Information on EC 3.2.1.99 - arabinan endo-1,5-alpha-L-arabinanase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

SplaateEC_Number,Commentary
EC NUMBER
COMMENTARY
3.2.1.99
-
SplaateRecommended_Name,GO_Number
RECOMMENDED NAME
GeneOntology No.
arabinan endo-1,5-alpha-L-arabinanase
-
SplaateReaction,Reaction_id,Commentary,IF(Commentary != '',Organism,'') ,IF(Commentary != '',Literature,'')
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
-
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
-
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
-
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
also acts slowly on beet-arabinan
-
-
-
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
three catalytic carboxylates: Asp27, the general base, Glu201, the general acid, and Asp147, the pKa modulator, substrate binding structure and catalytic mechanism, overview
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
Aspergillus niger N400, Aspergillus niger N400(CBS 120-49)
-
-
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
three catalytic carboxylates: Asp27, the general base, Glu201, the general acid, and Asp147, the pKa modulator, substrate binding structure and catalytic mechanism, overview
Geobacillus stearothermophilus T-6
-
-
SplaateReaction_Type,Organism,Commentary,Literature
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SplaatePathway,BRENDA_Link,KEGG_Link,MetaCyc_Link,Source_Database
SplaateSystematic_Name,Commentary_IUBMB
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.
SplaateSynonyms,Organism,Commentary,Literature
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1,5-alpha-arabinanase A
-
exhibits endo- and exo-mode of action
ABN
Geobacillus thermodenitrificans TS-3
AB063312
-
-
ABN
Thermotoga thermarum
-
-
Abn1
Chrysosporium lucknowense C1
-
-
-
Abn2
Bacillus subtilis 168, Bacillus subtilis 168T+
-
-
abnA1
Bacillus licheniformis DSM13
isoform
-
abnA2
Bacillus licheniformis DSM13
isoform
-
ABNase
Bacillus licheniformis DSM13
-
-
Abnc
Penicillium chrysogenum 31B
-
-
-
AbnS1
Penicillium chrysogenum 31B
-
-
AbnZ1
Paenibacillus polymyxa Z6
-
-
alpha-1,5-L-endo-arabinanase
-
-
alpha-1,5-L-endo-arabinanase
Botrytis cinerea IK2018
-
-
-
alpha-L-arabinohydrolase
-
-
alpha-L-arabinohydrolase
Chrysosporium lucknowense C1
-
-
-
ARA1
Botrytis cinerea IK2018
-
-
-
araban 5-alpha-L-arabinohydrolase
-
-
-
-
arabinanase A
-
exhibits endo- and exo-mode of action
arabinase, endo-1,5-alpha-L-
-
-
-
-
Arb43A
isoform, formally named AbnA
Arb43B
isoform, formally named Abn2
arbA
-
exhibits endo- and exo-mode of action
CEDAase
-
-
cold-adapted endo-arabinanase
-
-
cold-adapted endo-arabinanase
Penicillium chrysogenum 31B
-
-
-
endo-(1,5)-alpha-L-arabinanase
-
endo-(1,5)-alpha-L-arabinanase
Bacillus licheniformis DSM13
-
-
endo-(1->5)-alpha-L-arabinanase
-
-
-
-
endo-1,5-alpha-arabinanase
-
-
-
-
endo-1,5-alpha-arabinanase
-
endo-1,5-alpha-L-arabinanase
-
-
-
-
endo-1,5-alpha-L-arabinanase
-
-
endo-1,5-alpha-L-arabinanase
-
endo-1,5-alpha-L-arabinanase
-
-
endo-1,5-alpha-L-arabinanase
-
-
endo-1,5-alpha-L-arabinanase
Geobacillus thermodenitrificans TS-3
-
;
-
endo-1,5-alpha-L-arabinanase
-
-
endo-1,5-alpha-L-arabinanase
-
endo-1,5-alpha-L-arabinase
-
-
-
-
endo-1,5-alpha-L-arabinase
-
endo-1,5-alpha-L-arabinase
Paenibacillus polymyxa Z6
-
-
endo-1,5-alpha-L-arabinase A
-
-
endo-1,5-arabinase
-
endo-1,5-arabinase
Bacillus subtilis 168
-
-
endo-alpha-(1->5)-L-arabinanase
-
-
-
-
endo-alpha-1,5-arabanase
-
-
-
-
endo-alpha-1,5-L-arabinanase
-
endo-alpha-1,5-L-arabinanase
Bacillus subtilis 168T+
-
-
endo-alpha-arabinanase
-
-
endo-ara
-
-
endo-arabanase
-
-
-
-
endo-arabinanase
-
-
-
-
endo-arabinanase
Bacillus licheniformis DSM13
-
-
endo-arabinanase
-
-
endo-arabinanase
Botrytis cinerea IK2018
-
-
-
endo-arabinanase
Thermotoga thermarum
-
-
endo-arabinase
-
-
-
-
endo-arabinase
-
-
endo-arabinase
Penicillium chrysogenum 31B
-
-
endo-D-arabinase
-
-
endo-L-arabinanase
-
-
-
-
endoarabinanase
-
-
endoarabinanase
Chrysosporium lucknowense C1
-
-
-
endoarabinase
-
-
-
-
GH43 arabinanase
-
PPase-C
-
IFO 3134
protopectinase C
-
IFO 3134
protopectinase-C
-
IFO 3134
GH43 arabinanase
Bacillus subtilis 168T+
-
-
additional information
the enzyme belongs to the glycoside hydrolase family 43, GH43
additional information
Geobacillus stearothermophilus T-6
the enzyme belongs to the glycoside hydrolase family 43, GH43
-
additional information
-
the enzyme belongs to the glycoside hydrolase family 43, GH43
SplaateCAS_Registry_Number,Commentary
CAS REGISTRY NUMBER
COMMENTARY
75432-96-1
-
SplaateOrganism, Commentary,Literature, Sequence_Code,Sequence_db,Textmining
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild-type WG096
-
-
Manually annotated by BRENDA team
wild-type WG096 and cre mutant, carbon catabolite derepressed mutant
-
-
Manually annotated by BRENDA team
creA mutant, mutant relieved of carbon repression
-
-
Manually annotated by BRENDA team
wild-type N400 and mutant N572, lacks xylulose kinase activity
-
-
Manually annotated by BRENDA team
wild-type N402 and mutant N572, xylulose kinase negative mutant
-
-
Manually annotated by BRENDA team
Aspergillus niger N400
N400
-
-
Manually annotated by BRENDA team
Bacillus licheniformis DSM13
-
UniProt
Manually annotated by BRENDA team
F-11; IFO 3022
-
-
Manually annotated by BRENDA team
IFO 3022
-
-
Manually annotated by BRENDA team
IFO 3022; IFO 3134
-
-
Manually annotated by BRENDA team
IFO 3134
-
-
Manually annotated by BRENDA team
strain 168T+
UniProt
Manually annotated by BRENDA team
Bacillus subtilis 168
-
UniProt
Manually annotated by BRENDA team
Bacillus subtilis 168T+
strain 168T+
UniProt
Manually annotated by BRENDA team
Bacillus subtilis F-11
F-11
-
-
Manually annotated by BRENDA team
Botrytis cinerea IK2018
-
-
-
Manually annotated by BRENDA team
Chrysosporium lucknowense C1
-
-
-
Manually annotated by BRENDA team
Clostridium felsineum var. sikokianum
-
-
-
