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Information on EC 3.2.1.89 - arabinogalactan endo-beta-1,4-galactanase and Organism(s) Bacillus licheniformis and UniProt Accession Q65CX5

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IUBMB Comments
This enzyme, isolated from the bacterium Bacillus subtilis, hydrolyses the beta(1->4) bonds found in type I plant arabinogalactans, which are a component of the primary cell walls of dicots. The predominant product is a tetrasaccharide. cf. EC 3.2.1.181, galactan endo-beta-1,3-galactanase.
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Bacillus licheniformis
UNIPROT: Q65CX5
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The taxonomic range for the selected organisms is: Bacillus licheniformis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
galactanase, beta-1,4-galactanase, blgal, pcgal1, endo-1,4-beta-galactanase, arabinogalactanase, endo-beta-1,4-d-galactanase, arabinogalactan 4-beta-d-galactanohydrolase, endogalactanase a, gh53 endo-beta-1,4-galactanase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endo-beta-1,4-galactanase
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arabinogalactanase
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-
-
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beta-1,4-galactanase
-
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endo-1,4-beta-galactanase
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-
-
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galactanase
-
-
-
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GH53 endo-beta-1,4-galactanase
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-
additional information
the enzyme belongs to the glycoside hydrolase family 53, GH-53
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The enzyme specifically hydrolyses (1->4)-beta-D-galactosidic linkages in type I arabinogalactans.
show the reaction diagram
active site and substrate binding structures, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
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SYSTEMATIC NAME
IUBMB Comments
arabinogalactan 4-beta-D-galactanohydrolase
This enzyme, isolated from the bacterium Bacillus subtilis, hydrolyses the beta(1->4) bonds found in type I plant arabinogalactans, which are a component of the primary cell walls of dicots. The predominant product is a tetrasaccharide. cf. EC 3.2.1.181, galactan endo-beta-1,3-galactanase.
CAS REGISTRY NUMBER
COMMENTARY hide
58182-40-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-1,4-galactan + H2O
galactobiose + galactotriose
show the reaction diagram
AZCL-galactan + H2O
?
show the reaction diagram
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the enzyme shows a conserved beta-turn, characteristic of GH53 enzymes, which contributes to subsites -2 to +3
-
-
?
citrus fruit pectin + H2O
?
show the reaction diagram
-
-
-
-
?
potato galactan + H2O
galactotetraose
show the reaction diagram
-
-
-
-
?
sugarcane bagasse + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
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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
beta-1,4-galactan + H2O
galactobiose + galactotriose
show the reaction diagram
plant-cell-wall-degrading enzyme involved in the hydrolysis of beta-1,4-galactan in the hairy regions of pectin
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
about 110% activity at 5 mM
Co2+
-
about 130% activity at 5 mM
K+
-
about 128% activity at 5 mM
Li+
-
about 118% activity at 5 mM
Mg2+
-
about 103% activity at 5 mM
Mn2+
-
about 115% activity at 5 mM
Na+
-
about 138% activity at 5 mM
Ni2+
-
about 145% activity at 5 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
-
about 5% residual activity at 5 mM
EDTA
-
about 60% residual activity at 5 mM
EGTA
-
about 80% residual activity at 5 mM
Fe3+
-
about 2% residual activity at 5 mM
Zn2+
-
about 5% residual activity at 5 mM
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
555.8
potato galactan
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at pH 6.0 and 40°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
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the enzyme shows maximum activity (more than 90 %) in the pH range over 6.5 to 8.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
the enzyme retains 75% activity at pH values 6.0 and 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 45
-
about 20% activity at 20°C, about 50% activity at 30°C, 100% activity at 40°C, about 70% activity at 45°C, no activity at 50°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
-
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
-
x * 44000, SDS-PAGE of mutant E263A
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme free or in complex with products galactobiose and galactotriose, hanging drop vapour diffusion method, 0.002-0.004 ml of protein solution, containing 20-40 mg/ml protein, are mixed with 0.002 ml reservoir solution containing 21-26% w/v PEG 1500, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement modelling
wild-type and mutant E263A in complex with methyl-beta(1-4)-galactotetraoside, grown at room temperature in hanging drops with a resolution range of 30-2.3 A. Crystals of wild-type and mutant E263A both belong to the monoclinic space group P21, containing two molecules in the asymmetric unit
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E263A
-
inactive nucleophile mutant
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
the enzyme retains more than 75 % activity after 24 h at pH 4.0-10.0
749617
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 45
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the enzyme retains nearly 100% activity after 1 h at pH 7.0 at 25-45°C, The melting temperature is 52.9°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Bacillus subtilis by adsorption chromatography
Ni2+-chelating affinity column chromatography and Superdex G200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Bacillus subtilis
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ryttersgaard, C.; Le Nours, J.; Lo Leggio, L.; Jorgensen, C.T.; Christensen, L.L.; Bjornvad, M.; Larsen, S.
The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products
J. Mol. Biol.
341
107-117
2004
Bacillus licheniformis (Q65CX5), Bacillus licheniformis
Manually annotated by BRENDA team
Le Nours, J.; De Maria, L.; Welner, D.; Jorgensen, C.T.; Christensen, L.L.; Borchert, T.V.; Larsen, S.; Lo Leggio, L.
Investigating the binding of beta-1,4-galactan to Bacillus licheniformis beta-1,4-galactanase by crystallography and computational modeling
Proteins
75
977-989
2009
Bacillus licheniformis
Manually annotated by BRENDA team
de Lima, E.A.; Machado, C.B.; Zanphorlin, L.M.; Ward, R.J.; Sato, H.H.; Ruller, R.
GH53 endo-beta-1,4-galactanase from a newly isolated Bacillus licheniformis CBMAI 1609 as an enzymatic cocktail supplement for biomass saccharification
Appl. Biochem. Biotechnol.
179
415-426
2016
Bacillus licheniformis, Bacillus licheniformis CBMAI 1609
Manually annotated by BRENDA team