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Information on EC 3.2.1.99 - arabinan endo-1,5-alpha-L-arabinanase
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EC Tree
3.2.1.99 arabinan endo-1,5-alpha-L-arabinanaseIUBMB Comments
Acts best on linear 1,5-alpha-L-arabinan. Also acts on branched arabinan, but more slowly.
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Word Map
- 3.2.1.99
- arabinofuranosidase
- alpha-l-arabinofuranosidase
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debranched
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arabinases
- arabinotriose
- arabino-oligosaccharides
- nutrition
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magnetospheric
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endo-galactanase
- l-arabitol
- analysis
- rhamnogalacturonans
- lipoarabinomannans
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arabinose-containing
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exo-acting
- thermodenitrificans
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five-bladed
- p-nitrophenyl-alpha-l-arabinofuranoside
- cellvibrio
- biofuel production
- degradation
- synthesis
- industry
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
endo-arabinanase, endoarabinanase, arase, endo-arabinase, abn-ts, abns1, abnase, endo-1,5-alpha-l-arabinanase, arb43a, cedaase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ABN
Abn1
Abn2
ABNA
abnA1
abnA2
ABNase
Abnc
AbnS1
AbnZ1
alpha-1,5-L-endo-arabinanase
alpha-L-arabinohydrolase
ARA1
araban 5-alpha-L-arabinohydrolase
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arabinase, endo-1,5-alpha-L-
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BlAbn1
cold-adapted endo-arabinanase
endo-(1,5)-alpha-L-arabinanase
endo-(1->5)-alpha-L-arabinanase
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endo-1,5-alpha-arabinanase
endo-1,5-alpha-L-arabinanase
endo-1,5-alpha-L-arabinase
endo-1,5-arabinase
endo-alpha-(1->5)-L-arabinanase
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endo-alpha-1,5-arabanase
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endo-alpha-1,5-L-arabinanase
endo-arabanase
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endo-arabinanase
endo-arabinase
endo-L-arabinanase
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endoarabinanase
endoarabinase
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GH43 arabinanase
GH43 endo-arabinanase
Tpet_0637
additional information
endo-1,5-alpha-arabinanase
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endo-1,5-alpha-L-arabinanase
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endo-1,5-alpha-L-arabinase
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endo-arabinanase
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endo-arabinase
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additional information
the enzyme belongs to the glycoside hydrolase family 43, GH43
additional information
the enzyme belongs to the glycoside hydrolase family 43, GH43
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additional information
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the enzyme belongs to the glycoside hydrolase family 43, GH43
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O = alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O = alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
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alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O = alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
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alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O = alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
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alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O = alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
also acts slowly on beet-arabinan
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alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O = alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
three catalytic carboxylates: Asp27, the general base, Glu201, the general acid, and Asp147, the pKa modulator, substrate binding structure and catalytic mechanism, overview
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O = alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
Aspergillus niger N400 / DSM 2466 / ATCC 9029 / CBS 120.49
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alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O = alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
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alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O = alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
three catalytic carboxylates: Asp27, the general base, Glu201, the general acid, and Asp147, the pKa modulator, substrate binding structure and catalytic mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
5-alpha-L-arabinan 5-alpha-L-arabinanohydrolase
Acts best on linear 1,5-alpha-L-arabinan. Also acts on branched arabinan, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
75432-96-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1->5)-L-alphaarabinan + H2O
(1->5)-L-arabinooligosaccharides
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
1,5-alpha-L-arabinan + H2O
L-arabinose + alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
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?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
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?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
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?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranose
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?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
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?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
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DP6
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, product formation, end-products after exhaustive enzymatic degradation, intermediate enzymatic hydrolysis: L-arabinobiose + L-arabinotetraose and L-arabinotriose
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
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DP7
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, product formation, end-products after exhaustive enzymatic degradation, intermediate enzymatic hydrolysis: L-arabinotriose + L-arabinotetraose
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranose
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?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
branched arabinan + H2O
?
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branched arabinan from sugar beet. Hydrolyzed at 12% compared to debranched arabinan
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?
cell wall polysaccharide + H2O
arabinose + galactose + rhamnose + fucose
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F-11, apple
F-11, 34.3% arabinose + 10% galactose + 2.6% rhamnose/fucose
?
debranched (1->5)-L-arabinan + H2O
L-arabinose
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under the optimum conditions, 16 g/l L-arabinose is obtained from 20 g/l debranched arabinan with a hydrolysis yield of 80%
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?
debranched (1->5)-L-arabinan + H2O
L-arabinose + L-arabinosyl-alpha-(1->5)-L-arabinoside + ?
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debranched arabinan + H2O
arabinose + arabinobiose + arabinotriose
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?
reduced arabinohexaose + H2O
arabinotriose + reduced arabinotriose
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the enzyme hydrolyzes a branched arabinohexaose with a double substituted arabinose at subsite-2
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?
sugar beet arabinan + H2O
L-arabinose + L-arabinosyl-alpha-(1->5)-L-arabinoside
48% of the activity with debranched (1->5)-L-arabinan
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?
sugar beet arabinan arabinan + H2O
L-arabinose + ?
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conversion yield of 83% at pH 5.0 and 75°C for 216 h
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?
1,5-alpha-L-arabinan + H2O
?
Abn2, together with previously characterized AbnA, is responsible for the majority of the extracellular arabinan activity in Bacillus subtilis. Abn2 is monocistronic, and its expression is driven from two different promoters
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?
1,5-alpha-L-arabinan + H2O
?
Abn2, together with previously characterized AbnA, is responsible for the majority of the extracellular arabinan activity in Bacillus subtilis. Abn2 is monocistronic, and its expression is driven from two different promoters
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?
1,5-alpha-L-arabinan + H2O
?
debranched arabinan, best substrate
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?
1,5-alpha-L-arabinan + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + ?
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linear arabinan
main product
?
1,5-alpha-L-arabinan + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + ?