Manually annotated by BRENDA team
strain T-6, gene abnB
UniProt
Manually annotated by BRENDA team
Geobacillus stearothermophilus T-6
strain T-6, gene abnB
UniProt
Manually annotated by BRENDA team
strain TS-3
AB063312
GenBank
Manually annotated by BRENDA team
Geobacillus thermodenitrificans TS-3
strain TS-3
AB063312
GenBank
Manually annotated by BRENDA team
Geobacillus thermodenitrificans TS-3
strain TS-3
-
-
Manually annotated by BRENDA team
Paenibacillus polymyxa Z6
-
UniProt
Manually annotated by BRENDA team
Penicillium chrysogenum 31B
-
-
-
Manually annotated by BRENDA team
Penicillium chrysogenum 31B
-
UniProt
Manually annotated by BRENDA team
arabinanase A, exhibits endo- and exo-mode of action; subspecies cellulosa
-
-
Manually annotated by BRENDA team
Thermotoga thermarum
-
-
-
Manually annotated by BRENDA team
SplaateGeneral_Information, Organism, Commentary, Literature
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Botrytis cinerea IK2018
-
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
-
SplaateSubstrates,Products,id,Organism_Substrates,Commentary_Substrates, Literature_Substrates, Commentary_Products, Literature_Products,Reversibility
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1->5)-L-alphaarabinan + H2O
(1->5)-L-arabinooligosaccharides
show the reaction diagram
-
-
?
1,5-alpha-arabinan + H2O
?
show the reaction diagram
Chrysosporium lucknowense, Chrysosporium lucknowense C1
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
best substrate, endo mechanism
-
?
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
show the reaction diagram
-
best substrate, endo mechanism
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
best substrate, endo mechanism
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
show the reaction diagram
-
best substrate, endo mechanism
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
show the reaction diagram
-
best substrate: linear 1,5-alpha-L-haze arabinan
-
?
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
show the reaction diagram
-
i.e. debranched arabinan
-
?
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
show the reaction diagram
Geobacillus thermodenitrificans, Geobacillus thermodenitrificans TS-3
AB063312
i.e. debranched arabinan
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
-
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
-
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
IFO 3134, linear 1,5-alpha-L-arabinan
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
Bacillus subtilis F-11
-
-
-
?
1,5-alpha-L-arabinan + H2O
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + L-arabinose
show the reaction diagram
Bacillus subtilis F-11
-
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
show the reaction diagram
Bacillus subtilis F-11
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
Bacillus subtilis F-11
-
F-11 best substrate
-
?
1,5-alpha-L-arabinan + H2O
L-arabinan oligomers
show the reaction diagram
-
-
-
-
1,5-alpha-L-arabinan + H2O
L-arabinan oligomers
show the reaction diagram
-
-
-
ir
1,5-alpha-L-arabinan + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
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
show the reaction diagram
-
linear arabinan
main product
?
1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
-
-
-
-
-
1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
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
-
-
?
1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
debranched arabinan, best substrate
-
-
?
1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
Bacillus subtilis 168T+
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
-
-
?
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
-
-
?
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
Bacillus licheniformis DSM13
-
-
?
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside + L-arabinose
show the reaction diagram
-
-
-
?
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside + L-arabinose
show the reaction diagram
Bacillus subtilis 168
-
-
?
1,5-arabinan + H2O
L-arabinose + ?
show the reaction diagram
Geobacillus thermodenitrificans, Geobacillus thermodenitrificans TS-3
-
-
-
?
1,5-L-alpha-arabinoheptaose + H2O
1,5-L-alpha-arabinotriose + 1,5-L-alpha-arabinotetraose
show the reaction diagram
Chrysosporium lucknowense, Chrysosporium lucknowense C1
-
-
-
?
1,5-L-alpha-arabinopentaose + H2O
1,5-L-alpha-arabinotriose + 1,5-L-alpha-arabinobiose
show the reaction diagram
Chrysosporium lucknowense, Chrysosporium lucknowense C1
-
-
-
?
1,5-L-alpha-arabinotetraose + H2O
1,5-L-alpha-arabinobiose + 1,5-L-alpha-arabinobiose
show the reaction diagram
Chrysosporium lucknowense, Chrysosporium lucknowense C1
-
-
-
?
1,5-L-alpha-arabinotriose + H2O
L-arabinose + 1,5-L-alpha-arabinobiose
show the reaction diagram
Chrysosporium lucknowense, Chrysosporium lucknowense C1
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
mild hydrolysis: no significant degradation, exhaustive enzymatic hydrolysis: extremely low degradation, DP3
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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 + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara + alpha-L-arabinofuranose
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
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 + 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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
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 + H2O
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
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 + 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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
-
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
show the reaction diagram
-
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-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
show the reaction diagram
-
-
-
?
