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Information on EC 3.2.1.89 - arabinogalactan endo-beta-1,4-galactanase and Organism(s) Thermotoga maritima and UniProt Accession Q9X0S8

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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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This record set is specific for:
Thermotoga maritima
UNIPROT: Q9X0S8
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The taxonomic range for the selected organisms is: Thermotoga maritima
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
galactanase, beta-1,4-galactanase, blgal, endo-1,4-beta-galactanase, pcgal1, arabinogalactanase, endo-beta-1,4-d-galactanase, endo-beta-1,4-galactanase, arabinogalactan 4-beta-d-galactanohydrolase, endogalactanase a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endo-beta-1,4-D-galactanase
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arabinogalactanase
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-
-
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endo-1,4-beta-galactanase
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-
-
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galactanase
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-
-
-
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
galactan + H2O
?
show the reaction diagram
initially, rather long oligosaccharides are detected as hydrolysis products of potato galactan. Then, as the reaction proceeds, mainly galactotetraose is produced. After 24 h reaction, D-galactose, beta-1,4-D-galactobiose, beta-1,4-D-galactotriose and beta-1,4-D-galactotetraose are detected as the major products from potato galactan. The enzyme hydrolyzes galactans more efficiently than pectic galactans
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
pH 5.0: about 60% of maximal activity, pH 8.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70 - 100
70°C: about 50% of maximal activity, 100°C: about 95% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64000
x * 64000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 64000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
60°C, 60 min, about 60% of maximal activity
678791
3
60°C, 60 min, about 75% loss of activity
678791
4 - 9
60°C, 60 min, less than 20% los of activity in the pH-range 4-9
678791
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
pH 7.0, 60 min, no loss of activity
85
pH 7.0, 60 min, about 30% loss of activity
90
pH 7.0, 60 min, about 95% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, H.; Ichinose, H.; Yoshida, M.; Nakajima, M.; Kobayashi, H.; Kaneko, S.
Characterization of a thermostable endo-beta-1,4-D-galactanase from the hyperthermophile Thermotoga maritima
Biosci. Biotechnol. Biochem.
70
538-541
2006
Thermotoga maritima (Q9X0S8), Thermotoga maritima
Manually annotated by BRENDA team