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Information on EC 3.2.1.181 - galactan endo-beta-1,3-galactanase
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EC Tree
3.2.1.181 galactan endo-beta-1,3-galactanaseIUBMB Comments
The enzyme from the fungus Flammulina velutipes (winter mushroom) hydrolyses the beta(1->3) bonds found in type II plant arabinogalactans, which occur in cell walls of dicots and cereals. The enzyme is an endohydrolase, and requires at least 3 contiguous beta-1,3-residues. cf. EC 3.2.1.89, arabinogalactan endo-beta-1,4-galactanase and EC 3.2.1.145, galactan 1,3-beta-galactosidase.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
The enzyme specifically hydrolyses beta-1,3-galactan and beta-1,3-galactooligosaccharides
Synonyms
fven3gal, ncen3gal, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
endo-beta-1,3-galactanase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
The enzyme specifically hydrolyses beta-1,3-galactan and beta-1,3-galactooligosaccharides
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-
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The enzyme specifically hydrolyses beta-1,3-galactan and beta-1,3-galactooligosaccharides
beta-1,4- and beta-1,6-galactooligosaccharides, agarose, or keratan sulfate do not serve as substrates
The enzyme specifically hydrolyses beta-1,3-galactan and beta-1,3-galactooligosaccharides
beta-1,4- and beta-1,6-galactooligosaccharides, agarose, or keratan sulfate do not serve as substrates
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SYSTEMATIC NAME
IUBMB Comments
arabinogalactan 3-beta-D-galactanohydrolase
The enzyme from the fungus Flammulina velutipes (winter mushroom) hydrolyses the beta(1->3) bonds found in type II plant arabinogalactans, which occur in cell walls of dicots and cereals. The enzyme is an endohydrolase, and requires at least 3 contiguous beta-1,3-residues. cf. EC 3.2.1.89, arabinogalactan endo-beta-1,4-galactanase and EC 3.2.1.145, galactan 1,3-beta-galactosidase.
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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
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + H2O
3-O-beta-D-galactopyranosyl-beta-D-galactopyranose + D-galactose
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + H2O
3-O-beta-D-galactopyranosyl-beta-D-galactopyranose + D-galactose
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + H2O
3-O-beta-D-galactopyranosyl-beta-D-galactopyranose + D-galactose
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + H2O
3-O-beta-D-galactopyranosyl-beta-D-galactopyranose + beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + D-galactopyranose
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after 30 min of reaction time the enzyme produces 42% D-glalactose, 30% dimeric, 20% trimeric and less than 10% tetrameric or pentameric beta-1,3-galactooligosaccharides
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?
arabinogalactan + H2O
?
-
the enzyme specifically acts on beta-1,3-galactan within the plant proteoglycansin arabinogalactan-proteins (AGPs) in an endo-manner. The carbohydrate moieties of AGPs consist of beta-1,3-galactan main chains and beta-1,6-galactan side chains, to which other auxiliary sugars are attached. Enzyme Af3G hardly hydrolyze native arabinogalactan-proteins (AGPs) alone but acts synergistically with a fungal exo-beta-1,3-galactanase on the AGP
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-
?
arabinogalactan + H2O
?
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the enzyme specifically acts on beta-1,3-galactan within the plant proteoglycansin arabinogalactan-proteins (AGPs) in an endo-manner. The carbohydrate moieties of AGPs consist of beta-1,3-galactan main chains and beta-1,6-galactan side chains, to which other auxiliary sugars are attached. Enzyme NcEn3GAL hardly hydrolyze native arabinogalactan-proteins (AGPs) alone but acts synergistically with a fungal exo-beta-1,3-galactanase on the AGP. Very low activity on native gum arabic and the larch arabinogalactan
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-
?
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose
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best substrate
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-
?
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose
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best substrate
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-
?
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose
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-
-
?
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose
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best substrate
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-
?
beta-1,3-galactotetraose + H2O
2 beta-1,3-galactobiose
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the enzyme seems to prefer hydrolyzing the central beta-1,3-glycosidic linkage of three in beta-1,3-galactotetraose
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-
?
beta-1,3-galactotetraose + H2O
2 beta-1,3-galactobiose
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the enzyme seems to prefer hydrolyzing the central beta-1,3-glycosidic linkage of three in beta-1,3-galactotetraose
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-
?
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + H2O
3-O-beta-D-galactopyranosyl-beta-D-galactopyranose + D-galactose
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-
-
?
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + H2O
3-O-beta-D-galactopyranosyl-beta-D-galactopyranose + D-galactose
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-
-
?
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + H2O
3-O-beta-D-galactopyranosyl-beta-D-galactopyranose + D-galactose
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-
-
?
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + H2O
3-O-beta-D-galactopyranosyl-beta-D-galactopyranose + D-galactose
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-
-
?
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + H2O
3-O-beta-D-galactopyranosyl-beta-D-galactopyranose + D-galactose
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-
-
?
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + H2O
3-O-beta-D-galactopyranosyl-beta-D-galactopyranose + D-galactose
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?
additional information
?
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very low activity on native gum arabic and the larch arabinogalactan. Substrate specificity, overview
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?
additional information
?