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + H2O
L-arabinose
show the reaction diagram
-
at very low rate, with high enzyme concentration
-
?
alpha-L-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + H2O
L-arabinose
show the reaction diagram
-
no or extremely low degradation, DP2
-
?
apple pectin + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis 168T+
-
-
-
?
arabinan + H2O
?
show the reaction diagram
Geobacillus thermodenitrificans, Geobacillus thermodenitrificans TS-3
AB063312
-
-
-
-
arabinogalactan + H2O
?
show the reaction diagram
-
-
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
-
very poor substrate
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
-
for optimal breakdown of potato arabinogalactan combined action of endo-arabinase and endo-galactanase is required
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
-
onion arabinogalactan: not a substrate
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
-
potato arabinogalactan
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
-
potato arabinogalactan
-
-
?
arabinogalactan + H2O
hexa-alpha-(1->5)-arabinofuranoside + ?
show the reaction diagram
-
-
-
?
carboxymethylarabinan + H2O
?
show the reaction diagram
-
-
-
-
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
-
-
-
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
-
-
-
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
-
F-11, primary cell wall polysaccharides
-
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
-
F-11, sycamore
-
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
-
F-11, sycamore
-
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
Bacillus subtilis F-11
-
F-11, primary cell wall polysaccharides, F-11, sycamore
-
?
cell wall polysaccharide + H2O
arabinose + galactose + rhamnose + fucose
show the reaction diagram
-
F-11, apple
F-11, 34.3% arabinose + 10% galactose + 2.6% rhamnose/fucose
?
CM-cellulose + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
debranched (1->5)-L-arabinan + H2O
L-arabinose
show the reaction diagram
-
under the optimum conditions, 16 g/l L-arabinose is obtained from 20 g/l debranched arabinan with a hydrolysis yield of 80%
-
?
debranched 1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
highest activity
-
-
?
debranched 1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
Botrytis cinerea, Botrytis cinerea IK2018
-
best substrate
-
-
?
debranched 1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
Bacillus licheniformis DSM13
highest activity
-
-
?
debranched arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
Thermotoga thermarum
-
-
-
?
debranched arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
highest activity
-
?
feruloylated oligosaccharide + H2O
ferulic acid + ?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
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
?
show the reaction diagram
-
very poor substrate
-
-
?
galactan + H2O
?
show the reaction diagram
-
potato galactan: poor substrate, citrus galactan: very poor substrate
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
-
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
-
main product: L-arabinotriose
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
linear arabinan
main product: L-arabinotriose
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
apple and sugar beet pulp
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
branched and partially debranched arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar beet pulp
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar beet pulp
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar beet pulp
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar beet pulp
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar beet pulp
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar beet pulp
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar beet pulp
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
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
show the reaction diagram
-
branched sugar beet arabinan containing alpha-1,3-arabinose side chains: not a substrate
main product: L-arabinotriose
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
sugar-beet arabinan in commercial apple juice concentrate, beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
debranched and branched sugar beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
linear and branched arabinan
end-product: low molecular weight oligomeric products
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
random hydrolysis of L-arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
random hydrolysis of L-arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
random hydrolysis of L-arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
random hydrolysis of L-arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Clostridium felsineum var. sikokianum
-
random hydrolysis of L-arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
-
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
show the reaction diagram
-
debranched arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Aspergillus niger N400
-
sugar beet pulp
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Bacillus subtilis F-11
-
sugar-beet arabinan in commercial apple juice concentrate, beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Bacillus subtilis F-11
-
beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Bacillus subtilis F-11
-
beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Bacillus subtilis F-11
-
branched and partially debranched arabinan, beet arabinan
-
?
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
Aspergillus niger N400(CBS 120-49)
-
sugar beet pulp
-
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
-
-
-
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
-
-
main product: L-arabinotriose
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
-
-
product formation
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
-
-
small oligomeric products
?
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
-
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
show the reaction diagram
-
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
?
linear 1,5-alpha-L-arabinan + H2O
L-arabinose + ?
show the reaction diagram
-
-
-
?
linear 1,5-alpha-L-arabinan + H2O
L-arabinose + ?
show the reaction diagram
-
-
-
?
linear 1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
-
-
-
-
?
linear 1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
-
-
-
?
linear 1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
Botrytis cinerea IK2018
-
-
-
-
?
linear 1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
Bacillus licheniformis DSM13
-
-
-
?
linear 1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
Paenibacillus polymyxa, Paenibacillus polymyxa Z6
-
-
?
linear arabinan + H2O
?
show the reaction diagram
Geobacillus stearothermophilus, Geobacillus stearothermophilus T-6
-
-
-
?
protopectin + H2O
pectin
show the reaction diagram
-
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
show the reaction diagram
-
IFO 3134, protopectin of sugar-beet and apple pulp
IFO 3134, soluble pectin
?
red debranched arabinan + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis 168T+
-
-
-
?
red debranched arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
Paenibacillus polymyxa, Paenibacillus polymyxa Z6
-
-
?
reduced arabinohexaose + H2O
arabinotriose + reduced arabinotriose
show the reaction diagram
-
the enzyme hydrolyzes a branched arabinohexaose with a double substituted arabinose at subsite-2
-
?
sugar beet arabinan + H2O
L-arabinose + ?
show the reaction diagram
-
-
-
?
sugar beet arabinan + H2O
?
show the reaction diagram
-
-
-
?
sugar beet arabinan + H2O
?
show the reaction diagram
-
-
-
?
sugar beet arabinan + H2O
?
show the reaction diagram
-
weak activity
-
-
?
sugar beet arabinan + H2O
?
show the reaction diagram
weak activity
-
-
?
sugar beet arabinan + H2O
?
show the reaction diagram
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
?
show the reaction diagram
Bacillus subtilis 168T+
-
-
-
?
sugar beet arabinan + H2O
?
