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Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Talaromyces funiculosus and UniProt Accession Q9HFH0
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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
-
xylanolytic
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birchwood
- spelt
- cellulases
- straw
-
carbohydrate-binding
-
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: Talaromyces funiculosus
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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-
-
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1,4-beta-D-xylan xylanohydrolase
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-
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1,4-beta-D-xylan xylanohydrolase 22
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1,4-beta-xylan xylanohydrolase
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-
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34 kDa xylanase
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-
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beta-1,4-D-xylanase
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-
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beta-1,4-xylan xylanohydrolase
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-
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beta-1,4-xylanase
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-
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beta-D-xylanase
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-
-
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beta-xylanase
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-
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endo-(1--> 4)-beta-xylanase
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-
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endo-1,4-beta-D-xylanase
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-
-
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endo-1,4-beta-xylanase
endo-1,4-xylanase
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-
-
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endo-beta-1,4-xylanase
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-
-
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endoxylanase
FIA-xylanase
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-
-
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ORF4
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-
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TAXI
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-
-
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X34
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-
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XYLA
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-
-
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xylanase
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-
-
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Xylanase 22
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-
-
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xylanase, endo-1,4-
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XYLD
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XYLY
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endo-1,4-beta-xylanase
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endoxylanase
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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
wheat soluble arabinoxylan + H2O
xylotriose + xylobiose
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predominant production of xylotriose and xylobiose as end products
-
?
xylohexaose + H2O
2 xylotriose
rapid cleavage
xylohexaose is cleaved initially to produce mainly xylotriose and a small amount of xylobiose and xylotetraose
-
?
xylopentaose + H2O
xylobiose + xylotriose
rapid cleavage
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-
?
arabinoxylan + H2O
?
low to high viscosity arabinoxylans, and water-extractable wheat arabinoxylans with different ratio arabinose:xylose, overview
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-
?
additional information
?
-
no detectable activity on xylobiose
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-
?
additional information
?
-
the catalytic efficiency increases slightly with increasing their chain length with a small difference of the XynD catalytic efficiency against the different xylooligosaccharides
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-
?
additional information
?
-
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the catalytic efficiency increases slightly with increasing their chain length with a small difference of the XynD catalytic efficiency against the different xylooligosaccharides
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TAXI-I
endoxylanase inhibitor protein I, strong, competitive
-
additional information
not inhibitory: endoxylanase inhibitor protein TAXI-II
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additional information
-
not inhibitory: endoxylanase inhibitor protein TAXI-II
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
997
birchwood xylan
apparent value for the recombinant enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115.9
purified recombinant enzyme, substrate high viscosity arabinoxylan, pH 5.0, 70°C
50.4
purified recombinant enzyme, substrate birchwood xylan, pH 5.0, 70°C
additional information
additional information
substrate specificity with different arabinoxylans, overview
additional information
-
substrate specificity with different arabinoxylans, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6.5
displays over 50% activity in the pH range of 4.5 to 6.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
XynD possesses four catalytic subsites with a high energy of interaction with the substrate and a fifth subsite with a small energy of interaction
additional information
-
XynD possesses four catalytic subsites with a high energy of interaction with the substrate and a fifth subsite with a small energy of interaction
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). XYNC_TALFU
223
0
24045
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25902
x * 43000, SDS-PAGE, x * 25902, calculated, x * 29949-34912, ESI-MS
41540
x * 64000, SDS-PAGE, x * 46000, about, deglycoylated enzyme, mass spectrometry, x * 41540, sequence calculation
43000
x * 43000, SDS-PAGE, x * 25902, calculated, x * 29949-34912, ESI-MS
46000
x * 64000, SDS-PAGE, x * 46000, about, deglycoylated enzyme, mass spectrometry, x * 41540, sequence calculation
64000
x * 64000, SDS-PAGE, x * 46000, about, deglycoylated enzyme, mass spectrometry, x * 41540, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 43000, SDS-PAGE, x * 25902, calculated, x * 29949-34912, ESI-MS
?
x * 64000, SDS-PAGE, x * 46000, about, deglycoylated enzyme, mass spectrometry, x * 41540, sequence calculation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
sequence contains no putative N-glycosylation site
additional information
-
sequence contains no putative N-glycosylation site
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
stable at 30°C for 60 min, with more than 95% of the activity remaining
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme is purified via glutathione-agarose beads, native enzyme is purified via Sephacryl S-200 gel filtration
recombinant XynD 1.9fold from Pichia pastoris strain X33 by ultrafiltration and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (pLys) cells as glutathione S-transferase fusion protein
gene xynD, DNA and amino acid sequence determination and analysis, expression in Pichia pastoris strain X33
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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increasingly used in a number of biotechnological processes, including bread-making, gluten-starch separation, improving nutritional properties of animal feed, and the bleaching of cellulose pulp in paper manufacturing
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brutus, A.; Villard, C.; Durand, A.; Tahir, T.; Furniss, C.; Puigserver, A.; Juge, N.; Giardina, T.
The inhibition specificity of recombinant Penicillium funiculosum xylanase B towards wheat proteinaceous inhibitors
Biochim. Biophys. Acta
1701
121-128
2004
Talaromyces funiculosus (Q8J0K5), Talaromyces funiculosus
Berrin, J.G.; Ajandouz, e.l.H.; Georis, J.; Arnaut, F.; Juge, N.
Substrate and product hydrolysis specificity in family 11 glycoside hydrolases: an analysis of Penicillium funiculosum and Penicillium griseofulvum xylanases
Appl. Microbiol. Biotechnol.
74
1001-1010
2007
Penicillium griseofulvum, Talaromyces funiculosus (Q9HFH0)
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)
Belien, T.; Van Campenhout, S.; Robben, J.; Volckaert, G.
Microbial endoxylanases: effective weapons to breach the plant cell-wall barrier or, rather, triggers of plant defense systems?
Mol. Plant Microbe Interact.
19
1072-1081
2006
Aspergillus nidulans, Talaromyces funiculosus, Bipolaris sorokiniana (O13447), Fusarium oxysporum (O59938), Claviceps purpurea (O74716), Ascochyta pisi (Q00263), Pyricularia grisea (Q01176), Bipolaris zeicola (Q06562), Botrytis cinerea (Q2LMP0), Dickeya chrysanthemi (Q46961), Fusarium graminearum (Q7ZA57), Xanthomonas oryzae (Q9AM28)
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