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linear arabinan
main product
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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major final end-products, upon exhaustive degradation of substrate some monomers, L-arabinose, are produced, action patterns of initial hydrolysis products
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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best substrate, endo mechanism
action patterns of initial hydrolysis products, product formation, overview
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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product formation, overview: oligoarabinosides with degree of polymerization between 2 and 5 are the major products, but only trace amounts of free arabinose
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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major final end-products, upon exhaustive degradation of substrate some monomers, L-arabinose, are produced, action patterns of initial hydrolysis products
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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best substrate, endo mechanism
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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best substrate, endo mechanism
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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best substrate, endo mechanism
major final end-products, upon exhaustive degradation of substrate some monomers, L-arabinose, are produced
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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best substrate, endo mechanism
action patterns of initial hydrolysis products, product formation, overview
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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best substrate: linear 1,5-alpha-L-haze arabinan
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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i.e. debranched arabinan
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
AB063312
i.e. debranched arabinan
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
AB063312
i.e. debranched arabinan
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
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F-11 and IFO 3022: best substrate, endo mechanism
end-product
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
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F-11 best substrate
end-product, F-11: releases arabinose, arabinobiose, arabinotriose and higher oligosaccharides during hydrolysis, end-product are arabinose and arabinobiose
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
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IFO 3134, linear 1,5-alpha-L-arabinan
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
Bacillus subtilis F-11
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?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
Bacillus subtilis F-11
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F-11 and IFO 3022: best substrate, endo mechanism
end-product
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
Bacillus subtilis F-11
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F-11 best substrate
end-product, F-11: releases arabinose, arabinobiose, arabinotriose and higher oligosaccharides during hydrolysis, end-product are arabinose and arabinobiose
?
1,5-alpha-L-arabinan + H2O
L-arabinose + alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
-
F-11 and IFO 3022: best substrate, endo mechanism
-
-
?
1,5-alpha-L-arabinan + H2O
L-arabinose + alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
-
F-11 best substrate
-
-
?
1,5-alpha-L-arabinan + H2O
L-arabinose + alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
-
IFO 3022, best substrate
IFO 3022
?
1,5-alpha-L-arabinan + H2O
L-arabinose + alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
Bacillus subtilis F-11
-
F-11 and IFO 3022: best substrate, endo mechanism
-
-
?
1,5-alpha-L-arabinan + H2O
L-arabinose + alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
Bacillus subtilis F-11
-
F-11 best substrate
-
-
?
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
?
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
?
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside + L-arabinose
-
-
-
?
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside + L-arabinose
-
-
-
?
1,5-L-alpha-arabinoheptaose + H2O
1,5-L-alpha-arabinotriose + 1,5-L-alpha-arabinotetraose
-
-
-
-
?
1,5-L-alpha-arabinoheptaose + H2O
1,5-L-alpha-arabinotriose + 1,5-L-alpha-arabinotetraose
-
-
-
-
?
1,5-L-alpha-arabinopentaose + H2O
1,5-L-alpha-arabinotriose + 1,5-L-alpha-arabinobiose
-
-
-
-
?
1,5-L-alpha-arabinopentaose + H2O
1,5-L-alpha-arabinotriose + 1,5-L-alpha-arabinobiose
-
-
-
-
?
1,5-L-alpha-arabinotetraose + H2O
1,5-L-alpha-arabinobiose + 1,5-L-alpha-arabinobiose
-
-
-
-
?
1,5-L-alpha-arabinotetraose + H2O
1,5-L-alpha-arabinobiose + 1,5-L-alpha-arabinobiose
-
-
-
-
?
1,5-L-alpha-arabinotriose + H2O
L-arabinose + 1,5-L-alpha-arabinobiose
-
-
-
-
?
1,5-L-alpha-arabinotriose + H2O
L-arabinose + 1,5-L-alpha-arabinobiose
-
-
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
-
very poor substrate
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
-
poor substrate
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
-
mild hydrolysis: no significant degradation, exhaustive enzymatic hydrolysis: extremely low degradation
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
-
DP3
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
-
poor substrate
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
-
poor substrate
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
-
DP4
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, product formation, intermediate enzymatic hydrolysis: L-arabinobiose and much less L-arabinose + L-arabinotriose, end-products after exhaustive enzymatic degradation
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
-
-
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
-
DP5
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, product formation, end-products after exhaustive enzymatic degradation, intermediate enzymatic hydrolysis: L-arabinobiose + L-arabinotriose
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
-
-
-
-
?
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + H2O
alpha-L-arabinofuranose + alpha-L-arabinofuranosyl-(1-5)-O-alpha-L-arabinofuranose
-
DP8
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, product formation, end-products after exhaustive enzymatic degradation, intermediate enzymatic hydrolysis: L-arabinotriose + L-arabinopentaose and L-arabinobiose + L-arabinohexaose and L-arabinotetraose
?
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + H2O
L-arabinose
-
at very low rate, with high enzyme concentration
-
?
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + H2O
L-arabinose
-
at very low rate, with high enzyme concentration
-
?
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + H2O
L-arabinose
-
no or extremely low degradation
-
-
?
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + H2O
L-arabinose
-
DP2
-
-
?
arabinogalactan + H2O
?
-
for optimal breakdown of potato arabinogalactan combined action of endo-arabinase and endo-galactanase is required
-
-
?
cell wall polysaccharide + H2O
L-arabinan
-
F-11, primary cell wall polysaccharides
-
-
?
cell wall polysaccharide + H2O
L-arabinan
Bacillus subtilis F-11
-
F-11, primary cell wall polysaccharides
-
-
?
debranched 1,5-alpha-L-arabinan + H2O
?
highest activity
-
-
?
debranched 1,5-alpha-L-arabinan + H2O
?
highest activity
-
-
?
debranched arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
highest activity
-
-
?
debranched arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
-
?
feruloylated oligosaccharide + H2O
ferulic acid + ?
-
from sugar beet pulp, SBP
efficient releasing free ferulic acid from sugar beet pulp requires strong synergy involving three enzymes: endo-arabinanase, alpha-L-arabinofuranosidase and cinnamoyl esterase, free and esterified ferulic acid
?
feruloylated oligosaccharide + H2O
ferulic acid + ?
-
endo-arabinanase alone: very poor substrate, endo-arabinanase and alpha-L-arabinofuranosidase together: good substrate, best: combination endo-arabinanase, alpha-L-arabinofuranosidase and cinnamoyl esterase
efficient releasing free ferulic acid from sugar beet pulp requires strong synergy involving three enzymes: endo-arabinanase, alpha-L-arabinofuranosidase and cinnamoyl esterase, free and esterified ferulic acid
?
galactan + H2O
?