show the reaction diagram
Botrytis cinerea IK2018
-
weak activity
-
-
?
sugar beet arabinan + H2O
?
show the reaction diagram
Bacillus licheniformis DSM13
weak activity
-
-
?
sugar beet arabinan + H2O
L oligo-alpha-(1->5)-L-arabinoside + L-arabinose
show the reaction diagram
-
-
-
?
sugar beet arabinan + H2O
L oligo-alpha-(1->5)-L-arabinoside + L-arabinose
show the reaction diagram
Bacillus subtilis 168
-
-
?
sugar beet arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
Thermotoga thermarum
-
-
-
?
sugar beet arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
Paenibacillus polymyxa, Paenibacillus polymyxa Z6
-
-
?
sugar beet arabinan arabinan + H2O
L-arabinose + ?
show the reaction diagram
-
-
conversion yield of 83% at pH 5.0 and 75C for 216 h
?
wheat arabinoxylan + H2O
?
show the reaction diagram
lowest activity
-
-
?
linear arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
Thermotoga thermarum
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
substrate specificity, overview
-
-
-
additional information
?
-
-
substrate specificity, overview
-
-
-
additional information
?
-
-
substrate binding site, action pattern, subsite mapping
-
-
-
additional information
?
-
-
no bi-substrate reactions such as condensation or transglycosylation
-
-
-
additional information
?
-
-
IFO 3022: potato disc macerating activity, able to loosen potato tissue
-
-
-
additional information
?
-
-
inactive on p-nitrophenyl-alpha-L-arabinofuranoside
-
-
-
additional information
?
-
-
inactive on p-nitrophenylarabinofuranoside, onion arabinogalactan, stractan, wheat arabinoxylan, oat spelts arabinoxylan, avicel, polygalacturonic acid
-
-
-
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
?
-
-
product specificity, overview
-
-
-
additional information
?
-
-
product specificity, overview
-
-
-
additional information
?
-
-
inactive on arabinobiitol
-
-
-
additional information
?
-
-
IFO 3134, inactive on polygalacturonic acid and soluble pectin
-
-
-
additional information
?
-
-
F-11, substrate specificity
-
-
-
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
?
-
-
inactive towards phenyl and p-nitrophenyl alpha-L-arabinofuranoside, arabinoxylan, arabinogalactan, and gum arabic
-
-
-
additional information
?
-
-
F-11, inactive on potato galactan
-
-
-
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
?
-
-
plays a role in degradation of plant tissues, macerating enzyme
-
-
-
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
?
-
shows no activity toward larchwood arabinogalactan, wheat arabinoxylan, and p-nitrophenyl-alpha-L-arabinofuranoside
-
-
-
additional information
?
-
-
the enzyme shows the ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides
-
-
-
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
?
-
the enzyme acts on branched arabinan (from sugar beet), but more slowly when compared to linear or debranched arabinan
-
-
-
additional information
?
-
does not hydrolyze birchwood xylan and 4-nitrophenyl-alpha-L-arabinofuranoside
-
-
-
additional information
?
-
no activity with 4-nitrophenyl-alpha-L-arabinofuranoside, beechwood xylan, wheat flour arabinoxylan, larch arabinogalactan, gum arabic, and soluble starch
-
-
-
additional information
?
-
-
the enzyme fails to cleave 1,5-alpha-arabinobiose, branched arabinan, arabinoxylan, arabinogalactan, xylan, and galactan
-
-
-
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
?
-
Thermotoga thermarum
-
there is no activity towards 1,4-beta-D-mannan, galactan, 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-alpha-L-arabinofuranoside
-
-
-
additional information
?
-
Paenibacillus polymyxa Z6
no activity with 4-nitrophenyl-alpha-L-arabinofuranoside, beechwood xylan, wheat flour arabinoxylan, larch arabinogalactan, gum arabic, and soluble starch
-
-
-
additional information
?
-
Bacillus subtilis 168T+
shows no activity toward larchwood arabinogalactan, wheat arabinoxylan, and p-nitrophenyl-alpha-L-arabinofuranoside
-
-
-
additional information
?
-
Botrytis cinerea IK2018
-
the enzyme fails to cleave 1,5-alpha-arabinobiose, branched arabinan, arabinoxylan, arabinogalactan, xylan, and galactan
-
-
-
additional information
?
-
Geobacillus thermodenitrificans TS-3
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
?
-
Bacillus subtilis F-11
-
F-11, inactive on potato galactan
-
-
-
additional information
?
-
Bacillus subtilis F-11
-
IFO 3022: potato disc macerating activity, able to loosen potato tissue, 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
?
-
Bacillus subtilis F-11
-
F-11, substrate specificity
-
-
-
additional information
?
-
Bacillus licheniformis DSM13
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
-
-
-
SplaateNatural_Substrates,Natural_Products,id,Organism_Substrates,Commentary_Substrates,Literature_Substrates,Commentary_Products,Literature_Products,Reversibility
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
-
-
-
-
-
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
Q65GB9, Q65L63
-
-
?
1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
Bacillus licheniformis DSM13
Q65GB9, Q65L63
-
-
?
arabinogalactan + H2O
hexa-alpha-(1->5)-arabinofuranoside + ?
show the reaction diagram
-
-
-
?
