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Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Thermotoga maritima and UniProt Accession Q9WXS5

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Thermotoga maritima
UNIPROT: Q9WXS5 not found.
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The taxonomic range for the selected organisms is: Thermotoga maritima
The enzyme appears in selected viruses and cellular organisms
Synonyms
endoxylanase, xylanase a, endo-xylanase, xyn11a, xyn10a, beta-xylanase, endo-1,4-beta-xylanase, gh11 xylanase, xylanase b, xynii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(1--> 4)-beta-xylan 4-xylanohydrolase
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-
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1,4-beta-D-xylan xylanohydrolase
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1,4-beta-D-xylan xylanohydrolase 22
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1,4-beta-D-xylan-xylanohydrolase
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1,4-beta-xylan xylanohydrolase
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34 kDa xylanase
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beta-1,4-D-xylanase
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beta-1,4-xylan xylanohydrolase
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beta-1,4-xylanase
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beta-D-xylanase
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beta-xylanase
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endo-(1,4)-beta-xylanase
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endo-(1--> 4)-beta-xylanase
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endo-1,4-beta-D-xylanase
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endo-1,4-beta-xylanase
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endo-1,4-xylanase
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endo-beta-1,4-xylanase
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endoxylanase
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FIA-xylanase
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ORF4
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TAXI
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X34
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XYLA
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xylanase
xylanase 10B
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Xylanase 22
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xylanase A
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xylanase B
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xylanase, endo-1,4-
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XYLD
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XYLY
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-xylan xylanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-57-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-beta-D-xylan + H2O
?
show the reaction diagram
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?
beta-1,4-xylan + H2O
?
show the reaction diagram
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-
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-
?
beta-1,4-xylan + H2O
xylobiose + xylotriose + ?
show the reaction diagram
-
from birchwood
the main degradation products
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?
carboxymethylcellulose + H2O
?
show the reaction diagram
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low activity, 1.4% activity compared to xylan
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-
?
gellan gum + H2O
?
show the reaction diagram
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low activity, 7.3% activity compared to xylan
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-
?
laminarin + H2O
?
show the reaction diagram
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low activity, 3.4% activity compared to xylan
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-
?
lichenan + H2O
?
show the reaction diagram
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low activity, 19% activity compared to xylan
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-
?
oat spelt xylan + H2O
?
show the reaction diagram
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-
-
-
?
xylan + H2O
?
show the reaction diagram
xylan + H2O
xylobiose + xylose + ?
show the reaction diagram
-
birchwood and soluble oat spelt xylan, endo-acting
main degradation products
-
?
xylooligosaccharides + H2O
xylobiose + xylose
show the reaction diagram
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predominantly xylobiose
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?
additional information
?
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substrate specificity, no activity with Avicel, filter paper, starch, amylopectin, pullulan, galactoglucomannan, or galactomannan
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-1,4-xylan + H2O
?
show the reaction diagram
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-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
89.7 - 106.5
xylan
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1022
-
substrate oat spelt xylan, purified recombinant enzyme
1099
-
substrate beechwood xylan, purified recombinant enzyme
12
-
substrate carboxymethylcellulose, purified recombinant enzyme
164
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substrate lichenan, purified recombinant enzyme
30
-
substrate laminarin, purified recombinant enzyme
64
-
substrate gellan gum, purified recombinant enzyme
867
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substrate birchwood xylan, purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
assay at
65
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recombinant hybrid mutant
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 90
-
activity range of mutant hybrid enzyme, profile, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
most XynA remains cell associated in the outer membrane
Manually annotated by BRENDA team
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XynB is detected in the periplasmic fraction and in the culture supernatant
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the N-terminal domain A2 is responsible for both the thermostability and substrate-binding capacity of XynA
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
119642
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x * 119642, calculated
120000
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XynA, SDS-PAGE
26000
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x * 26000, mutant hybrid enzyme, SDS-PAGE
40000
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XynB, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme folds into a (beta/alpha)8-barrel structure, and has characteristic clusters of aromatic residues together with a lack of exposed hydrophobic residues, crystallization data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with xylotriose and xylobiose
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purified recombinant enzyme, sitting drop vapour diffusion method, 40 mM zinc acetate, 20 mM MES, pH 6.0, 3% ethanol, X-ray diffraction structure determination and preliminary analysis at 2.5 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
improving the thermostability of Trichoderma reesei xylanase 2 by introducing the thermostabilizing domain A2 from Thermotoga maritima XynA into the N-terminal region of the Xyn2 protein
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
recombinant mutant hybrid enzyme, 30 min, over 85% activity remaining
90
-
stable below
additional information
-
features that account for the high thermostability of enzyme are clusters of aromatic residues together with a lack of exposed hydrophobic residues
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli, 12.5fold to homogeneity by Ni2+-chelate affinity chromatography
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recombinant protein
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
xylanase (XynB) and alpha-glucuronidase (AguA) from Thermotoga maritima are coproduced in Escherichia coli through dual-promoter and bicistronic constructs
expressed in Escherichia coli
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expression of the hybrid gene in Pichia pastoris under control of the inducible alcohol oxidase 1, AOX1, promoter using the secretion signal sequence from Saccharomyces cerevisiae, subcloning in Escherichia coli strain DH5alpha
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gene xynB, expression as His-tagged enzyme in Escherichia coli BL21
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
xylooligosaccharide derived from enzymatic hydrolysis of biopolymers is of considerable importance in preparing nutritional health oligosaccharides useful in food and pharmaceutical industries. To create added value products from hardwood xylan, xylanase (XynB) and alpha-glucuronidase (AguA) from Thermotoga maritima were co-produced in Escherichia coli through dual-promoter and bicistronic constructs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ihsanawati; Kumasaka, T.; Kaneko, T.; Morokuma, C.; Nakamura, S.; Tanaka, N.