-
potato galactan: poor substrate, citrus galactan: very poor substrate
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
apple juice ultrafiltration retentate arabinan, branched sugar-beet arabinan, linear apple arabinan
end-product: low molecular weight oligomeric products
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
linear and branched arabinan
end-product: low molecular weight oligomeric products
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
random hydrolysis of L-arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
apple and sugar beet pulp
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
sugar beet pulp
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
apple juice ultrafiltration retentate arabinan, branched sugar-beet arabinan, linear apple arabinan
end-product: low molecular weight oligomeric products
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
beet and apple juice ultrafiltration retentate, UFR, arabinan
end-product: L-arabinose disaccharide + L-arabinose trisaccharide, upon exhaustive degradation of substrate some monomers, L-arabinose, are produced
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
sugar beet pulp
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
sugar beet pulp
end-product: L-arabinose disaccharide + L-arabinose trisaccharide, upon exhaustive degradation of substrate some monomers, L-arabinose, are produced
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
debranched and branched sugar beet arabinan
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
linear and branched arabinan
end-product: low molecular weight oligomeric products
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
random hydrolysis of L-arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
random hydrolysis of L-arabinan
end-product: L-arabinose disaccharide + L-arabinose trisaccharide, upon exhaustive degradation of substrate some monomers, L-arabinose, are produced
?
L-arabinan + H2O
L-arabino-oligosaccharides
Aspergillus niger N400 / DSM 2466 / ATCC 9029 / CBS 120.49
-
sugar beet pulp
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
sugar beet pulp
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
branched and partially debranched arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
sugar-beet arabinan in commercial apple juice concentrate
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
random hydrolysis of L-arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
random hydrolysis of L-arabinan
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
Bacillus subtilis F-11
-
sugar-beet arabinan in commercial apple juice concentrate
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
Bacillus subtilis F-11
-
branched and partially debranched arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
Clostridium felsineum var. sikokianum
-
random hydrolysis of L-arabinan
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
-
main product: L-arabinotriose
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
linear arabinan
main product: L-arabinotriose
?
L-arabinan + H2O
L-arabino-oligosaccharides
-
branched sugar beet arabinan containing alpha-1,3-arabinose side chains: not a substrate
main product: L-arabinotriose
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
-
-
-
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
-
-
product formation, small oligomeric products
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
-
-
product formation, small oligomeric products
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
-
degree of polymerization 2-8, DP2-8
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, L-arabinose + L-arabinobiose: end-products after exhaustive enzymatic degradation, product formation
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
-
linear 1,5-alpha-L-arabino-oligosaccharide
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times, L-arabinose + L-arabinobiose: end-products after exhaustive enzymatic degradation, product formation
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
-
-
main product: L-arabinotriose
?
linear 1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
?
linear 1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
?
linear arabinan + H2O
?
-
hydrolyzed at 62% compared to debranched arabinan
-
-
?
linear arabinan + H2O
?
the enzyme is selective for linear arabinan
-
-
?
linear arabinan + H2O
?
the enzyme is selective for linear arabinan
-
-
?
protopectin + H2O
pectin
-
IFO 3134, protopectin of sugar beet pulp and various citrus fruit peels, but much less on that from lemon peel
IFO 3134, highly polymerized pectin
?
protopectin + H2O
pectin
-
IFO 3134, protopectin of sugar-beet and apple pulp
IFO 3134, soluble pectin
?
red debranched arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
?
red debranched arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
?
sugar beet arabinan + H2O
?
the substrate is composed of 1,2-alpha- and 1,3-alpha-L-arabinofuranosyl side chains linked to a 1,5-alpha-L-arabinofuranosyl backbone
-
-
?
sugar beet arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
?
sugar beet arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
?
sugar beet arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
-
?
sugar beet arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside + L-arabinose
-
-
-
?
sugar beet arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside + L-arabinose
-
-
-
?
additional information
?
-
-
substrate binding site, action pattern, subsite mapping
-
-
?
additional information
?
-
-
no bi-substrate reactions such as condensation or transglycosylation
-
-
?
additional information
?
-
-
inactive on p-nitrophenylarabinofuranoside, onion arabinogalactan, stractan, wheat arabinoxylan, oat spelts arabinoxylan, avicel, polygalacturonic acid
-
-
?
additional information
?
-
-
inactive on p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
additional information
?
-
-
substrate binding site, action pattern, subsite mapping
-
-
?
additional information
?
-
-
no bi-substrate reactions such as condensation or transglycosylation
-
-
?
additional information
?
-
-
composition of end-products depends largely on substrate and enzyme concentrations, and on incubation times
-
-
?
additional information
?
-
-
inactive towards synthetic arabinosides, p-nitrophenyl-alpha-L-arabinoside, arabinose disaccharide, arabinogalactan, stractan and xylan from oat spelts
-
-
?
additional information
?
-
the enzyme randomly cleaves the internal alpha-(1,5)-linked L-arabinofuranosyl residues of a branchless arabinan backbone to release arabinotriose mainly, although a small amount of arabino-oligosaccharide intermediates is also liberated
-
-
?
additional information
?
-
the enzyme randomly cleaves the internal alpha-(1,5)-linked L-arabinofuranosyl residues of a branchless arabinan backbone to release arabinotriose mainly, although a small amount of arabino-oligosaccharide intermediates is also liberated
-
-
?
additional information
?
-
-
no activity with: laminarin, lichenan, galactomannan, beta-glucan, wheat and rye arabinoxylan, xyloglucan, carboxymethyl cellulose, pectin from fruits, larch arabinogalactan, galactan (potato), xylan from beechwood, and 1,4-beta-mannan
-
-
?
additional information
?
-
the enzyme shows a synergic effect with the commercial cocktail Accellerase 1500 on cellulose hydrolysis. It weakens the interaction between cellulose fibers in filter paper, thus providing an increased access to the cellulases of the cocktail
-
-
?
additional information
?
-
-
the enzyme shows a synergic effect with the commercial cocktail Accellerase 1500 on cellulose hydrolysis. It weakens the interaction between cellulose fibers in filter paper, thus providing an increased access to the cellulases of the cocktail
-
-
?
additional information
?