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
-
-
-
SplaateCofactor,Organism,Commentary,Literature,Filename
SplaateMetals_Ions,Organism,Commentary, Literature
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
(NH4)2HPO4
-
IFO 3134, stimulation of enzyme production and activity
(NH4)H2PO4
-
IFO 3134, stimulation of enzyme production and activity
Ba2+
Thermotoga thermarum
-
113% activity at 1 mM
BaCl2
-
IFO 3134, slight activation
Ca2+
-
isoform Arb43B possesses a cluster containing a calcium ion in the catalytic domain
Ca2+
Thermotoga thermarum
-
113% activity at 1 mM
Ca2+
-
the enzyme contains Ca2+ which also stimulates activity
CaCl2
-
IFO 3134, slight activation
CoCl2
-
IFO 3134, very slight activation
Hg2Cl2
-
IFO 3134, slight activation
K2HPO4
-
IFO 3134, stimulation of enzyme production and activity
KH2PO4
-
IFO 3134, stimulation of enzyme production and activity
MgCl2
-
IFO 3134, activation
Mn2+
Thermotoga thermarum
-
128% activity at 1 mM
Na2HPO4
-
IFO 3134, stimulation of enzyme production and activity
NaH2PO4
-
IFO 3134, stimulation of enzyme production and activity
Ni2+
-
stimulates activity
Mn2+
-
stimulates activity
additional information
-
F-11, no divalent cation requirement
additional information
-
IFO 3134, stimulation of enzyme production by several phosphates, but not by chloride, acetate or sulfate
additional information
not influenced by K+ and Mn2+
additional information
Thermotoga thermarum
-
not affected by Mg2+
SplaateInhibitors, Organism, Commentary, Literature,Filename
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
IFO 3134, slight inhibition
Ag2+
AB063312
complete inhibition at 1 mM
AgNO3
-
IFO 3134
Al3+
Thermotoga thermarum
-
complete inhibition at 1 mM
branched arabinofuranosides
-
-
-
Ca2+
about 40% residual activity at 5 mM
CdCl2
-
IFO 3134
CH3COO- NH4+
-
IFO 3134, complete inhibition of enzyme production
CH3COONa
-
IFO 3134, inhibition of enzyme production
Co2+
about 70% residual activity at 5 mM
Co2+
Thermotoga thermarum
-
82% residual activity at 1 mM
Cu2+
about 10% residual activity at 5 mM
Cu2+
Thermotoga thermarum
-
complete inhibition at 1 mM
EGTA
-
isoform Arb43B shows a drastic decrease in the activity of the enzyme in the presence of 1 mm EGTA
Fe2(SO4)3
-
IFO 3134
Fe2+
-
IFO 3022
Fe2+
about 60% residual activity at 5 mM
Fe3+
-
IFO 3022
Fe3+
about 55% residual activity at 5 mM
Hg2+
-
IFO 3022, completely
Hg2+
-
completely
Hg2+
-
IFO 3134, completely
Hg2+
AB063312
complete inhibition at 1 mM
HgCl2
-
completely
HgCl2
-
IFO 3134, completely
iodoacetamide
-
very slight inhibition
Mg2+
about 80% residual activity at 5 mM
MgSO4
-
very slight inhibition
Mn2+
-
IFO 3134, completely
NaN3
-
IFO 3134, slight inhibition
NaNO2
-
IFO 3134, strong inhibition
Ni2+
about 70% residual activity at 5 mM
Ni2+
Thermotoga thermarum
-
31% residual activity at 1 mM
o-phenanthroline
-
IFO 3134, slight inhibition
p-chloromercuribenzoate
-
IFO 3134, slight inhibition
PbCl2
-
IFO 3134
Sn2+
-
IFO 3134, strong inhibition
SnCl2
-
IFO 3134, strong inhibition
Tris
Thermotoga thermarum
-
41% residual activity at 0.05% (w/v)
Zn2+
about 40% residual activity at 5 mM
Zn2+
Thermotoga thermarum
-
14% residual activity at 1 mM
MnCl2
-
IFO 3134, completely
additional information
-
IFO 3022: no inhibition by L-arabonic-gamma-lactone, D- and L-galactonic-gamma-lactones
-
additional information
-
no inhibition by CaCl2, EDTA, L-arabono-gamma-lactone, L-arabinose, D-arabitol
-
additional information
-
IFO 3134, inhibition of enzyme production
-
additional information
-
-
-
additional information
AB063312
no inhibition by Ba2+, Mn2+ and Mg2+
-
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
-
SplaateActivating_Compound, Organism, Commentary, Literature,Filename
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
apple pulp
-
induction of endo-arabinase and activation
-
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
SDS
Thermotoga thermarum
-
111% activity at 0.1% SDS
sugar beet pulp
-
induction of endo-arabinase and activation
-
sugar beet pulp
-
induction of endo-arabinase and activation
-
Tween 60
Thermotoga thermarum
-
133% activity at 0.05% Tween 60
additional information
expression of abn2 is stimulated by arabinan and pectin, arabinose is not the natural inducer. EDTA does not affect the activity
-
SplaateKM_Value,KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.052
1,5-alpha-L-arabinan
-
CM-linear 1,5-alpha-L-arabinan
0.336
1,5-alpha-L-arabinan
-
CM-linear 1,5-alpha-L-arabinan
4.2
1,5-alpha-L-arabinan
-
-
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
-
-
0.0556
arabinogalactan
-
at pH 8.0 and 40C
9.3
L-arabinan
-
apple juice ultrafiltration retentate, UFR, arabinan, linearised
26
L-arabinan
-
apple juice ultrafiltration retentate, UFR, arabinan
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
0.1177
linear 1,5-alpha-L-arabinan
at 40C and pH 6.0
5.92
linear 1,5-alpha-L-arabinan
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic data and mechanism
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic data
-
additional information
additional information
-
kinetic data
-
additional information
additional information
AB063312
-
-
SplaateTurnover_Number, Turnover_Number_Maximum, Substrate,Organism,Commentary, Literature, Filename
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
50
1,5-alpha-L-arabinan
Caldicellulosiruptor saccharolyticus DSM 8903
A4XJR7
recombinant enzyme, pH 6.5, 75C
3.1
linear 1,5-alpha-L-arabinan
Bacillus subtilis
-
mutant H318A of isoform Arb43B, pH and temperature not specified in the publication
68.7
linear 1,5-alpha-L-arabinan
Paenibacillus polymyxa
V5LER1
wild type enzyme, at 40C and pH 6.0
99.7
linear 1,5-alpha-L-arabinan
Paenibacillus polymyxa
V5LER1
mutant enzyme H218D, at 40C and pH 6.0
191.6
linear 1,5-alpha-L-arabinan
Bacillus subtilis
-
wild type isoform Arb43B, pH and temperature not specified in the publication
349.3
linear arabinan
Thermotoga thermarum
-
at pH 6.5 and 75C
SplaateKCat_KM_Value,KCat_KM_Value_Maximum, Substrate,Organism, Commentary, Literature, Filename
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00004
linear 1,5-alpha-L-arabinan
