Information on EC 3.2.1.164 - galactan endo-1,6-beta-galactosidase

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The expected taxonomic range for this enzyme is: leotiomyceta

EC NUMBER
COMMENTARY
3.2.1.164
-
RECOMMENDED NAME
GeneOntology No.
galactan endo-1,6-beta-galactosidase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
show the reaction diagram
-
-
-
-
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
show the reaction diagram
mode of action, overview
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6GAL
Q7S2S4
-
beta-(1,6)-galactanase
Q76FP5
-
beta-1,6-galactanase
-
-
beta-1,6-galactanase
Fusarium oxysporum 12S
-
-
-
beta-D-galactanase
-
-
endo-beta-(1-6)-D-galactanase
-
-
endo-beta-(1-6)-galactanase
-
-
endo-beta-(1-6)-galactanase
Q76FP5
-
endo-beta-(1->6)-D-galactanase
Q76FP5
-
endo-beta-(1->6)-galactanase
Q7S2S4
-
endo-beta-1,6-D-galactanase
-
-
Tv6GAL
Q76FP5
-
type II arabinogalactan-degrading enzyme
-
-
type II arabinogalactan-degrading enzyme
Fusarium oxysporum 12S
-
-
-
GAL1
Fusarium oxysporum 12S
-
-
-
additional information
-
the enzyme belongs to the glycoside hydrolase family 5
additional information
Fusarium oxysporum 12S
-
the enzyme belongs to the glycoside hydrolase family 5
-
CAS REGISTRY NUMBER
COMMENTARY
136111-49-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain 12S, gene Fogal1
-
-
Manually annotated by BRENDA team
Fusarium oxysporum 12S
strain 12S, gene Fogal1
-
-
Manually annotated by BRENDA team
IFO 31 137
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
arabinogalactan-protein + H2O
beta-GlcA-(1->6)-Gal + 4-methyl-beta-GlcA-(1->6)-Gal
show the reaction diagram
Q7S2S4
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->3)(1->6)-galactan + H2O
?
show the reaction diagram
Q7S2S4
100% activity
-
-
?
beta-(1->6)-galactotriose + H2O
beta-(1->6)-galactobiose + galactose
show the reaction diagram
Q7S2S4
-
-
-
?
beta-galactan + H2O
?
show the reaction diagram
-
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
-
-
?
Reactive Black 5-dyed desarabinosylated gum arabic + H2O
?
show the reaction diagram
Q76FP5
-
-
-
?
type II arabinogalactans + H2O
?
show the reaction diagram
Fusarium oxysporum, Fusarium oxysporum 12S
-
the enzyme preferentially debranches beta-1,6-galactobiose from the substrate, type II arabinogalactans from Western larch
-
-
?
desarabinosylated grape 3,6-galactan-protein + H2O
?
show the reaction diagram
-
the enzyme liberates beta-1,6-D-galactobiose and galactose
-
-
?
additional information
?
-
Q76FP5
substrate specificity, overview
-
-
-
additional information
?
-
-
activity with galactans from different sources, overview
-
-
-
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
-
-
-
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
?
-
Q7S2S4
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)
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
activity with galactans from different sources, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
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
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ag+
-
1 mM, 50% inhibition
Cd2+
-
1 mM, 45% inhibition
Cu2+
-
1 mM, 45% inhibition
Fe2+
-
1 mM, 65% inhibition
-
Zn2+
-
1 mM, 60% inhibition
Hg2+
-
1 mM, 80% inhibition
additional information
-
no inhibition by EDTA
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.017
-
Q76FP5
using Reactive Black 5-de-arabinosylated gum arabic as substrate
1.55
-
-
purified native enzyme
25.29
-
-
purified enzyme
192
-
Q7S2S4
culture medium, using beta-(1->3)(1->6)-galactan as substrate, at pH 5.0 and 37°C
292
-
Q7S2S4
after fold purification, using beta-(1->3)(1->6)-galactan as substrate, at pH 5.0 and 37°C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.3
-
-
-
5.5
-
Q7S2S4
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
7.5
-
activity range, 85% of maximal activity at pH 2.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
50
-
Q7S2S4
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
75
-
activity range
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
commercial pectinase preparation
Manually annotated by BRENDA team
-
commercial cellulase preparation Onozuka R-10
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17000
-
-
gel filtration, the enzyme shows unusual behaviour in gel filtration
17000
-
-
gel filtration
29000
-
-
gel filtration
47000
-
-
native PAGE
60000
-
-
native PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 47000, SDS-PAGE
?
Q76FP5
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
?
Q7S2S4
x * 51264, calculated from amino acid sequence; x * 54000, SDS-PAGE
?
Fusarium oxysporum 12S
-
x * 47000, SDS-PAGE
-
monomer
-
1 * 58000, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
7.5
-
2 h, 40°C, 50% remaining activity at pH 2.0 and at pH 7.5
4
10
-
16 h, purified native enzyme, over 80% remaining activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
4 h, purified enzyme, 1 M acetate buffer, pH 4.2, completely stable
45
-
-
4 h, purified enzyme, 1 M acetate buffer, pH 4.2, 50% remaining activity
60
-
-
4 h, purified enzyme, 1 M acetate buffer, pH 4.2, 17% remaining activity
60
-
-
1 h, purified native enzyme, over 80% remaining activity
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme 26.2fold to homogeneity by several chromatographic steps, overview
-
native enzyme from commercial pectinase preparation by anion and cation exchange chromatography, ultrafiltration, and gel filtration
-
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
-
native enzyme form a commercial cellulase preparation, 57fold to homogeneity by ammonium sulfate fractionation, two steps of ion exchange chromatography, and gel filtration
-
recombinant His6-tagged enzyme from Escherichia coli strain Bl21 by two steps of metal chelating chromatography, the thioredoxin tag is cleaved off
Q76FP5
CM-32 column chromatography, DEAE-Sepharose column chromatography and Sephadex G-100 gel filtration
Q7S2S4
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene Fogal1, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha as maltose-binding-protein fusion enzyme
-
DNA and maino acid sequence determination and analysis, sequence comparison, expression in Escherichia coli strain BL21 as His6-tagged enzyme fused to thioredoxin
Q76FP5
expressed in Pichia pastoris
Q7S2S4