-
the enzyme shows a synergic effect with the commercial cocktail Accellerase 1500 on cellulose hydrolysis. It weakens the interaction between cellulose fibers in filter paper, thus providing an increased access to the cellulases of the cocktail
-
-
?
additional information
?
-
the enzyme randomly cleaves the internal alpha-(1,5)-linked L-arabinofuranosyl residues of a branchless arabinan backbone to release arabinotriose mainly, although a small amount of arabino-oligosaccharide intermediates is also liberated
-
-
?
additional information
?
-
the enzyme randomly cleaves the internal alpha-(1,5)-linked L-arabinofuranosyl residues of a branchless arabinan backbone to release arabinotriose mainly, although a small amount of arabino-oligosaccharide intermediates is also liberated
-
-
?
additional information
?
-
-
IFO 3022: potato disc macerating activity, able to loosen potato tissue
-
-
?
additional information
?
-
-
IFO 3022: potato disc macerating activity, able to loosen potato tissue
-
-
?
additional information
?
-
-
IFO 3022: inactive on p-nitrophenyl alpha-L-arabinofuranoside, p-nitrophenyl alpha-D-galactopyranoside, p-nitrophenyl beta-D-galactopyranoside, arabinogalactan, carboxymethyl cellulose, filter paper, pectin and polygalacturonic acid
-
-
?
additional information
?
-
-
F-11: inactive on phenyl alpha-L-arabinofuranoside, p-nitrophenyl alpha-D-galactopyranoside, p-nitrophenyl beta-D-galactopyranoside, arabinoxylan, arabinogalactan and gum arabic
-
-
?
additional information
?
-
-
IFO 3134, inactive on polygalacturonic acid and soluble pectin
-
-
?
additional information
?
-
-
inactive towards phenyl and p-nitrophenyl alpha-L-arabinofuranoside, arabinoxylan, arabinogalactan, and gum arabic
-
-
?
additional information
?
-
-
plays a role in degradation of plant tissues, macerating enzyme
-
-
?
additional information
?
-
shows no activity toward larchwood arabinogalactan, wheat arabinoxylan, and p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
additional information
?
-
-
shows no activity toward larchwood arabinogalactan, wheat arabinoxylan, and p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
additional information
?
-
shows no activity toward larchwood arabinogalactan, wheat arabinoxylan, and p-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
additional information
?
-
Bacillus subtilis F-11
-
IFO 3022: potato disc macerating activity, able to loosen potato tissue
-
-
?
additional information
?
-
Bacillus subtilis F-11
-
inactive towards phenyl and p-nitrophenyl alpha-L-arabinofuranoside, arabinoxylan, arabinogalactan, and gum arabic
-
-
?
additional information
?
-
Bacillus subtilis F-11
-
F-11: inactive on phenyl alpha-L-arabinofuranoside, p-nitrophenyl alpha-D-galactopyranoside, p-nitrophenyl beta-D-galactopyranoside, arabinoxylan, arabinogalactan and gum arabic
-
-
?
additional information
?
-
-
the enzyme fails to cleave 1,5-alpha-arabinobiose, branched arabinan, arabinoxylan, arabinogalactan, xylan, and galactan
-
-
?
additional information
?
-
-
the enzyme fails to cleave 1,5-alpha-arabinobiose, branched arabinan, arabinoxylan, arabinogalactan, xylan, and galactan
-
-
?
additional information
?
-
no activity for arabinoxylan, 1,4-beta-D-xylose units with side chains of 1,3-alpha-L-arabinose, xylan, starch, or 4-nitrophenyl-alpha-L-arabinofuranoside, a typical substrate for the arabinofuranosidase. Synergistic hydroysis of arabinan by endo-1,5-alpha-L-arabinanase and alpha-L-arabinofuranosidase
-
-
?
additional information
?
-
AB063312
no substrates: carboxymethyl cellulose, xylan, polygalacturonate, pectin, galactan, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside,4-nitrophenyl-alpha-D-xylopyranoside and 4-nitrophenyl-beta-D-cellobioside
-
-
?
additional information
?
-
-
no substrates: carboxymethyl cellulose, xylan, polygalacturonate, pectin, galactan, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside,4-nitrophenyl-alpha-D-xylopyranoside and 4-nitrophenyl-beta-D-cellobioside
-
-
?
additional information
?
-
AB063312
no substrates: carboxymethyl cellulose, xylan, polygalacturonate, pectin, galactan, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-beta-D-galactopyranoside, 4-nitrophenyl-alpha-D-galactopyranoside,4-nitrophenyl-alpha-D-xylopyranoside and 4-nitrophenyl-beta-D-cellobioside
-
-
?
additional information
?
-
-
alkali extract of cell walls of Gossypium hirsutum is sequentially digested by endo-polygalacturonase, arabinofuranosidase, endo-arabinase, and rhamnogalacturonan hydrolase AN9314.2
-
-
?
additional information
?
-
no activity with 4-nitrophenyl-alpha-L-arabinofuranoside, beechwood xylan, wheat flour arabinoxylan, larch arabinogalactan, gum arabic, and soluble starch
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl-alpha-L-arabinofuranoside, beechwood xylan, wheat flour arabinoxylan, larch arabinogalactan, gum arabic, and soluble starch
-
-
?
additional information
?
-
no activity with 4-nitrophenyl-alpha-L-arabinofuranoside, beechwood xylan, wheat flour arabinoxylan, larch arabinogalactan, gum arabic, and soluble starch
-
-
?
additional information
?
-
-
no activity with 4-nitrophenyl-alpha-L-arabinofuranoside, beechwood xylan, wheat flour arabinoxylan, larch arabinogalactan, gum arabic, and soluble starch
-
-
?
additional information
?
-
does not hydrolyze birchwood xylan and 4-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
additional information
?
-
-
does not hydrolyze birchwood xylan and 4-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
additional information
?
-
-
inactive on cellulose, avicel, amorphous cellulose, carboxymethylcellulose, xylan, galactan, mannan, 4-nitrophenyl alpha-L-arabinofuranoside, 4-nitrophenyl alpha-L-arabinopyranoside, 4-nitrophenyl beta-xyloside and 2,4-dinitrophenyl beta-xylobioside
-
-
?
additional information
?
-
-
there is no activity towards 1,4-beta-D-mannan, galactan, 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-alpha-L-arabinofuranoside
-
-
?
additional information
?