Bacillus subtilis
-
mutant H318A of isoform Arb43B, pH and temperature not specified in the publication
13897
0.00172
linear 1,5-alpha-L-arabinan
Bacillus subtilis
-
wild type isoform Arb43B, pH and temperature not specified in the publication
13897
SplaateKI_Value,KI_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
SplaateIC50_Value,IC50_Value_Maximum, Inhibitor,Organism, Commentary, Literature, Filename
SplaateSpecific_Activity, Specific_Activity_Maximum, Organism ,Commentary, Literature
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 55C; sugar beet arabinan as substrate, in 50 mM sodium acetate buffer (pH 6.0) at 55C
0.36
-
apple juice ultrafiltration retentate, UFR, arabinan
1.2
-
best substrate: 1,5-alpha-L-arabinan
2.6
purified recombinant enzyme, substrate is sugar beet arabinan
5.8
-
IFO 3134
7.78
-
IFO 3022
12
purified recombinant enzyme, substrate 1,5-alpha-L-arabinan
14
-
substrate: branched sugar beet arabinan
26
-
using linear arabinan as substrate, pH and temperature not specified in the publication
42.5
Thermotoga thermarum
-
with sugar beet arabinan as substrate, at pH 6.5 and 75C
64.52
with linear 1,5-alpha-L-arabinan as substrate, in 50 mM sodium acetate buffer (pH 6.0) at 55C; with linear 1,5-alpha-L-arabinan as substrate, in 50 mM sodium acetate buffer (pH 6.0) at 55C
71.69
with debranched 1,5-alpha-L-arabinan as substrate, in 50 mM sodium acetate buffer (pH 6.0) at 55C; with debranched 1,5-alpha-L-arabinan as substrate, in 50 mM sodium acetate buffer (pH 6.0) at 55C
73.4
with linear linear 1,5-alpha-L-arabinan as substrate, at 40C, pH 6.0
81.1
-
substrate: debranched sugar beet arabinan
90.2
-
best substrate: linear 1,5-alpha-L-arabinan
116
-
sugar beet arabinan, at 37C, pH 6.6
152.1
purified protein, using L-arabinan as substrate, at pH 6.0 and 70C
199.7
Thermotoga thermarum
-
with debranched arabinan as substrate, at pH 6.5 and 75C
237.7
Thermotoga thermarum
-
with linear arabinan as substrate, at pH 6.5 and 75C
366
-
linear 1,5-alpha-L-arabinan, at 37C, pH 6.6
additional information
-
-
additional information
-
no detectable activity against larch wood arabinoxylan, wheat arabinoxylan or p-nitrophenyl-alpha-L-arabinofuranoside
SplaatepH_Optimum, pH_Optimum_Maximum, Organism, Commentary, Literature
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 5.5
-
-
4.6
-
maximum, pH optimum is quite broad
4.8
-
maximum
6
-
F-11; IFO 3022
6
-
IFO 3022
6
-
IFO 3134
6
-
IFO 3134, at 37C
6
-
mutant enzyme DELTAV2-W17
6
-
using sugar beet arabinan as substrate
6
-
free and Duolite A568-immobilized enzyme
6.5
-
using debranched arabinan as substrate
6.5
Thermotoga thermarum
-
-
8
-
IFO 3134, at 60C
SplaatepH_Range,pH_Range_Maximum, Organism,Commentary, Literature
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 - 9
-
IFO 3022
4 - 10
-
IFO 3134
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; 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
5.5 - 7.5
Thermotoga thermarum
-
about 35% activity at pH 5.5, about 50% activity at pH 7.5
SplaateTemperature_Optimum, Temperature_Optimum_Maximum, Organism, Commentary, Literature
SplaateTemperature_Range, Temperature_Range_Maximum, Organism, Commentary, Literature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 80
-
IFO 3134, activity between
30 - 70
about 45% activity at 30C, about 65% activity at 40C, about 85% activity at 50C, about 80% activity at 60C, and about 20% activity at 70C; about 45% activity at 30C, about 65% activity at 40C, about 85% activity at 50C, about 80% activity at 60C, and about 20% activity at 70C
30 - 80
the enzyme shows less than 40% activity at 30C, less than 50% activity at 40C, and more than 80% activity at 50V. Enzyme activity decreases rapidly when the reaction temperature is above 60C, and the enzyme loses most of ist activity at 80C
60 - 90
Thermotoga thermarum
-
about 50% activity at pH 60C, about 70% activity at pH 70C, about 95% activity at pH 80C, about 92% activity at pH 85C, about 20% activity at 90C
62 - 80
the enzyme shows relative activity ranging from 77% to 78% at temperatures of 62C and 80C, respectively
SplaatepI_Value,pI_Value_Maximum, Organism,Commentary, Literature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
AB063312
isoelectric focusing, pH gradient 3-10
4.9
-
calculated from amino acid sequence
9.2
calculated from amino acid sequence
9.4
-
isoelectric focusing
SplaateSource_Tissue, Organism, Commentary, Literature, Textmining
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Aspergillus niger N400, Aspergillus niger N400(CBS 120-49)
-
-
-
Manually annotated by BRENDA team
Bacillus subtilis F-11
-
F-11; F-11
-
Manually annotated by BRENDA team
SplaateLocalization, Organism, Commentary, id_go, Literature, Textmining
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Aspergillus niger N400, Aspergillus niger N400(CBS 120-49)
-
-
-
-
Manually annotated by BRENDA team
Bacillus subtilis F-11
-
F-11
-
-
Manually annotated by BRENDA team
SplaatePDB,PDB,PDB,Organism,Uniprot_ID
SplaateMolecular_Weight, Molecular_Weight_Maximum, Organism, Commentary, Literature
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
-
3134, gel filtration on Toyopearl HW-55S
171761
27000
gel filtration
713925
30000
-
IFO 3134, SDS-PAGE
171760, 171761
31000
-
SDS-PAGE
664988
32000
-
F-11, SDS-PAGE
171744, 171748
32500
-
calculated from nucleotide sequence
171762
33000
-
IFO 3022, SDS-PAGE
171744, 171746
33900
-
MALDI-TOF-MS
171753
34000
-
SDS-PAGE
171758
34000
-
-
171759
35000
-
SDS-PAGE
171743
35000
AB063312
SDS-PAGE
654260
35000
-
SDS-PAGE
655027, 663476
35280
-
calculated from amino acid sequence
655027
35710
-
IFO 3134, calculated from nucleotide sequence
171760
36000
-
F-11, gel filtration
171748
39440
-
calculated from nucleotide sequence
171758
40000
-
SDS-PAGE
171765
41000
-
gel filtration
171753
42500
-
SDS-PAGE
171753
43000
-
SDS-PAGE
171762, 171764, 171765
45000
-
SDS-PAGE
171750
52380
sequence analysis
698584
112000
recombinant His-tagged enzyme, gel filtration
707816
SplaateSubunits, Organism, Commentary, Literature
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 33000, mutant enzyme DELTAV2-W17, SDS-PAGE
?
