6-galactobiose from the substrate, type II arabinogalactans from Western larch
-
-
?
additional information
?
-
-
activity with galactans from different sources, overview
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-
?
additional information
?
-
-
the beta-1,6-galactanase liberates galactose and 1,6-galactobiose from acid-treated larchwood and Norway spruce arabinogalactans
-
-
?
additional information
?
-
-
the enzyme does not cleave beta-D-1,3-galactosidic bonds
-
-
?
additional information
?
-
the enzyme fails to act on gum arabic, beta-(1->6)-galactobiose beza-(1->4)-galactan from lupin, beta-(1->3)(1->4)-glucan from barley, beta-(1->3)(1->6)-glucan from Laminaria digitata, beta-(1->6)-glucan from Umbilicaria papullosa, carboxymethyl-curdlan (beta-(1->3)-glucan), carboxymethyl-cellulose (beta-(1->4)-glucan), galactomannan from guar, galactomannan from locust bean, beta-(1->4)-xylan from birchwood, arabino-beta-(1->4)-xylan from wheat flour, arabinan (alpha-(1->3)(1->5)-arabinan), and debranched arabinan (alpha-(1->5)-arabinan)
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-
?
additional information
?
-
-
substrate preparations and specificity, the endo-galactanase hydrolyzes specifically beta-1,6-galactooligosaccharides with a degree of polymerization higher than 3 and their acidic derivatives with 4-O-methyl-glucosyluronic or glucosyluronic groups at the nonreducing terminals, oveview
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-
?
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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
arabinogalactan + H2O
oligo-beta-(1->6)-galactans + beta-(1->6)-D-galactobiose
-
-
-
?
additional information
?
-
-
activity with galactans from different sources, overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme activity does not require metal ions and is not affected by the presence of Ba2+, Ca2+, Co2+, Fe3+, K+, Mg2+, Mn2+, Na+, or Ni2+, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.017
using Reactive Black 5-de-arabinosylated gum arabic as substrate
192
culture medium, using beta-(1->3)(1->6)-galactan as substrate, at pH 5.0 and 37°C
292
after fold purification, using beta-(1->3)(1->6)-galactan as substrate, at pH 5.0 and 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Glomerella lindemuthiana, pathogenic race 1472 and non-pathogenic race 0
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
growth of both races with glucose show basal transcription levels of enzyme. When glucose is replaced with arabinogalactan, xylan or plant cell walls, gene ebg transcription markedly increases in pathogenic race 1472 but not in non-pathogenic race 0
brenda
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commercial cellulase preparation Onozuka R-10
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme contains an N-terminal secretion signal
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glycosylhydrolase family 30, GH30
physiological function
endo-breta-(1,6)-D-galactanase is a debranching hemicellulase that catalyzes the hydrolysis of beta-(1,6)-galactosyl side chains in arabinogalactans (AGs), producing beta-(1,6)-galacto-oligomers and beta-(1,6)-D-galactobiose. The enzyme plays a critical role in cell wall degradation. Arabinogalactan proteins (AGPs) are putative co-receptors in signaling pathways that function during growth and plant developmen. AGPs also play a key role in both beneficial and pathogenic root-microorganism interactions. They are essential for root cells to recognize beneficial microorganisms as well for root cells to trigger localized and efficient defense responses to control pathogenic organisms. Since the carbohydrate groups in AGPs are critical for their function, it is conceivable to hypothesize that the pathogenic race of Colletotrichum lindemuthianum, which more rapidly expresses gene ebg at higher levels in the presence of plant cell wall polysaccharides, is better adapted to degrade AGPs for the establishment of the infection as the non-pathogenic race
additional information
putative DNA-binding sites for Cre, Xlnr, ACEI, PacC and Gal4 transcriptional factors are predicted in ebg genes from Colletotrichum species. Identification of potential functional and structural domains, protein structure homology modelling and structure comaprisons. In enzyme EBG, the catalytic proton donor E191 is positioned in a coil and the catalytic nucleophile E293 is positioned in a beta-strand
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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). 6GAL_HYPRU
479
0
52762
Swiss-Prot
Secretory Pathway (Reliability: 3)
A0A8J8W495_9EURO
487
0
53253
TrEMBL
Secretory Pathway (Reliability: 2)
K4R0H9_STRDJ
Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768)
490
0
53324
TrEMBL
-
A0A086YZJ7_9BIFI
1518
2
163589
TrEMBL
-
A0A1R3STW0_9BACT
527
0
59265
TrEMBL
-
A0A0F8AZ05_CERFI
484
0
52735
TrEMBL
Secretory Pathway (Reliability: 1)
A0A852ZYK0_9ACTN
488
0
53269
TrEMBL
-
Q7S2S4_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
488
0
53756
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17000
47000
50488
x * 50488, sequence calculation, x * 64000, recombinant enzyme, SDS-PAGE, x * 50687, detagged recombinant enzyme, mass spectrometry, x * 68296, recombinant His6-tagged thioredoxin fusion enzyme, sequence calculation
50687
x * 50488, sequence calculation, x * 64000, recombinant enzyme, SDS-PAGE, x * 50687, detagged recombinant enzyme, mass spectrometry, x * 68296, recombinant His6-tagged thioredoxin fusion enzyme, sequence calculation
64000
x * 50488, sequence calculation, x * 64000, recombinant enzyme, SDS-PAGE, x * 50687, detagged recombinant enzyme, mass spectrometry, x * 68296, recombinant His6-tagged thioredoxin fusion enzyme, sequence calculation
68296
x * 50488, sequence calculation, x * 64000, recombinant enzyme, SDS-PAGE, x * 50687, detagged recombinant enzyme, mass spectrometry, x * 68296, recombinant His6-tagged thioredoxin fusion enzyme, sequence calculation
17000
-
gel filtration, the enzyme shows unusual behaviour in gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
?