-
no substrates: birchwood xylan, 4-nitrophenyl-alpha-L-arabinofuranoside, 4-nitrophenyl-alpha-L-arabinopyranoside, and 4-nitrophenyl-beta-D-xylopyranoside
-
-
?
additional information
?
-
no activity with birchwood xylan, beechwood xylan, citric pectin and arabinogalactan
-
-
?
additional information
?
-
-
no activity with birchwood xylan, beechwood xylan, citric pectin and arabinogalactan
-
-
?
additional information
?
-
-
the enzyme shows the ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides
-
-
?
additional information
?
-
the enzyme acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan
-
-
?
additional information
?
-
-
the enzyme acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
?
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
-
-
-
?
additional information
?
-
-
plays a role in degradation of plant tissues, macerating enzyme
-
-
?
additional information
?
-
-
the enzyme shows the ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
CaCl2
Co2+
MgCl2
Mn2+
additional information
Ca2+
activity is partially dependent of a bound Ca2+ since 70% of the maximal activity is preserved even when 1 mM EDTA is added to the reaction medium
Ca2+
isoform Arb43B possesses a cluster containing a calcium ion in the catalytic domain
additional information
-
IFO 3134, stimulation of enzyme production by several phosphates, but not by chloride, acetate or sulfate
additional information
the addition of Ca2+ has no effect
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EGTA
isoform Arb43B shows a drastic decrease in the activity of the enzyme in the presence of 1 mm EGTA
additional information
-
no inhibition by CaCl2, EDTA, L-arabono-gamma-lactone, L-arabinose, D-arabitol
-
additional information
-
IFO 3022: no inhibition by L-arabonic-gamma-lactone, D- and L-galactonic-gamma-lactones
-
additional information
expression of abn2 is repressed by glucose. Glucose causes a 17- and 44fold repression of the abn2'-lacZ fusion expression during the exponential growth phase and the early postexponential phase, respectively
-
additional information
-
expression of abn2 is repressed by glucose. Glucose causes a 17- and 44fold repression of the abn2'-lacZ fusion expression during the exponential growth phase and the early postexponential phase, respectively
-
additional information
-
Abn1 is not inhibited by arabinobiose in the degradation of linear arabinan even when 50 mg/ml arabinobiose are added
-
additional information
AB063312
no inhibition by Ba2+, Mn2+ and Mg2+
-
additional information
-
no inhibition by Ba2+, Mn2+ and Mg2+
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-arabinose
-
induction of endo-arabinase, addition of D-glucose prevents this induction
L-arabinose
-
induction of endo-arabinase, addition of D-glucose prevents this induction
L-arabitol
-
induction of endo-arabinase, addition of D-glucose prevents this induction
L-arabitol
-
induction of endo-arabinase, addition of D-glucose prevents this induction
additional information
expression of abn2 is stimulated by arabinan and pectin, arabinose is not the natural inducer. EDTA does not affect the activity
-
additional information
-
expression of abn2 is stimulated by arabinan and pectin, arabinose is not the natural inducer. EDTA does not affect the activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
The endo-arabinanase BcAra1 is a novel host-specific virulence factor of the necrotic fungal phytopathogen Botrytis cinerea.
Neoplasms
Inositol phosphate capping of the nonreducing termini of lipoarabinomannan from rapidly growing strains of Mycobacterium.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.37
4-nitrophenyl alpha-L-arabinofuranoside
pH 4.5, 37°C
0.388 - 0.592
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
0.388
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
-
-
0.592
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
-
-
9.3
L-arabinan
-
apple juice ultrafiltration retentate, UFR, arabinan, linearised
0.076
linear 1,5-alpha-L-arabinan
mutant H318A of isoform Arb43B, pH and temperature not specified in the publication
0.111
linear 1,5-alpha-L-arabinan
wild type isoform Arb43B, pH and temperature not specified in the publication
additional information
additional information
-
kinetic data and mechanism
-
additional information
additional information
-
kinetic data and mechanism
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
50
1,5-alpha-L-arabinan
recombinant enzyme, pH 6.5, 75°C
3.1
linear 1,5-alpha-L-arabinan
mutant H318A of isoform Arb43B, pH and temperature not specified in the publication
68.7
linear 1,5-alpha-L-arabinan
wild type enzyme, at 40°C and pH 6.0
99.7
linear 1,5-alpha-L-arabinan
mutant enzyme H218D, at 40°C and pH 6.0
191.6
linear 1,5-alpha-L-arabinan
wild type isoform Arb43B, pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00004
linear 1,5-alpha-L-arabinan
mutant H318A of isoform Arb43B, pH and temperature not specified in the publication
0.00172
linear 1,5-alpha-L-arabinan
wild type isoform Arb43B, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.13
sugar beet arabinan as substrate, in 50 mM sodium acetate buffer (pH 6.0) at 55°C
12
purified recombinant enzyme, substrate 1,5-alpha-L-arabinan
152.1
purified protein, using L-arabinan as substrate, at pH 6.0 and 70°C
2.6
purified recombinant enzyme, substrate is sugar beet arabinan
26
-
using linear arabinan as substrate, pH and temperature not specified in the publication
64.52
with linear 1,5-alpha-L-arabinan as substrate, in 50 mM sodium acetate buffer (pH 6.0) at 55°C
71.69
with debranched 1,5-alpha-L-arabinan as substrate, in 50 mM sodium acetate buffer (pH 6.0) at 55°C
73.4
with linear linear 1,5-alpha-L-arabinan as substrate, at 40°C, pH 6.0
additional information
additional information
-
no detectable activity against larch wood arabinoxylan, wheat arabinoxylan or p-nitrophenyl-alpha-L-arabinofuranoside
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6
5.5
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
the enzyme shows 30%, 55%, 100%, 70%, 15% and less than 5% activity at pH 3.0, 4.0, 5.0, 6.0, 7.0, and 8.0, respectively
3.5 - 5
pH 3.5: about 45% of maximal activity, pH 5.0: about 50% of maximal activity
4 - 7
the enzyme retains more than 75% activity over a pH range from 4.0 to 7.0
5 - 6.5
activity is markedly reduced to about 50% at pH 5.0 and at pH 6.5, respectively
5 - 7
the enzyme achieves about 20.4 and 83.6% of the maximal activity at pH 5.0 and 7.0, respectively
5 - 8
