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

EC NUMBER
COMMENTARY hide
3.2.1.99
-
RECOMMENDED NAME
GeneOntology No.
arabinan endo-1,5-alpha-L-arabinanase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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 hide
75432-96-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
N400
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
strain 168T+
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
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
strain T-6, gene abnB
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
arabinanase A, exhibits endo- and exo-mode of action; subspecies cellulosa
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
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
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 + L-arabinose
show the reaction diagram
1,5-alpha-L-arabinan + H2O
L-arabinan oligomers
show the reaction diagram
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
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 + L-arabinose
show the reaction diagram
1,5-arabinan + H2O
L-arabinose + ?
show the reaction diagram
1,5-L-alpha-arabinoheptaose + H2O
1,5-L-alpha-arabinotriose + 1,5-L-alpha-arabinotetraose
show the reaction diagram
1,5-L-alpha-arabinopentaose + H2O
1,5-L-alpha-arabinotriose + 1,5-L-alpha-arabinobiose
show the reaction diagram
1,5-L-alpha-arabinotetraose + H2O
1,5-L-alpha-arabinobiose + 1,5-L-alpha-arabinobiose
show the reaction diagram
1,5-L-alpha-arabinotriose + H2O
L-arabinose + 1,5-L-alpha-arabinobiose
show the reaction diagram
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 + 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 + 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-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 + 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 + 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 + 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-(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 + 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-(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-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-arabinopyranosyl-(1-5)-O-alpha-L-arabinopyranose + H2O
L-arabinose
show the reaction diagram
apple pectin + H2O
?
show the reaction diagram
arabinan + H2O
?
show the reaction diagram
arabinogalactan + H2O
?
show the reaction diagram
arabinogalactan + H2O
hexa-alpha-(1->5)-arabinofuranoside + ?
show the reaction diagram
-
-
-
-
?
carboxymethylarabinan + H2O
?
show the reaction diagram
-
-
-
-
?
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
?
cell wall polysaccharide + H2O
L-arabinan
show the reaction diagram
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
debranched arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
feruloylated oligosaccharide + H2O
ferulic acid + ?
show the reaction diagram
galactan + H2O
?
show the reaction diagram
L-arabinan + H2O
L-arabino-oligosaccharides
show the reaction diagram
L-arabino-oligosaccharide + H2O
L-arabino-oligosaccharide
show the reaction diagram
linear 1,5-alpha-L-arabinan + H2O
?
show the reaction diagram
linear 1,5-alpha-L-arabinan + H2O
L-arabinose + ?
show the reaction diagram
-
-
-
-
?
linear 1,5-alpha-L-arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
linear arabinan + H2O
?
show the reaction diagram
linear arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
-
-
-
-
?
protopectin + H2O
pectin
show the reaction diagram
red debranched arabinan + H2O
?
show the reaction diagram
red debranched arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
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
?
show the reaction diagram
sugar beet arabinan + H2O
L oligo-alpha-(1->5)-L-arabinoside + L-arabinose
show the reaction diagram
sugar beet arabinan + H2O
L-arabinose + ?
show the reaction diagram
-
-
-
-
?
sugar beet arabinan + H2O
oligo-alpha-(1->5)-L-arabinoside
show the reaction diagram
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
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
arabinogalactan + H2O
hexa-alpha-(1->5)-arabinofuranoside + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(NH4)2HPO4
-
IFO 3134, stimulation of enzyme production and activity
(NH4)H2PO4
-
IFO 3134, stimulation of enzyme production and activity
Ba2+
-
113% activity at 1 mM
BaCl2
-
IFO 3134, slight activation
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
Na2HPO4
-
IFO 3134, stimulation of enzyme production and activity
NaH2PO4
-
IFO 3134, stimulation of enzyme production and activity
Ni2+
-
stimulates activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
IFO 3134, slight inhibition
Ag2+
AB063312
complete inhibition at 1 mM
AgNO3
-
IFO 3134
Al3+
-
complete inhibition at 1 mM
branched arabinofuranosides
CdCl2
-
IFO 3134
CH3COO- NH4+
-
IFO 3134, complete inhibition of enzyme production
CH3COONa
-
IFO 3134, inhibition of enzyme production
Fe2(SO4)3
-
IFO 3134
iodoacetamide
-
very slight inhibition
Mg2+
about 80% residual activity at 5 mM
MgSO4
-
very slight inhibition
Mn2+
-
IFO 3134, completely
MnCl2
-
IFO 3134, completely
NaN3
-
IFO 3134, slight inhibition
NaNO2
-
IFO 3134, strong inhibition
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
-
41% residual activity at 0.05% (w/v)
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
apple pulp
-
induction of endo-arabinase and activation
-
L-arabinose
L-arabitol
SDS
-
111% activity at 0.1% SDS
sugar beet pulp
Tween 60
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.052 - 4.2
1,5-alpha-L-arabinan
0.388 - 0.592
alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara-(1-5)-O-alpha-L-Ara
0.0556
arabinogalactan
-
at pH 8.0 and 40C
9.3 - 26
L-arabinan
0.076 - 5.92
linear 1,5-alpha-L-arabinan
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
50
1,5-alpha-L-arabinan
Caldicellulosiruptor saccharolyticus DSM 8903