x * 50488, sequence calculation, x * 64000, recombinant enzyme, SDS-PAGE, x * 50687, detagged recombinant enzyme, mass spectrometry, x * 68296, recombinant His6-tagged thioredoxin fusion enzyme, sequence calculation
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the enzyme contains 3 putative N-glycosylation sites at Asp45, Asp233, and Asp416
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
-
4 h, purified enzyme, 1 M acetate buffer, pH 4.2, 50% remaining activity
60
60
-
4 h, purified enzyme, 1 M acetate buffer, pH 4.2, 17% remaining activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CM-32 column chromatography, DEAE-Sepharose column chromatography and Sephadex G-100 gel filtration
native enzyme 26.2fold to homogeneity by several chromatographic steps, overview
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native enzyme form a commercial cellulase preparation, 57fold to homogeneity by ammonium sulfate fractionation, two steps of ion exchange chromatography, and gel filtration
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native enzyme from commercial pectinase preparation by anion and cation exchange chromatography, ultrafiltration, and gel filtration
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recombinant His6-tagged enzyme from Escherichia coli strain Bl21 by two steps of metal chelating chromatography, the thioredoxin tag is cleaved off
recombinant maltose-binding-protein fusion enzyme from Escherichia coli strain DH5alpha, by cation exchange and amylose affinity chromatography, followed by hydrophobic interaction chromatography, native enzyme 88fold from strain S12 culture filtrate by anion exchange and hydrophobic interaction chromatography, followed by cation exchange chromatography, dialysis and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and maino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain BL21 as His6-tagged enzyme fused to thioredoxin
gene ebg, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of enzyme EBG from races 0 and 1472 in Escherichia coli TOP10
gene Fogal1, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha as maltose-binding-protein fusion enzyme
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
growth of both races with glucose show basal transcription levels of ebg. When glucose is replaced with arabinogalactan, xylan or plant cell walls, gene ebg transcription markedly increased in pathogenic race 1472 but not in non-pathogenic race 0
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Luonteri, E.; Laine, C.; Uusitalo, S.; Teleman, A.; Siika-aho, M.; Tenkanen, M.
Purification and characterization of Aspergillus beta-D-galactanases acting on beta-1,4- and beta-1,3/6-linked arabinogalactans
Carbohydr. Polym.
53
155-168
2003
Aspergillus niger
-
brenda
Brillouet, J.M.; Williams, P.; Moutounet, M.
Purification and some properties of a novel endo-beta-(1-6)-D-galactanase from Aspergillus niger
Agric. Biol. Chem.
55
1565-1571
1991
Aspergillus niger
-
brenda
Sakamoto, T.; Taniguchi, Y.; Suzuki, S.; Ihara, H.; Kawasaki, H.
Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan
Appl. Environ. Microbiol.
73
3109-3112
2007
Fusarium oxysporum, Fusarium oxysporum 12S
brenda
Kotake, T.; Kaneko, S.; Kubomoto, A.; Haque, M.A.; Kobayashi, H.; Tsumuraya, Y.
Molecular cloning and expression in Escherichia coli of a Trichoderma viride endo-beta-(1-6)-galactanase gene
Biochem. J.
377
749-755
2004
Trichoderma viride (Q76FP5)
brenda
Okemoto, K.; Uekita, T.; Tsumuraya, Y.; Hashimoto, Y.; Kasama, T.
Purification and characterization of an endo-beta-(1-6)-galactanase from Trichoderma viride
Carbohydr. Res.
338
219-230
2003
Trichoderma viride
brenda
Ling, N.; Pettolino, F.; Liao, M.; Bacic, A.
Preparation of a new chromogenic substrate to assay for beta-galactanases that hydrolyse type II arabino-3,6-galactans
Carbohydr. Res.
344
1941-1946
2009
Trichoderma viride (Q76FP5)
brenda
Takata, R.; Tokita, K.; Mori, S.; Shimoda, R.; Harada, N.; Ichinose, H.; Kaneko, S.; Igarashi, K.; Samejima, M.; Tsumuraya, Y.; Kotake, T.
Degradation of carbohydrate moieties of arabinogalactan-proteins by glycoside hydrolases from Neurospora crassa
Carbohydr. Res.
345
2516-2522
2010
Neurospora crassa (Q7S2S4)
brenda
Villa-Rivera, M.; Zavala-Paramo, M.; Conejo-Saucedo, U.; Lopez-Romero, E.; Lara-Marquez, A.; Cano-Camacho, H.
Differences in the expression profile of endo-beta-(1,6)-D-galactanase in pathogenic and non-pathogenic races of Colletotrichum lindemuthianum grown in the presence of arabinogalactan, xylan or Phaseolus vulgaris cell walls
Physiol.Mol. Plant Pathol.
99
75-86
2017
Colletotrichum lindemuthianum (A0A1L2S4I5)
-
brenda
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