x * 33000, SDS-PAGE; x * 33900, calculated from amino acid sequence
?
Thermotoga thermarum
-
x * 36000, SDS-PAGE
?
x * 35477, calculated from amino acid sequence
?
x * 30000, recombinant enzyme, SDS-PAGE; x * 30000, recombinant enzyme, SDS-PAGE; x * 36358, calculated from amino acid sequence; x * 36358, calculated from amino acid sequence
?
-
x * 45000, SDS-PAGE
?
Bacillus licheniformis DSM13
-
x * 30000, recombinant enzyme, SDS-PAGE; x * 30000, recombinant enzyme, SDS-PAGE; x * 36358, calculated from amino acid sequence; x * 36358, calculated from amino acid sequence
-
?
Geobacillus thermodenitrificans TS-3
-
x * 33000, mutant enzyme DELTAV2-W17, SDS-PAGE
-
?
Paenibacillus polymyxa Z6
-
x * 35477, calculated from amino acid sequence
-
dimer
2 * 56000, recombinant His-tagged enzyme, SDS-PAGE, 2 x 56268, sequence calculation
monomer
-
F-11, 1 * 32000, SDS-PAGE
monomer
-
IFO 3134, 1 * 30000, SDS-PAGE
monomer
1 * 31000, SDS-PAGE
monomer
1 * 49000, small angle X-ray scattering
monomer
Bacillus subtilis F-11
-
F-11, 1 * 32000, SDS-PAGE
-
monomer
Penicillium chrysogenum 31B
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1 * 31000, SDS-PAGE
-
additional information
structure modelling and analysis, overview
SplaatePosttranslational_Modification, Organism, Commentary, Literature
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
-
glycoprotein
-
O-linked glycosylation: approximately 10000 Da
additional information
no glycoprotein
additional information
Penicillium chrysogenum 31B
-
no glycoprotein
-
SplaateCommentary, Organism, Literature
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 vapour-diffusion
-
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
-
preliminary x-ray analysis; resolution limit of 3.5 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
-
SplaatepH_Stability,pH_Stability_Maximum, Organism, Commentary, Literature
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; the enzyme shows more than 60% activity at pH 5.0-11.0 after 1 h incubation
732332
3.5 - 8
-
85% activity retained between, 67 h at 25C
171753
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
5 - 9
-
IFO 3134, stable between at 50C: 30 min
171761
5.5 - 6.3
-
stable between
171750
6 - 11
AB063312
quite stable at 37C for 16 h
654260
6 - 9
-
the enzyme remains stable at pH 6.0-9.0 after 24 h incubation
732878
7 - 10
-
F-11, stable between
171745
9
-
F-11, most stable at
171745
SplaateTemperature_Stability,Temperature_Stability_Maximum, Organism, Commentary, Literature
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
the specific activity of the enzyme remains 54.1% of maximum at 5C
731976
40
-
long incubation times, 26.5 h, at 40C: 90% activity retained
171753
45
-
up to 45C: more than 95% activity retained for 3 h
171753
50
-
up to, full retention of activity, sharp drop in activity beyond 50C
171743
50
remains fully active after 30 min of preincubation at 50C. After preincubation at 60C, the residual activity is only 15%
698584
50
-
no obvious enzymatic activity decline is observed for enzyme incubated at 40C for 120 min. The enzyme retains the most of its initial enzyme activity at 50C for a 120 min incubation. However, the activity decreases rapidly following its incubation at 60C
732878
50 - 60
the enzyme maintains 100% of the initial activity by treatment it at 50C for 1 h, while approximately 70% of the activity is lost at 60C
713925
50 - 60
the half-life of the enzyme at 50, 55, and 60C are 280, 152, and 30 min, respectively; the half-life of the enzyme at 50, 55, and 60C are 280, 152, and 30 min, respectively
732332
60
-
IFO 3134, up to, retains more than 80% of activity after 10 min
171761
60
-
mutant enzyme DELTAV2-W17 loses 65% of its activity after 4 h, half-life: 2.5 h
665426
65
-
mutant enzyme DELTAV2-W17, 70% loss of activity after 5 min
665426
65
purified recombinant His-tagged enzyme, half-life is 2440 h
707816
70
-
stable for 30 min
655027
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
665426
70
purified recombinant His-tagged enzyme, half-life is 254 h
707816
70 - 80
-
the half-lives of the immobilized endoarabinanase at 70C, 75C, and 80C are 745, 290, and 64 h, respectively
732201
70 - 85
Thermotoga thermarum
-
the enzyme retains more than 95% of its initial activity at 70C for 1 h. After being incubated at 80C 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 85C after 10 min incubation
731545
75
AB063312
half-life: 4 h
654260
75
-
4 h half-life
663476
75
-
half-life of wild-type enzyme: 4 h
665426
75
purified recombinant His-tagged enzyme, half-life is 93 h
707816
90 - 95
the enzyme is fully heat-stable (up to 10 h) and retains activity at temperatures up to 90C. The enzyme loses its activity only after 90 min when incubated at 95C
714032
SplaateGeneral_Stability, Organism, Literature
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
IFO 3134, EDTA stabilizes during purification
-
IFO 3134, enzyme stable against protease secreted by the microorganism even during 2 days cultivation
-
SplaateOrganic_Solvent, Organism, Commentary, Literature
SplaateOxidation_Stability,Organism,Literature
SplaateStorage_Stability, Organism, Literature
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 10 mM sodium acetate or piperazine buffer, pH 5.0 dispensed in small tubes
-
-80C, 20 mM Na-phosphate buffer, pH 7.4, 50 mM NaCl, 10% glycerol
SplaateCommentary, Organism, Literature