Crystallization and preliminary X-ray studies of xylanase 10B from Thermotoga maritima
Acta Crystallogr. Sect. D
59
1659-1661
2003
Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Manually annotated by BRENDA team
Jiang, Z.Q.; Deng, W.; Zhu, Y.P.; Li, L.T.; Sheng, Y.J.; Hayashi, K.
The recombinant xylanase B of Thermotoga maritima is highly xylan specific and produces exclusively xylobiose from xylans, a unique character for industrial applications
J. Mol. Catal. B
27
207-213
2004
Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
Manually annotated by BRENDA team
Yoon, H.; Han, N.S.; Kim, C.H.
Expression of Thermotoga maritima endo-beta-1,4-xylanase gene in E. coli and characterization of the recombinant enzyme
Agric. Chem. Biotechnol.
47
157-160
2004
Thermotoga maritima
-
Manually annotated by BRENDA team
Ihsanawati, K.; Kumasaka, T.; Kaneko, T.; Morokuma, C.; Yatsunami, R.; Sato, T.; Nakamura, S.; Tanaka, N.
Structural basis of the substrate subsite and the highly thermal stability of xylanase 10B from Thermotoga maritima MSB8
Proteins
61
999-1009
2005
Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Manually annotated by BRENDA team
Berrin, J.G.; Juge, N.
Factors affecting xylanase functionality in the degradation of arabinoxylans
Biotechnol. Lett.
30
1139-150
2008
Bacillus sp. (in: Bacteria), Cellvibrio japonicus, Cellvibrio japonicus (Q59675), Acetivibrio thermocellus (O52780), Streptomyces lividans (P26514), Neocallimastix patriciarum (P29127), Paenibacillus polymyxa (P45796), Cellulomonas fimi (P54865), Aspergillus niger (P55329), Rhodothermus marinus (P96988), Aspergillus nidulans (Q00177), Thermotoga maritima (Q60037), Streptomyces olivaceoviridis (Q7SI98), Thermoclostridium stercorarium (Q8GJ44), Talaromyces funiculosus (Q9HFH0), Trichoderma viride (Q9UVF9)
Manually annotated by BRENDA team
Liebl, W.; Winterhalter, C.; Baumeister, W.; Armbrecht, M.; Valdez, M.
Xylanase attachment to the cell wall of the hyperthermophilic bacterium Thermotoga maritima
J. Bacteriol.
190
1350-1358
2008
Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Manually annotated by BRENDA team
Jun, H.; Bing, Y.; Keying, Z.; Xuemei, D.; Daiwen, C.
Thermostable carbohydrate binding module increases the thermostability and substrate-binding capacity of Trichoderma reesei xylanase 2
New Biotechnol.
26
53-59
2009
Thermotoga maritima, Trichoderma reesei, Trichoderma reesei RUT C-30
Manually annotated by BRENDA team
Zhou, T.; Xue, Y.; Ren, F.; Dong, Y.
Antioxidant activity of xylooligosaccharides prepared from Thermotoga maritima using recombinant enzyme cocktail of beta-xylanase and alpha-glucuronidase
J. Carbohydr. Chem.
37
210-224
2018
Thermotoga maritima (Q9WXS5), Thermotoga maritima ATCC 43589 (Q9WXS5)
-
Manually annotated by BRENDA team