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The enzyme does not hydrolyze beta1,3:1,4-glucan, beta-1,3:1,6-glucan, beta-1,3-glucan, xyloglucan, keratan sulfste, kappa-carrageenan, agaraose, 4-nitrophenyl beta-D-galactoside, 4-nitrophenyl beta-D-glucoside, 4-nitrophenyl beta-D-glucuronide, 4-nitrophenyl beta-D-xyloside. It is inactive towards beta-1,4-galactan. It does not hydrolyze 3-O-beta-D-galactopyranosyl-beta-D-galactopyranose. The enzyme requires at least 3 contiguous beta-1,3-residues. The enzyme shows a weak transglycosylation activity.
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-
?
additional information
?
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The enzyme does not hydrolyze beta1,3:1,4-glucan, beta-1,3:1,6-glucan, beta-1,3-glucan, xyloglucan, keratan sulfste, kappa-carrageenan, agaraose, 4-nitrophenyl beta-D-galactoside, 4-nitrophenyl beta-D-glucoside, 4-nitrophenyl beta-D-glucuronide, 4-nitrophenyl beta-D-xyloside. It is inactive towards beta-1,4-galactan. It does not hydrolyze 3-O-beta-D-galactopyranosyl-beta-D-galactopyranose. The enzyme requires at least 3 contiguous beta-1,3-residues. The enzyme shows a weak transglycosylation activity.
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?
additional information
?
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substrate specificity, overview. Gum arabic from acacia tree is a poor substrate
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?
additional information
?
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The enzyme does not hydrolyze beta1,3:1,4-glucan, beta-1,3:1,6-glucan, beta-1,3-glucan, xyloglucan, keratan sulfste, kappa-carrageenan, agaraose, 4-nitrophenyl beta-D-galactoside, 4-nitrophenyl beta-D-glucoside, 4-nitrophenyl beta-D-glucuronide, 4-nitrophenyl beta-D-xyloside. It is inactive towards beta-1,4-galactan. It does not hydrolyze 3-O-beta-D-galactopyranosyl-beta-D-galactopyranose. The enzyme requires at least 3 contiguous beta-1,3-residues. The enzyme shows a weak transglycosylation activity.
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?
additional information
?
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very low activity on native gum arabic and the larch arabinogalactan. Substrate specificity, overview
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?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.25
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose
pH 5.0, 37°C
0.57
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose
pH 5.0, 37°C
additional information
beta-1,3-galactan
the value for beta-1,3-galactan is 0.137 mg/ml
additional information
beta-1,3-galactan
-
the value for beta-1,3-galactan is 0.137 mg/ml
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.47
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose
pH 5.0, 37°C
6.5
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose
pH 5.0, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.38
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose
pH 5.0, 37°C
1.14
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose
pH 5.0, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7
3 - 7
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over 50% of maximal activity within this range, inactive above pH 8.0, profile overview, recombinant enzyme
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
10 - 60
-
40% of maximal activity at 50°C and 50% at 10°C, profile overview, recombinant enzyme
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
evolution
-
the enzyme belongs to the glycosyl hydrolase family 16, GH16
physiological function
-
the endo-beta-1,3-galactanases presumably aid hydrolysis of arabinogalactan-proteins (AGPs) by internally breaking up AGPs, which creates more sites of attack for exo-beta-1,3-galactanase
physiological function
-
the endo-beta-1,3-galactanases presumably aid hydrolysis of arabinogalactan-proteins (AGPs) by internally breaking up AGPs, which creates more sites of attack for exo-beta-1,3-galactanase
physiological function
-
the endo-beta-1,3-galactanases presumably aid hydrolysis of arabinogalactan-proteins (AGPs) by internally breaking up AGPs, which creates more sites of attack for exo-beta-1,3-galactanase
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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). E3GAL_FLAVE
249
0
26690
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A084FVS5_PSEDA
239
0
26844
TrEMBL
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 1.2fold from Pichia pastoris by cation exchange chromatography and gel filtration
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recombinant enzyme 1.6fold from Pichia pastoris by cation exchange chromatography and gel filtration
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recombinant enzyme 1.7fold from Pichia pastoris by cation exchange chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Pichia pastoris
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Pichia pastoris
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DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Pichia pastoris
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DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression in Pichia pastoris
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kotake, T.; Hirata, N.; Degi, Y.; Ishiguro, M.; Kitazawa, K.; Takata, R.; Ichinose, H.; Kaneko, S.; Igarashi, K.; Samejima, M.; Tsumuraya, Y.
Endo-beta-1,3-galactanase from winter mushroom Flammulina velutipes
J. Biol. Chem.
286
27848-27854
2011
Flammulina velutipes (F7J1C8), Flammulina velutipes, Flammulina velutipes NBRC 7663 (F7J1C8)
brenda
Yoshimi, Y.; Yaguchi, K.; Kaneko, S.; Tsumuraya, Y.; Kotake, T.
Properties of two fungal endo-beta-1,3-galactanases and their synergistic action with an exo-beta-1,3-galactanase in degrading arabinogalactan-proteins
Carbohydr. Res.
453-454
26-35
2017
Aspergillus flavus, Flammulina velutipes, Neurospora crassa
brenda
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Release 2023.1 (January 2023)
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