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Information on EC 3.2.1.99 - arabinan endo-1,5-alpha-L-arabinanase and Organism(s) Bacillus subtilis and UniProt Accession P42293
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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
-
debranched
-
arabinases
- arabinotriose
- arabino-oligosaccharides
- nutrition
-
magnetospheric
-
endo-galactanase
- l-arabitol
- analysis
- rhamnogalacturonans
- lipoarabinomannans
-
arabinose-containing
-
exo-acting
- thermodenitrificans
-
five-bladed
- p-nitrophenyl-alpha-l-arabinofuranoside
- cellvibrio
- biofuel production
- degradation
- synthesis
- industry
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
endo-arabinanase, endo-arabinase, endoarabinanase, arase, abn-ts, abns1, abnase, endo-1,5-alpha-l-arabinanase, arb43a, cedaase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
araban 5-alpha-L-arabinohydrolase
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arabinase, endo-1,5-alpha-L-
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endo-(1->5)-alpha-L-arabinanase
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endo-1,5-alpha-arabinanase
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endo-1,5-alpha-L-arabinanase
endo-1,5-alpha-L-arabinase
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endo-alpha-(1->5)-L-arabinanase
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endo-alpha-1,5-arabanase
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endo-arabanase
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endo-arabinanase
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endo-arabinase
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endo-L-arabinanase
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endoarabinase
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endo-1,5-alpha-L-arabinanase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
regulation, induction and carbon catabolite repression of endo-1,5-alpha-arabinanase
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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.
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-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
oligo-alpha-(1->5)-L-arabinoside + L-arabinose
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-
?
sugar beet arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside + L-arabinose
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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 + 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
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
?
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
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
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F-11 and IFO 3022: best substrate, endo mechanism
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-
?
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
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F-11 best substrate
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?
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
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IFO 3022, best substrate
IFO 3022
?
cell wall polysaccharide + H2O
L-arabinan
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F-11, primary cell wall polysaccharides
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?
L-arabinan + H2O
L-arabino-oligosaccharides
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branched and partially debranched arabinan
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?
L-arabinan + H2O
L-arabino-oligosaccharides
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sugar-beet arabinan in commercial apple juice concentrate
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?
L-arabinan + H2O
L-arabino-oligosaccharides
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random hydrolysis of L-arabinan
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?
L-arabinan + H2O
L-arabino-oligosaccharides
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random hydrolysis of L-arabinan
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?
protopectin + H2O
pectin
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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
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IFO 3134, protopectin of sugar-beet and apple pulp
IFO 3134, soluble pectin
?
additional information
?
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shows no activity toward larchwood arabinogalactan, wheat arabinoxylan, and p-nitrophenyl-alpha-L-arabinofuranoside
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?
additional information
?
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shows no activity toward larchwood arabinogalactan, wheat arabinoxylan, and p-nitrophenyl-alpha-L-arabinofuranoside
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?
additional information
?
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IFO 3022: potato disc macerating activity, able to loosen potato tissue
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?
additional information
?
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IFO 3022: potato disc macerating activity, able to loosen potato tissue
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?
additional information
?
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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
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?
additional information
?
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F-11: inactive on phenyl alpha-L-arabinofuranoside, p-nitrophenyl alpha-D-galactopyranoside, p-nitrophenyl beta-D-galactopyranoside, arabinoxylan, arabinogalactan and gum arabic
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?
additional information
?
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IFO 3134, inactive on polygalacturonic acid and soluble pectin
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?
additional information
?
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inactive towards phenyl and p-nitrophenyl alpha-L-arabinofuranoside, arabinoxylan, arabinogalactan, and gum arabic
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?
additional information
?
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plays a role in degradation of plant tissues, macerating enzyme
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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
additional information
?
-
-
plays a role in degradation of plant tissues, macerating enzyme
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
additional information
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
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
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
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additional information
-
IFO 3022: no inhibition by L-arabonic-gamma-lactone, D- and L-galactonic-gamma-lactones
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.1
linear 1,5-alpha-L-arabinan
mutant H318A of isoform Arb43B, pH and temperature not specified in the publication
191.6
linear 1,5-alpha-L-arabinan
wild type isoform Arb43B, pH and temperature not specified in the publication
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no detectable activity against larch wood arabinoxylan, wheat arabinoxylan or p-nitrophenyl-alpha-L-arabinofuranoside
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H318A
the mutant of isoform Arb43B displays a drastic decrease in enzymatic activity
H318Q
additional information
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
remains fully active after 30 min of preincubation at 50°C. After preincubation at 60°C, the residual activity is only 15%
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
IFO 3134, enzyme stable against protease secreted by the microorganism even during 2 days cultivation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and selenol-methionine-labelled protein purified on nickel column, more than 95% pure
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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
analysis
-
useful in structural analysis of primary cell wall polysaccharides
nutrition
-
useful for pectin extraction from citrus peel from fruit-juice industries and sugar-beet pulp from sugar factories
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Voragen, A.G.J.; Geerst, F.; Pilnik, W.