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by fast protein liquid chromatography, FPLC
-
wild-type N400
-
Ni-NTA column chromatography; Ni-NTA column chromatography
by gel filtration, more than 95% pure
F-11; IFO 3022
-
His-Trap column chromatography
-
HisTrap column chromatography
-
Ni-NTA agarose affinity chromatography
-
wild-type and selenol-methionine-labelled protein purified on nickel column, more than 95% pure
-
His-Trap column chromatography, gel filtration
-
recombinant His-tagged enzyme 39fold from Escherichia coli by nickel affinity chromatography
DEAE Sepharose column chromatography, Sephacryl S-300 gel filtration, and Blue Sepharose affinity chromatography
-
recombinant wild-type and mutant enzymes
hydrophobic chromatography, anion-exchange chromatography, gel filtration chromatography
-
Ni-Sepharose column chromatography
CM-Toyopearl 650 M column chromatography, Ni Sepharose 6 column chromatography, butyl-Toyopearl column chromatography, and Superdex 75 gel filtration; CM-Toyopearl 650 M column chromatography, Ni Sepharose 6 column chromatography, butyl-Toyopearl column chromatography, and Superdex 75 gel filtration
Ni2+ His-tag column chromatography
recombinant arabinanase
-
Ni2+-chelating affinity column chromatography and Superdex 75 gel filtration
recombinant His-tagged enzyme from Escherichia coli
-
nickel affinity column chromatography
Thermotoga thermarum
-
SplaateCommentary, Organism, Literature
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNA clone, overexpression in Aspergillus niger and Aspergillus nidulans
-
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
Abn2 overexpressed in Escherichia coli BL21(DE3) pLysS harboring pZI39
expressed in Escherichia coli BL21(DE3) pLysS cells
-
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
-
expressed in Nicotiana benthamiana
-
expressed in Escherichia coli ER2566 cells
-
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli
gene abnB, expression of wild-type and mutant enzymes
expressed in Bacillus subtilis
-
expressed in Bacillus subtilis strain MI112
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expressed in Pichia pastoris strain GS115
expressed in Escherichia coli; hyperexpression in Escherichia coli
-
expressed in Escherichia coli BL21 cells
overexpression of His-tagged enzyme in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
Thermotoga thermarum
-
SplaateCommentary, Organism, Literature
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
Penicillium chrysogenum 31B
-
-
SplaateEngineering, Organism, Commentary, Literature
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D171A
-
the mutant of isoform Arb43B displays no measurable activity
D38A
-
the mutant of isoform Arb43B displays no measurable activity
E224A
-
the mutant of isoform Arb43B displays no measurable activity
H318A
-
the mutant of isoform Arb43B displays a drastic decrease in enzymatic activity
H318Q
-
enzymatic activity is completely lost in this mutant
D147A
site-directed mutagenesis, structure comparison with the wild-type enzyme
E201A
site-directed mutagenesis, structure comparison with the wild-type enzyme
D147A
Geobacillus stearothermophilus T-6
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
E201A
Geobacillus stearothermophilus T-6
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
DELTAV2-W17
-
deletion of the N-terminal amino acids causes thermal instability
DELTAV2-W17
Geobacillus thermodenitrificans TS-3
-
deletion of the N-terminal amino acids causes thermal instability
-
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
H218R
Paenibacillus polymyxa Z6
-
inactive
-
H48D
Paenibacillus polymyxa Z6
-
inactive
-
H48E
Paenibacillus polymyxa Z6
-
inactive
-
H48K
Paenibacillus polymyxa Z6
-
inactive
-
H48R
Paenibacillus polymyxa Z6
-
inactive
-
H318Q
-
inactive, contains Ni2+ instead of Ca2+
additional information
mutant strains IQB413 (DELTAabnA), IQB485 (DELTAabn2), and IQB486 (DELTAabnA DELTAabn2). Almost complete loss of activity in the DELTAabn2 DELTAabnA double mutant
H318Q
Bacillus subtilis 168
-
inactive, contains Ni2+ instead of Ca2+
-
additional information
Bacillus subtilis 168T+
-
mutant strains IQB413 (DELTAabnA), IQB485 (DELTAabn2), and IQB486 (DELTAabnA DELTAabn2). Almost complete loss of activity in the DELTAabn2 DELTAabnA double mutant
-
SplaateCommentary, Organism, Literature
SplaateApplication,Organism,Commentary,Literature
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
analysis
-
structural analysis of plant cell pectic polysaccharides and arabinans
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
-
-
analysis
-
useful in structural analysis of primary cell wall polysaccharides
analysis
-
useful for studies on structure of protopectin
nutrition
-
role in juice clarification
nutrition
-
useful for pectin extraction from citrus peel from fruit-juice industries and sugar-beet pulp from sugar factories
nutrition
-
useful for pectin production from sugar beet pulp
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
analysis
Bacillus subtilis F-11
-
useful in structural analysis of primary cell wall polysaccharides
-
nutrition
Bacillus subtilis F-11
-
role in juice clarification
-
nutrition
-
production of L-arabinose from plant arabinan at high temperatures
nutrition
Geobacillus thermodenitrificans TS-3
-
production of L-arabinose from plant arabinan at high temperatures
-
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