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Information on EC 3.2.1.55 - non-reducing end alpha-L-arabinofuranosidase and Organism(s) Saccharolobus solfataricus and UniProt Accession P22498

for references in articles please use BRENDA:EC3.2.1.55
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EC Tree
IUBMB Comments
The enzyme acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Some beta-galactosidases (EC 3.2.1.23) and beta-D-fucosidases (EC 3.2.1.38) also hydrolyse alpha-L-arabinosides. cf. EC 3.2.1.185, non-reducing end beta-L-arabinofuranosidase.
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This record set is specific for:
Saccharolobus solfataricus
UNIPROT: P22498
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Word Map
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
arabinofuranosidase, arabinosidase, alpha-l-araf, alpha-arabinosidase, alpha-l-arabinosidase, afase, alpha-l-arabinofuranosidase b, arabinoxylan arabinofuranohydrolase, alpha-araf, alpha-arabinofuranosidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L213A variant beta-glycosidase
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ABF
-
-
-
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alpha-arabinofuranosidase
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-
-
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alpha-arabinosidase
-
-
-
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Alpha-L-AF
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-
-
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alpha-L-arabinanase
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-
-
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alpha-L-arabinofuranoside hydrolase
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-
-
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alpha-L-arabinosidase
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-
-
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arabinosidase
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-
-
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beta-D-xylosidase/alpha-L-arabinosidase
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beta-xylosidase/alpha-arabinosidase
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L-arabinosidase
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-
-
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polysaccharide alpha-L-arabinofuranosidase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-L-arabinofuranoside non-reducing end alpha-L-arabinofuranosidase
The enzyme acts on alpha-L-arabinofuranosides, alpha-L-arabinans containing (1,3)- and/or (1,5)-linkages, arabinoxylans and arabinogalactans. Some beta-galactosidases (EC 3.2.1.23) and beta-D-fucosidases (EC 3.2.1.38) also hydrolyse alpha-L-arabinosides. cf. EC 3.2.1.185, non-reducing end beta-L-arabinofuranosidase.
CAS REGISTRY NUMBER
COMMENTARY hide
9067-74-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ginsenoside C-Mc + H2O
ginsenoside C-K + alpha-L-arabinofuranose
show the reaction diagram
-
-
-
?
ginsenoside Rc + H2O
ginsenoside Rd + alpha-L-arabinofuranose
show the reaction diagram
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + D-glucopyranose
show the reaction diagram
-
1.7% of activity with p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
-
9% of activity with p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
o-nitrophenyl-beta-D-xylopyranoside + H2O
o-nitrophenol + beta-D-xylopyranose
show the reaction diagram
-
3% of activity with p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
p-nitrophenyl-alpha-L-arabinofuranoside + H2O
p-nitrophenol + L-arabinofuranose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-L-arabinopyranoside + H2O
p-nitrophenol + alpha-L-arabinopyranose
show the reaction diagram
-
46% of activity with p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
p-nitrophenyl-beta-D-xylopyranoside + H2O
p-nitrophenol + beta-D-xylopyranose
show the reaction diagram
-
14% of activity with p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
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
additional information
?
-
-
specifically induced by xylan and repressed by monosaccharides like D-glucose and L-arabinose
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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
82000
-
4 * 82000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 82000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
-
half-life: 2 h
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Morana, A.; Paris, O.; Maurelli, L.; Rossi, M.; Cannio, R.
Gene cloning and expression in Escherichia coli of a bi-functional beta-D-xylosidase/alpha-L-arabinosidase from Sulfolobus solfataricus involved in xylan degradation
Extremophiles
11
123-132
2007
Saccharolobus solfataricus, Saccharolobus solfataricus P2
Manually annotated by BRENDA team
Kambourova, M.; Mandeva, R.; Fiume, I.; Maurelli, L.; Rossi, M.; Morana, A.
Hydrolysis of xylan at high temperature by co-action of the xylanase from Anoxybacillus flavithermus BC and the beta-xylosidase/alpha-arabinosidase from Sulfolobus solfataricus Oalpha
J. Appl. Microbiol.
102
1586-1593
2007
Saccharolobus solfataricus, Saccharolobus solfataricus Oalpha
Manually annotated by BRENDA team
Choi, J.H.; Shin, K.C.; Oh, D.K.
An L213A variant of beta-glycosidase from Sulfolobus solfataricus with increased alpha-L-arabinofuranosidase activity converts ginsenoside Rc to compound K
PLoS ONE
13
e0191018
2018
Saccharolobus solfataricus (P22498), Saccharolobus solfataricus DSM 1617 (P22498)
Manually annotated by BRENDA team