arabinanase activity drops to about 55% and 70% of the highest activity at pH 5.0 and 8.0, respectively
5 - 8.5
-
pH 5.0: about 65% of maximal activity, pH 8.5: about 40% of maximal activity
5.5 - 7.5
7 - 9
pH 7.0: about 55% of maximal activity, pH 9.0: about 20% of maximal activity
5.5 - 7.5
-
about 35% activity at pH 5.5, about 50% activity at pH 7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
50
55
60
70
75
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 40
15°C: about 45% of maximal activity, 40°C: about 70% of maximal activity
30 - 45
-
30°C: about 75% of maximal activity, 45°C: about 70% of maximal activity
30 - 60
30°C: about 35% of maximal activity, 60°C: about 40% of maximal activity
30 - 70
about 45% activity at 30°C, about 65% activity at 40°C, about 85% activity at 50°C, about 80% activity at 60°C, and about 20% activity at 70°C
30 - 80
the enzyme shows less than 40% activity at 30°C, less than 50% activity at 40°C, and more than 80% activity at 50°V. Enzyme activity decreases rapidly when the reaction temperature is above 60°C, and the enzyme loses most of ist activity at 80°C
60 - 90
-
about 50% activity at pH 60°C, about 70% activity at pH 70°C, about 95% activity at pH 80°C, about 92% activity at pH 85°C, about 20% activity at 90°C
62 - 80
the enzyme shows relative activity ranging from 77% to 78% at temperatures of 62°C and 80°C, respectively
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type WG096 and cre mutant, carbon catabolite derepressed mutant
-
-
brenda
-
-
-
brenda
arabinanase A, exhibits endo- and exo-mode of action
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the mesocarp promotes the production of the enzyme (71%) when compared to the whole fruit (60.6%) and the other epicarp layers endocarp (26%) and kernel (28%). The mesocarp of Terminalia catappa is a potential and cost effective source for the production of alpha 1,5-L-endo-arabinase
brenda
-
the mesocarp promotes the production of the enzyme (71%) when compared to the whole fruit (60.6%) and the other epicarp layers endocarp (26%) and kernel (28%). The mesocarp of Terminalia catappa is a potential and cost effective source for the production of alpha 1,5-L-endo-arabinase
brenda
-
the mesocarp promotes the production of the enzyme (71%) when compared to the whole fruit (60.6%) and the other epicarp layers endocarp (26%) and kernel (28%). The mesocarp of Terminalia catappa is a potential and cost effective source for the production of alpha 1,5-L-endo-arabinase
brenda
-
the mesocarp promotes the production of the enzyme (71%) when compared to the whole fruit (60.6%) and the other epicarp layers endocarp (26%) and kernel (28%). The mesocarp of Terminalia catappa is a potential and cost effective source for the production of alpha 1,5-L-endo-arabinase
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
the enzyme plays an important role as a virulence factor during the infection of Arabidopsis thaliana, but the enzyme is not required for full virulence of Botrytis cinerea on Nicotiana benthamiana and tomato
physiological function
-
screening of thermophilic and thermotolerant filamentous fungi for the production of beta-xylosidase and arabinanase at different temperatures. beta-Xylosidase and arabinanase activities from mycelial extract (intracellular form) are higher in cultures grown at high temperatures (35-40°C), while the correspondent extracellular activities are favorably secreted from cultures at 30°C. Aspergillus niger and Aspergillus thermomutatus are the filamentous fungi with the most expressive production of beta-xylosidase and arabinanase, respectively
physiological function
-
the enzyme plays an important role as a virulence factor during the infection of Arabidopsis thaliana, but the enzyme is not required for full virulence of Botrytis cinerea on Nicotiana benthamiana and tomato
-
Show AA Sequence and Transmembrane Helices (2379 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
112000
recombinant His-tagged enzyme, gel filtration
27000
30000
31000
33000
33900
34000
35000
36000
45000
56000
2 * 56000, recombinant His-tagged enzyme, SDS-PAGE, 2 x 56268, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 56000, recombinant His-tagged enzyme, SDS-PAGE, 2 x 56268, sequence calculation
monomer
additional information
structure modelling and analysis, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
additional information
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native and seleno-methionine-labelled derivative, by sitting-drop vapour-diffusion method, to 1.9 and 2.7 A resolution, respectively. Native protein crystals appear in two different space groups, P1, with unit-cell parameters a=51.9, b=57.6, c=86.2 A, alpha=82.3, beta=87.9, gamma=63.6, and P212121, with unit-cell parameters a=57.9, b=163.3, c=202.0 A. The selenol-methionine-labelled derivative of Abn2 only crystallizes in one crystal form, which is similar to the form of space group P212121 of the wild-type protein, with unit-cell parameters a=57.84, b=163.22, c=201.85 A, which can accommodate four molecules (each containing 13 selenomethionine residues) in the asymmetric unit
sitting drop vapor diffusion method, using 65% (w/v) 2-methyl-2,4-pentadiol and 100 mM Tris, pH 8.5
vapor diffusion method, using 10 mM NiCl2, 100 mM tris(hydroxymethyl)aminomethane-HCl pH 8.5, and 20% PEG 2000 monomethyl ether
purified recombinant wild-type enzyme, and mutant enzyme E201A in complex with arabinotriose, hanging drop vapour diffusion, 0.0025-0.003 ml of protein solution with 6.5-13 mg/ml protein is mixed with an equal volume of precipitant solution containing 1.7 M lithium sulfate, 0.1 M Tris buffer, pH 7.5, and 15% v/v glycerol for the wild-type enzyme, and 1.9 M lithium sulfate, 0.1 M Tris buffer, pH 8.5, and 4% w/v PEG 400 for the mutant enzyme, X-ray diffraction structure determination and analysis, molecular replacement
hanging-drop vapor-diffusion method using 1.0 mM sodium citrate as a precipitant at pH 6.0. Structure determined at 1.9 A to an R-factor of 18.3% and an R-free-factor of 22.5%. The enzyme molecule has a five-bladed beta-propeller fold. Crystals belong to orthorhombic space group P2(1)2(1)2(1) with unit cell parameters of a = 40.3, b = 77.8 and c = 89.7 A
-
sitting-drop vapor-diffusion method at 20°C. Crystal structures of inactive mutant enzymes D27A and D147N, are determined in complex with arabino-oligosaccharides
