Information on EC 3.2.1.32 - endo-1,3-beta-xylanase

New: Word Map on EC 3.2.1.32
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
3.2.1.32
-
RECOMMENDED NAME
GeneOntology No.
endo-1,3-beta-xylanase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
random endohydrolysis of (1->3)-beta-D-glycosidic linkages in (1->3)-beta-D-xylans
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(1,3)-beta-D-xylan degradation
-
-
d-xylose degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
3-beta-D-xylan xylanohydrolase
This enzyme is found mostly in marine bacteria, which break down the beta(1,3)-xylan found in the cell wall of some green and red algae. The enzyme produces mainly xylobiose, xylotriose and xylotetraose.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-55-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
A-07
-
-
Manually annotated by BRENDA team
No. C-59-2
-
-
Manually annotated by BRENDA team
Bacillus sp. No. C-59-2
No. C-59-2
-
-
Manually annotated by BRENDA team
PT-5
-
-
Manually annotated by BRENDA team
PT-5
-
-
Manually annotated by BRENDA team
gene xyl4
UniProt
Manually annotated by BRENDA team
strain AX4
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl 3-O-(3-O-methyl-etab-D-xylopyranosyl)-beta-D-xylopyranoside + H2O
?
show the reaction diagram
-
-
-
?
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl 3-O-beta-D-xylopyranosyl-beta-D-xylopyranoside + H2O
?
show the reaction diagram
-
-
-
?
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranoside + H2O
beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranose + 4-(trifluoromehtyl)umbelliferone
show the reaction diagram
-
-
-
?
beta-1,3-xylan + H2O
?
show the reaction diagram
beta-1,3-xylan + H2O
beta-1,3-D-xylobiose
show the reaction diagram
beta-1,3-xylan + H2O
beta-1,3-xylobiose + beta-1,3-xylotriose + ?
show the reaction diagram
beta-1,3-xylan + H2O
D-xylose + xylooligosaccharides
show the reaction diagram
-
-
-
?
beta-1,3-xylan + H2O
disaccharides + trisaccharides + tetrasaccharides
show the reaction diagram
-
-
disaccharides, trisaccharides and tetrasaccharides are the major products, whereas the monosaccharides, pentasaccharides and oligosaccharides with more than five xylose units are produces at small quantities
-
?
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
-
?
glycol beta-1,3-xylan + H2O
?
show the reaction diagram
glycol-beta-1,3-xylan + H2O
xylose + ?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
rhodymenan + H2O
beta-1,4-xylotriose + beta-1,4-linked xylooligosaccharides
show the reaction diagram
xylan (birchwood) + H2O
xylotetraose + ?
show the reaction diagram
-
-
xylotetraose is main product of xylan degradation
-
?
xylan (larchwood) + H2O
xylotetraose + ?
show the reaction diagram
-
-
xylotetraose is main product of xylan degradation
-
?
xylan (oat spelts) + H2O
xylotetraose + ?
show the reaction diagram
-
-
xylotetraose is main product of xylan degradation
-
?
xylopentaose + H2O
xylose + ?
show the reaction diagram
-
-
-
-
?
xylopentaose + H2O
xylose + xylotetraose + xylobiose + xylotriose
show the reaction diagram
xylotetraose + H2O
xylose + ?
show the reaction diagram
-
-
-
-
?
xylotetraose + H2O
xylose + xylotriose + xylobiose
show the reaction diagram
xylotriose + H2O
xylose + xylobiose
show the reaction diagram
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
beta-1,3-xylan + H2O
?
show the reaction diagram
beta-1,3-xylan + H2O
beta-1,3-xylobiose + beta-1,3-xylotriose + ?
show the reaction diagram
beta-1,3-xylan + H2O
xylose + xylooligosaccharides
show the reaction diagram
D5MP61
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activates
Mg2+
-
activates
NaCl
both the enzyme and the binding activities for insoluble beta-1,3-xylan but not soluble glycol-beta-1,3-xylan, are enhanced by NaCl
additional information
Ca2+, Mg2+, and Na+ have no significant effects on enzyme activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3R,4R)-4-hydroxy-3-[beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranosyloxy]-piperidine
competitive
-
(3R,4R)-4-hydroxy-[beta-D-xylopyranosyloxy]-piperidine
competitive
-
2,4-dinitrophenyl-beta-D-xylopyranosyl-(1->)-beta-D-xylopyranosyl-(1->3)2-deoxy-2-fluoro-beta-D-xylopyranoside
-
-
Ag2+
-
-
Cd2+
-
-
dithiothreitol
-
-
Fe2+
complete inhibition at 1 mM
N-bromosuccinimide
Ni2+
45-55% inhibition at 1 mM
Pb(CH3COO)2
-
1 mM, strong
phenyl 1-thio-beta-D-xylopyranoside
-
-
phenyl 4-O-beta-D-xylopyranosyl-1-thio-beta-D-xylopyranoside
-
-
phenyl beta-D-xylopyranosyl-(1->3)-1-thio-beta-D-xylopyranoside
-
-
additional information
dithiothreitol, and EDTA have no significant effects on enzyme activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
71
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl 3-O-(3-O-methyl-etab-D-xylopyranosyl)-beta-D-xylopyranoside
at pH 7.5 and 37C
1.7
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl 3-O-beta-D-xylopyranosyl-beta-D-xylopyranoside
at pH 7.5 and 37C
0.0038
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranoside
at pH 7.5 and 37C
0.75
xylopentaose
-
pH 7.5, 37C
0.74
xylotetraose
-
pH 7.5, 37C
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl 3-O-(3-O-methyl-etab-D-xylopyranosyl)-beta-D-xylopyranoside
Vibrio sp.