Hemi-cellulases in enzymic fruit processing
Util. Enzymes Technol. Aliment. , Symp. Int. (Dupuy, P. , ed. ), Tech. Doc. Lavoisier Paris
497-502
1982
Bacillus subtilis, Bacillus subtilis F-11
-
Kaji, A.
L-Arabinosidases
Adv. Carbohydr. Chem. Biochem.
42
383-394
1984
Bacillus subtilis, Bacillus subtilis F-11, Clostridium felsineum var. sikokianum
-
Kaji, A.; Saheki, T.
endo-Arabinanase from Bacillus subtilis F-11
Biochim. Biophys. Acta
410
354-360
1975
Bacillus subtilis, Bacillus subtilis F-11
Yoshihara, O.; Kaji, A.
An endo-1,5-alpha-L-arabinase, which can disintegrate potato tissue
Agric. Biol. Chem.
47
1935-1940
1983
Bacillus subtilis
-
Weinstein, L.; Albersheim, P.
Structure of plant cell walls. IX. Purification and partial characterization of a wall-degrading endo-arabanase and an arabinosidase from Bacillus subtilis
Plant Physiol.
63
425-432
1979
Bacillus subtilis, Bacillus subtilis F-11
Sakamoto, T.; Yamada, M.; Kawasaki, H.; Sakai, T.
Molecular cloning and nucleotide sequence of an endo-1,5-alpha-L-arabinase gene from Bacillus subtilis
Eur. J. Biochem.
245
708-714
1997
Bacillus subtilis
Sakai, T.; Sakamoto, T.
Purification and some properties of a protopectin-solubilizing enzyme that has potent activity on sugar beet protopectin
Agric. Biol. Chem.
54
879-889
1990
Bacillus subtilis
-
Raposo, M.P.; Inacio, J.M.; Mota, L.J.; de Sa-Nogueira, I.
Transcriptional regulation of genes encoding arabinan-degrading enzymes in Bacillus subtilis
J. Bacteriol.
186
1287-1296
2004
Bacillus subtilis
Leal, T.L.; de Sa-Nogueira I.
Purification, characterization and functional analysis of an endo-arabinanase (AbnA) from Bacillus subtilis
FEMS Microbiol. Lett.
241
41-48
2004
Bacillus subtilis
de Sanctis, D.; Bento, I.; Inacio, J.M.; Custodio, S.; de Sa-Nogueira, I.; Carrondo, M.A.
Overproduction, crystallization and preliminary X-ray characterization of Abn2, an endo-1,5-alpha-arabinanase from Bacillus subtilis
Acta Crystallogr. Sect. F
64
636-638
2008
Bacillus subtilis (P42293), Bacillus subtilis
Inacio, J.M.; de Sa-Nogueira, I.
Characterization of abn2 (yxiA), encoding a Bacillus subtilis GH43 arabinanase, Abn2, and its role in arabino-polysaccharide degradation
J. Bacteriol.
190
4272-4280
2008
Bacillus subtilis (P42293), Bacillus subtilis, Bacillus subtilis 168T+ (P42293)
de Sanctis, D.; Inacio, J.M.; Lindley, P.F.; de Sa-Nogueira, I.; Bento, I.
New evidence for the role of calcium in the glycosidase reaction of GH43 arabinanases
FEBS J.
277
4562-4574
2010
Bacillus subtilis (P42293)
McVey, C.E.; Ferreira, M.J.; Correia, B.; Lahiri, S.; de Sanctis, D.; Carrondo, M.A.; Lindley, P.F.; de Sa Nogueira, I.; Soares, C.M.; Bento, I.
The importance of the Abn2 calcium cluster in the endo-1,5-arabinanase activity from Bacillus subtilis
J. Biol. Inorg. Chem.
19
505-513
2014
Bacillus subtilis (P42293), Bacillus subtilis, Bacillus subtilis 168 (P42293)
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