crystallization is performed by the sitting-drop vapour-diffusion method. Single crystals are obtained from a solution containing 0.1 M MES buffer pH 6.5, 0.8 M ammonium sulfate, 0.1 M EDTA, 0.1 M L-proline and 5% (v/v) dioxane. X-ray diffraction data are collected to a resolution of 2.86 A using synchrotron radiation. The diffraction pattern is indexed in the tetragonal space group P422, with unit-cell parameters a = b = 83.71, c = 408.25 A
purified recombinant His-tagged enzyme, 0.0005 ml of protein solution containing 30 mg/ml in 25 mM Tris-HCl buffer, pH 7, 5, is mixed with 0.0005 ml of reservoir solution containing 0.1 M MES buffer, pH 6.5, 0.8 M ammonium sulfate, 0.1 M EDTA, 0.1 M L-proline and 5% v/v dioxane, X-ray diffraction structure determination and analysis at 2.86 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H318A
the mutant of isoform Arb43B displays a drastic decrease in enzymatic activity
H318Q
D147A
site-directed mutagenesis, structure comparison with the wild-type enzyme
E201A
site-directed mutagenesis, structure comparison with the wild-type enzyme
D147A
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
E201A
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
DELTAV2-W17
H218D
the mutant shows higher catalytic efficiency, kcat is improved about 45% versus that of the wild type enzyme
H218E
the mutant is active, but it does not change the enzymatic property obviously under acidic condition compared with the wild type enzyme
additional information
DELTAV2-W17
-
deletion of the N-terminal amino acids causes thermal instability
DELTAV2-W17
-
deletion of the N-terminal amino acids causes thermal instability
-
additional information
mutant strains IQB413 (DELTAabnA), IQB485 (DELTAabn2), and IQB486 (DELTAabnA DELTAabn2). Almost complete loss of activity in the DELTAabn2 DELTAabnA double mutant
additional information
-
mutant strains IQB413 (DELTAabnA), IQB485 (DELTAabn2), and IQB486 (DELTAabnA DELTAabn2). Almost complete loss of activity in the DELTAabn2 DELTAabnA double mutant
additional information
-
mutant strains IQB413 (DELTAabnA), IQB485 (DELTAabn2), and IQB486 (DELTAabnA DELTAabn2). Almost complete loss of activity in the DELTAabn2 DELTAabnA double mutant
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 12
the enzyme shows more than 60% activity at pH 5.0-11.0 after 1 h incubation
732332
5 - 7
the enzyme is stable at pH 7.0 compared with 55.5 and 5.78% of maximal activity remaining after 30 min of incubation at pH 6.0 and 5.0 respectively
731976
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
45
5
the specific activity of the enzyme remains 54.1% of maximum at 5°C
50
50 - 60
60
65
70
70 - 80
-
the half-lives of the immobilized endoarabinanase at 70°C, 75°C, and 80°C are 745, 290, and 64 h, respectively
70 - 85
-
the enzyme retains more than 95% of its initial activity at 70°C for 1 h. After being incubated at 80°C for 2 h, the residual activity retained is more than 80% of the initial activity. The enzyme retains more than 90% of its maximum activity at 85°C after 10 min incubation
75
90 - 95
the enzyme is fully heat-stable (up to 10 h) and retains activity at temperatures up to 90°C. The enzyme loses its activity only after 90 min when incubated at 95°C
additional information
50
-
50% loss of activity after 30 min incubation at 50°C. After 60 min the activity is about 20% of the initial value
50
remains fully active after 30 min of preincubation at 50°C. After preincubation at 60°C, the residual activity is only 15%
50
-
no obvious enzymatic activity decline is observed for enzyme incubated at 40°C for 120 min. The enzyme retains the most of its initial enzyme activity at 50°C for a 120 min incubation. However, the activity decreases rapidly following its incubation at 60°C
50 - 60
the half-life of the enzyme at 50, 55, and 60°C are 280, 152, and 30 min, respectively
50 - 60
the enzyme maintains 100% of the initial activity by treatment it at 50°C for 1 h, while approximately 70% of the activity is lost at 60°C
60
-
mutant enzyme DELTAV2-W17 loses 65% of its activity after 4 h, half-life: 2.5 h
65
purified recombinant His-tagged enzyme, half-life is 2440 h
65
-
mutant enzyme DELTAV2-W17, 70% loss of activity after 5 min
70
purified recombinant His-tagged enzyme, half-life is 254 h
70
-
wild-type enzyme retains more than 80% of its activity after 4 h, complete loss of activity of mutant enzyme DELTAV2-W17 after 5 min
75
purified recombinant His-tagged enzyme, half-life is 93 h
additional information
adding CoCl2 hexahydrate results in a marked increase in melting temperature, of almost 10°C. Strontium chloride also stabilizes BlAbn1 against thermal denaturation
additional information
-
adding CoCl2 hexahydrate results in a marked increase in melting temperature, of almost 10°C. Strontium chloride also stabilizes BlAbn1 against thermal denaturation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
IFO 3134, enzyme stable against protease secreted by the microorganism even during 2 days cultivation
-
the enzyme stability increases 128fold when immobilized with glyoxyl agarose
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM sodium acetate or piperazine buffer, pH 5.0 dispensed in small tubes
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CM-Toyopearl 650 M column chromatography, Ni Sepharose 6 column chromatography, butyl-Toyopearl column chromatography, and Superdex 75 gel filtration
DEAE Sepharose column chromatography, Sephacryl S-300 gel filtration, and Blue Sepharose affinity chromatography
-
hydrophobic chromatography, anion-exchange chromatography, gel filtration chromatography
-
Ni2+-chelating affinity column chromatography and Superdex 75 gel filtration
recombinant His-tagged enzyme 39fold from Escherichia coli by nickel affinity chromatography
wild-type and selenol-methionine-labelled protein purified on nickel column, more than 95% pure
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Abn2 overexpressed in Escherichia coli BL21(DE3) pLysS harboring pZI39
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) pLysS cells
expression in Escherichia coli
expression in Escherichia coli BL21(DE3) cells as fusion proteins with a His-tag at the C-terminus
wild-type ligated into vector pET30a(+) and overexpressed in Escherichia coli BL21 (DE3) pLysS harbouring pZI39. Selenol-methionine-labelled protein overexpressed in an auxotrophic Escherichia coli strain B834 (DE3) harbouring pZI39
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the gene encoding cold-adapted endo-arabinase Abnc is strongly induced by arabinose, arabinitol, and arabinan