D5MP61
at pH 7.5 and 37C
1.9
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl 3-O-beta-D-xylopyranosyl-beta-D-xylopyranoside
Vibrio sp.
D5MP61
at pH 7.5 and 37C
0.89
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranoside
Vibrio sp.
D5MP61
at pH 7.5 and 37C
588.2
beta-1,3-xylan
Thermotoga neapolitana
B9K760
at pH 6.5 and 85C
322.6
glycol beta-1,3-xylan
Thermotoga neapolitana
B9K760
at pH 6.5 and 85C
14000
xylopentaose
Vibrio sp.
-
pH 7.5, 37C
350
xylotetraose
Vibrio sp.
-
pH 7.5, 37C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl 3-O-(3-O-methyl-etab-D-xylopyranosyl)-beta-D-xylopyranoside
Vibrio sp.
D5MP61
at pH 7.5 and 37C
197806
1.1
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl 3-O-beta-D-xylopyranosyl-beta-D-xylopyranoside
Vibrio sp.
D5MP61
at pH 7.5 and 37C
197805
230
2-oxo-4-(trifluoromethyl)-2H-chromen-7-yl beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranoside
Vibrio sp.
D5MP61
at pH 7.5 and 37C
197807
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
(3R,4R)-4-hydroxy-3-[beta-D-xylopyranosyl-(1->3)-beta-D-xylopyranosyloxy]-piperidine
at pH 7.5 and 37C
-
0.0031
(3R,4R)-4-hydroxy-[beta-D-xylopyranosyloxy]-piperidine
at pH 7.5 and 37C
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
-
-
6.4
-
enzyme form EF-3 and EF-5
8.5
-
enzyme form EF-4
9.3
-
enzyme form EF-2
9.9
-
-
13.3
-
enzyme form EF-6
13.6
-
-
15.2
-
enzyme form EF-1
207
-
xylan (oat spelts), pH 6.0, 30C
225
-
xylan (birchwood), pH 6.0, 30C
226
-
laminarin, pH 6.0, 30C
253
-
xylan (larchwood), pH 6.0, 30C
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
enzyme form EF-4
4.5
-
enzyme forms EF-5 and EF-6
5
-
enzyme forms EF-1 and EF-3
5.5
-
enzyme form EF-2
6 - 8
-
-
6 - 6.5
-
-
6 - 7.5
-
-
7 - 7.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
about 50% of maximal activity at pH 4.0 and at pH 10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
enzyme form EF-2
50
-
enzyme form EF-3 and EF-6
55
-
enzyme form EF-1
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 70
-
about 20% of maximal activity at 30C and at 70C
37 - 60
-
37C: optimum, 60C: does not hydrolyze beta-1,3-xylan above 60C at pH 7.5
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 4.7
-
or higher, enzyme Xyl I
5
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
-
gel filtration
53000
-
gel filtration
340000
-
PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
multimer
-
x * 20000, SDS-PAGE, x * 20000-24000, gel filtration
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure of recombinant carbohydrate-binding module of beta-1,3-xylanase is determined at a resolution of 1.25 A
-
to 1.8 A resolution, space group P21
-
sitting-drop and hanging-drop vapour-diffusion method, crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 51.6 A, b = 75.8 A, c = 82.0 A. X-ray diffraction data are collected to 1.44 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 6
-
30C, 1 h, stable
136244
3 - 10
the enzyme remains stable at pH 3.0-10.0 after incubation at 4C for 20 h
729069
4
-
4C, 24 h, 35% loss of activity
136250
4.5 - 10
-
4C, 20 h, stable
136243
5 - 9
-
50C, 10 min, stable
136246
5 - 8
-
4C, 20 h, stable
136251
5.5 - 8
-
4C, 20 h, stable
136249
6 - 10
-
4C, 24 h, enzyme retains 90-100% of activity
136250
7 - 7.5
-
60C, 10 min, stable
136246
8
-
30C, 1 h, almost all activity is lost
136244
12
-
4C, 24 h, retains 70% of its activity
136250
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
stable below
55
-
pH 6.0, 15 min, complete loss of activity
80 - 85
the enzyme activity half-life is 23.9 h at 85C and retains over 80% of initial activity at 80C for 24 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, stable for more than 3 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
6 different enzyme forms: EF-1, EF-2, EF-3, EF-4, EF-5 and EF-6
-
HisTrap HP column chromatography and HiTrap Q column chromatography
nickel affinity column chromatography and Superdex 200 gel filtration
recombinant
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL2(DE3) by nickel affinity and beta-1,3-xylan affinity chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a fusion protein with tandem repeats of the N-terminal domain of Protein S from Myxocuccus xanthus in Escherichia coli BL21(DE3) cells. ArgHCl efficiently solubilizes the fusion protein
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DELTADE3)pLysS cells
-
expression in Escherichia coli
expression in Escherichia coli DH5alpha
-
gene xyl4, DNA and amino acid sequence determination and comparison, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
wild-type and mutant enzymes are expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E126Q/E238Q
inactive
E126Q
-
inactive
-
E126Q/E238Q
-
inactive
-
E238Q
-
inactive
-
E138D
-
activity is extremely low
E138Q
-
inactive mutant
E234D
-
activity is extremely low
E234Q
-
inactive mutant
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis