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Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Streptomyces olivaceoviridis and UniProt Accession Q7SI98
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3.2.1.8 endo-1,4-beta-xylanaseSpecify your search results
Word Map
- 3.2.1.8
- xylans
- xylanases
- xylose
- arabinoxylans
- trichoderma
- xylooligosaccharides
- reesei
- xylotriose
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xylanolytic
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birchwood
- spelt
- cellulases
- straw
-
carbohydrate-binding
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lignocellulosic
- beta-xylosidase
- xylotetraose
- bran
-
hemicellulases
- lanuginosus
- thermomyces
- corncob
- arabinofuranosidase
- bagasse
- cellobiohydrolase
- alpha-l-arabinofuranosidase
- cellulomonas
-
saccharification
-
cellulose-binding
- avicel
-
thermoascus
- degradation
- agriculture
- cellulosome
- paper production
- glucuronoxylans
-
lignocellulolytic
- endo-1,4-beta-glucanase
- halodurans
- arabinan
- industry
- xylosidase
- biofuel production
-
breadmaking
- analysis
-
hemicellulolytic
- nutrition
- cellulolyticus
- longibrachiatum
-
taxi
- food industry
- synthesis
-
kraft
- biotechnology
-
biobleaching
-
cellulase-free
- neocallimastix
-
water-extractable
- cellulosa
-
dockerin
The taxonomic range for the selected organisms is: Streptomyces olivaceoviridis
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1--> 4)-beta-xylan 4-xylanohydrolase
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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-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-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 22
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xylanase, endo-1,4-
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XYLD
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XYLY
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additional information
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the enzyme belongs to the glycosyl hydrolase family 11, GH11
xylanase
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-xylan xylanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9025-57-4
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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
1,4-beta-D-xylan + H2O
additional information
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-
oat spelt xylan
xylotriose + xylotetraose are the main products from soluble oat spelt xylan, xylose is produced at very low levels
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00789
p-nitrophenyl-beta-D-xylobioside
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switching enzyme with azide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0523
p-nitrophenyl-beta-D-xylobioside
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switching enzyme with azide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activities of wild-type and mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme N-terminal structure analysis and homology modelling, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
switching enzyme with azide, by the hanging-drop vapor-diffusion method, at 1.7 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E128H
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inhibits the breakdown of the glycosyl-enzyme intermediate. Restoration of the breakdown activity of the mutant by adding exogenous nucleophiles, such as sodium azide, results in a mutant that acts as a switching enzyme with azide
G23A/G24P/S26T
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the mutation increases the enzyme's thermostability
T11Y/N12H/N13D/F15Y/F16F
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the mutation increases the enzyme's thermostability
T30E/N32G/S33P
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the mutation increases the enzyme's thermostability
V3A/I4V/T6S/Q8E
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the mutation increases the enzyme's thermostability
additional information
additional information
-
obtained switching mutant N127S-E128H, rate of hydrolysis is apparently zero in the absence of sodium azide, accumulates the glycosyl-enzyme intermediate, breakdown rate of glycosyl-enzyme intermediate is dramatically accelerated by two orders of magnitude in the presence of 300 mM sodium azide
additional information
-
substituting of Streptomyces olivaceovirdis SoxB 33 N-terminal amino acid residues with the corresponding residues of the thermophilic xylanase TfxA from Thermomonospora fusca strain ATCC 27730 significantly enhances the enzyme thermostability, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant SoxBs in Escherichia coli strain BL21 (DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaneko, S.; Kuno, A.; Muramatsu, M.; Iwamatsu, S.; Kusakabe, I.; Hayashi, K.
Purification and characterization of a family G/11 beta-xylanase from Streptomyces olivaceoviridis E-86
Biosci. Biotechnol. Biochem.
634
447-451
2000
Streptomyces olivaceoviridis, Streptomyces olivaceoviridis E-86
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)
Suzuki, R.; Fujimoto, Z.; Ito, S.; Kawahara, S.I.; Kaneko, S.; Taira, K.; Hasegawa, T.; Kuno, A.
Crystallographic snapshots of an entire reaction cycle for a retaining xylanase from Streptomyces olivaceoviridis E-86
J. Biochem.
146
61-70
2009
Streptomyces olivaceoviridis, Streptomyces olivaceoviridis E-86
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