expression of the gene encoding cold-adapted endo-arabinase Abnc is strongly induced by arabinose, arabinitol, and arabinan
expression of the gene encoding cold-adapted endo-arabinase Abnc is strongly induced by arabinose, arabinitol, and arabinan
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biofuel production
degradation
synergistic action of arase and pectinase can significantly improve the degradation of sugar beet pulp
industry
-
endo-1,5-alpha-L-arabinanases belonging to glycoside hydrolase family 43 are of great industrial interest for use in food technology, organic synthesis and biofuel production owing to their ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides
nutrition
synthesis
-
applied to the refinement of cotton fiber, enzyme is able to release the cotton fiber coating, yielding product of high quality but with lower amounts of wastes
additional information
-
the hydrolysis of pretreated sugar cane biomass increases by 15% when a commercial enzyme cocktail is supplemented with immobilized ABNase. Pectin hydrolysis by recombinant ABNase plays a role in the effective application of enzymatic cocktails for biomass saccharification
analysis
-
structural analysis of plant cell pectic polysaccharides and arabinans
analysis
-
useful in structural analysis of primary cell wall polysaccharides
analysis
Bacillus subtilis F-11
-
useful in structural analysis of primary cell wall polysaccharides
-
biofuel production
conversion of lignocellulosic biomass to biofuels. Endo-1,5-alpha-L-arabinanase hydrolyzes alpha-1,5-arabinofuranosidic bonds in hemicelluloses such as arabinoxylan and arabinan as well as in other arabinose-containing polysaccharides
biofuel production
-
conversion of lignocellulosic biomass to biofuels. Endo-1,5-alpha-L-arabinanase hydrolyzes alpha-1,5-arabinofuranosidic bonds in hemicelluloses such as arabinoxylan and arabinan as well as in other arabinose-containing polysaccharides
-
nutrition
-
commercial applications in fruit and vegetable processing, particularly in apple juice manufacture where their use prevents haze formation in pectinase-treated apple pulp by depolymerizing debranched arabinan, linear alpha-1,5-arabinan, formed by the action of alpha-L-arabinofuranosidases during this process
nutrition
-
commercial applications in fruit and vegetable processing, particularly in apple juice manufacture where their use prevents haze formation in pectinase-treated apple pulp by depolymerizing debranched arabinan, linear alpha-1,5-arabinan, formed by the action of alpha-L-arabinofuranosidases during this process
nutrition
-
useful for pectin extraction from citrus peel from fruit-juice industries and sugar-beet pulp from sugar factories
nutrition
-
production of L-arabinose from plant arabinan at high temperatures
nutrition
-
production of L-arabinose from plant arabinan at high temperatures
-
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REF.
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ORGANISM (UNIPROT)
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Caldicellulosiruptor saccharolyticus
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14
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Cloning and characterization of a cold-adapted endo-1,5-alpha-L-arabinanase from Paenibacillus polymyxa and rational design for acidic applicability
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brenda
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50
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Bacillus licheniformis (Q65GB9), Bacillus licheniformis (Q65L63), Bacillus licheniformis DSM 13 (Q65GB9), Bacillus licheniformis DSM 13 (Q65L63)
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27
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31
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brenda
Chen, Z.; Liu, Y.; Yan, Q.; Yang, S.; Jiang, Z.
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63
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Rhizomucor miehei (A0A0C4JZB0)
brenda
Squina, F.; Prade, R.; Wang, H.; Murakami, M.
Expression, purification, crystallization and preliminary crystallographic analysis of an endo-1,5-alpha-L-arabinanase from hyperthermophilic Thermotoga petrophila
Acta Crystallogr. Sect. F
65
902-905
2009
Thermotoga petrophila (A5IKD4), Thermotoga petrophila, Thermotoga petrophila DSM 13995 (A5IKD4)
brenda
Yamaguchi, A.; Sogabe, Y.; Fukuoka, S.; Sakai, T.; Tada, T.
Structures of endo-1,5-alpha-L-arabinanase mutants from Bacillus thermodenitrificans TS-3 in complex with arabino-oligosaccharides
Acta Crystallogr. Sect. F
74
774-780
2018
Geobacillus thermodenitrificans (Q93HT9), Geobacillus thermodenitrificans
brenda
Machado, C.B.; Citadini, A.P.; Goldbeck, R.; de Lima, E.A.; Figueiredo, F.L.; da Silva, T.M.; Hoffmam, Z.B.; de Sousa, A.S.; Squina, F.M.; de Lourdes Teixeira de Moraes Polizeli, M.; Ruller, R.; Ward, R.J.
Increased biomass saccharification by supplementation of a commercial enzyme cocktail with endo-arabinanase from Bacillus licheniformis
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37
1455-1462
2015
Bacillus licheniformis
brenda
Vilches, F.; Ravanal, M.C.; Bravo-Moraga, F.; Gonzalez-Nilo, D.; Eyzaguirre, J.
Penicillium purpurogenum produces a novel endo-1,5-arabinanase, active on debranched arabinan, short arabinooligosaccharides and on the artificial substrate p-nitrophenyl arabinofuranoside
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455
106-113
2018
Talaromyces purpureogenus (A0A2H4RAB6), Talaromyces purpureogenus
brenda
Farro, E.G.S.; Leite, A.E.T.; Silva, I.A.; Filgueiras, J.G.; de Azevedo, E.R.; Polikarpov, I.; Nascimento, A.S.
GH43 endo-arabinanase from Bacillus licheniformis Structure, activity and unexpected synergistic effect on cellulose enzymatic hydrolysis
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117
7-16
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Bacillus licheniformis (Q65GB9), Bacillus licheniformis, Bacillus licheniformis ATCC 14580 (Q65GB9)
brenda
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Mesocarp of Terminalia catappa L. - a potential and cost effective source for the production of alpha 1,5-L-endo-arabinase
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9
222-227
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Terminalia catappa
-
brenda
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Release 2023.1 (January 2023)
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