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Information on EC 3.2.1.181 - galactan endo-beta-1,3-galactanase and Organism(s) Flammulina velutipes and UniProt Accession F7J1C8

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EC Tree
IUBMB 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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This record set is specific for:
Flammulina velutipes
UNIPROT: F7J1C8
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The taxonomic range for the selected organisms is: Flammulina velutipes
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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The enzyme specifically hydrolyses beta-1,3-galactan and beta-1,3-galactooligosaccharides
Synonyms
fven3gal, ncen3gal, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endo-beta-1,3-galactanase
-
endo-beta-1,3-galactanase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The enzyme specifically hydrolyses beta-1,3-galactan and beta-1,3-galactooligosaccharides
show the reaction diagram
beta-1,4- and beta-1,6-galactooligosaccharides, agarose, or keratan sulfate do not serve as substrates
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose
show the reaction diagram
-
-
-
?
beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranosyl-(1->3)-beta-D-galactopyranose + H2O
3-O-beta-D-galactopyranosyl-beta-D-galactopyranose + D-galactose
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
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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
-
?
arabinogalactan + H2O
?
show the reaction diagram
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from radish leaves
-
-
?
beta-1,3-galactan + H2O
oligo-beta-(1->3)-D-galactose
show the reaction diagram
-
best substrate
-
-
?
beta-1,3-galactotetraose + H2O
2 beta-1,3-galactobiose
show the reaction diagram
-
-
-
-
?
beta-1,4-galactan + H2O
?
show the reaction diagram
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from lupin
-
-
?
gum arabic beta-1,3-galactan I + H2O
?
show the reaction diagram
-
-
-
-
?
gum arabic beta-1,3-galactan II + H2O
?
show the reaction diagram
-
-
-
-
?
larch arabinogalactan + H2O
?
show the reaction diagram
-
-
-
-
?
larch beta-galactan I + H2O
?
show the reaction diagram
-
-
-
-
?
larch beta-galactan II + H2O
?
show the reaction diagram
-
-
-
-
?
larch beta-galactan III + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12.8
pH 5.0, 37°C, liberation of D-galactose
17
-
purified recombinant enzyme, pH 5.0, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
recombinant enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
winter mushroom
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the enzyme belongs to the glycosyl hydrolase family 16, GH16
physiological function
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
E3GAL_FLAVE
249
0
26690
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26690
calculated from amino acid sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E138D
no activity
E143D
no activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 1.6fold from Pichia pastoris by cation exchange chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed 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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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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team