A4XJR7
recombinant enzyme, pH 6.5, 75C
3.1 - 191.6
linear 1,5-alpha-L-arabinan
349.3
linear arabinan
Pseudothermotoga thermarum
-
at pH 6.5 and 75C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00004 - 0.00172
linear 1,5-alpha-L-arabinan
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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
-
with debranched arabinan as substrate, at pH 6.5 and 75C
237.7
-
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 5.5
-
-
4.8
-
maximum
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
-
IFO 3022
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
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
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
IFO 3134, SDS-PAGE
31000
-
SDS-PAGE
32000
-
F-11, SDS-PAGE
32500
-
calculated from nucleotide sequence
33000
-
IFO 3022, SDS-PAGE
33900
-
MALDI-TOF-MS
35280
-
calculated from amino acid sequence
35710
-
IFO 3134, calculated from nucleotide sequence
36000
-
F-11, gel filtration
39440
-
calculated from nucleotide sequence
40000
-
SDS-PAGE
41000
-
gel filtration
42500
-
SDS-PAGE
52380
sequence analysis
112000
recombinant His-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 56000, recombinant His-tagged enzyme, SDS-PAGE, 2 x 56268, sequence calculation
monomer
additional information
structure modelling and analysis, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
additional information
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
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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 - 9
-
IFO 3134, stable between at 50C: 30 min
171761
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
5.5 - 6.3
-
stable between
171750
6 - 9
-
the enzyme remains stable at pH 6.0-9.0 after 24 h incubation
732878
6 - 11
AB063312
quite stable at 37C for 16 h
654260
7 - 10
-
F-11, stable between
171745
9
-
F-11, most stable at
171745
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
the specific activity of the enzyme remains 54.1% of maximum at 5C
40
-
long incubation times, 26.5 h, at 40C: 90% activity retained
45
-
up to 45C: more than 95% activity retained for 3 h
50
-
up to, full retention of activity, sharp drop in activity beyond 50C
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
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
70 - 80
-
the half-lives of the immobilized endoarabinanase at 70C, 75C, and 80C are 745, 290, and 64 h, respectively
70 - 85
-
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
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
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
-
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by fast protein liquid chromatography, FPLC
-
by gel filtration, more than 95% pure
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
DEAE Sepharose column chromatography, Sephacryl S-300 gel filtration, and Blue Sepharose affinity chromatography
-
F-11; IFO 3022
-
His-Trap column chromatography
-
His-Trap column chromatography, gel filtration
-
HisTrap column chromatography
-
hydrophobic chromatography, anion-exchange chromatography, gel filtration chromatography
-
Ni-NTA agarose affinity chromatography
-
Ni-NTA column chromatography; Ni-NTA column chromatography
Ni-Sepharose column chromatography
Ni2+ His-tag column chromatography
Ni2+-chelating affinity column chromatography and Superdex 75 gel filtration
nickel affinity column chromatography
-
recombinant arabinanase
-
recombinant His-tagged enzyme 39fold from Escherichia coli by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli
-
recombinant wild-type and mutant enzymes
wild-type and selenol-methionine-labelled protein purified on nickel column, more than 95% pure
-
wild-type N400
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Abn2 overexpressed in Escherichia coli BL21(DE3) pLysS harboring pZI39
cDNA clone, overexpression in Aspergillus niger and Aspergillus nidulans
-
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli
expressed in Bacillus subtilis
-
expressed in Bacillus subtilis strain MI112
-
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli ER2566 cells
-
expressed in Escherichia coli; hyperexpression in Escherichia coli
-
expressed in Nicotiana benthamiana
-
expressed in Pichia pastoris strain GS115
gene abnB, expression of wild-type and mutant enzymes
overexpression of His-tagged enzyme in Escherichia coli
-
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the gene encoding cold-adapted endo-arabinase Abnc is strongly induced by arabinose, arabinitol, and arabinan
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
D147A
site-directed mutagenesis, structure comparison with the wild-type enzyme
E201A
site-directed mutagenesis, structure comparison with the wild-type enzyme
D147A
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
E201A
-
site-directed mutagenesis, structure comparison with the wild-type enzyme
-
DELTAV2-W17
H218D
the mutant shows higher catalytic efficiency, kcat is improved about 45% versus that of the wild type enzyme
H218E
the mutant is active, but it does not change the enzymatic property obviously under acidic condition compared with the wild type enzyme
H218R
-
inactive
-
H48D
-
inactive
-
H48E
-
inactive
-
H48K
-
inactive
-
H48R
-
inactive
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
industry
-
endo-1,5-alpha-L-arabinanases belonging to glycoside hydrolase family 43 are of great industrial interest for use in food technology, organic synthesis and biofuel production owing to their ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides
nutrition
synthesis
-
applied to the refinement of cotton fiber, enzyme is able to release the cotton fiber coating, yielding product of high quality but with lower amounts of wastes
Show AA Sequence (562 entries)
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