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Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Neocallimastix patriciarum and UniProt Accession P29127

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Neocallimastix patriciarum
UNIPROT: P29127 not found.
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The taxonomic range for the selected organisms is: Neocallimastix patriciarum
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
endo-(1,4)-beta-xylanase
-
(1--> 4)-beta-xylan 4-xylanohydrolase
-
-
-
-
1,4-beta-D-xylan xylanohydrolase
-
-
-
-
1,4-beta-D-xylan xylanohydrolase 22
-
-
-
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1,4-beta-xylan xylanohydrolase
-
-
-
-
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
-
-
-
-
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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endo-beta-1,4-xylanase
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-
-
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endoxylanase
FIA-xylanase
-
-
-
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GH 11 xylanase
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ORF4
-
-
-
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TAXI
-
-
-
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X34
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-
-
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XYLA
-
-
-
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xylanase
Xylanase 22
-
-
-
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xylanase Xyl11A
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xylanase, endo-1,4-
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-
-
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XYLD
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-
-
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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
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-57-4
-
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
-
-
-
?
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside] + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-xylobioside + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-xylotrioside + H2O
?
show the reaction diagram
-
-
-
?
beechwood xylan + H2O
?
show the reaction diagram
161% of the activity with xyloheptaose
-
-
?
oat spelt xylan + H2O
?
show the reaction diagram
-
-
-
?
wheat arabinoxylan + H2O
?
show the reaction diagram
117% of the activity with xyloheptaose
-
-
?
xyloheptaose + H2O
?
show the reaction diagram
-
-
-
?
xylohexaose + H2O
?
show the reaction diagram
xylopentaose + H2O
?
show the reaction diagram
xylotetraose + H2O
?
show the reaction diagram
xylotriose + H2O
?
show the reaction diagram
-
-
-
?
arabinoxylan + H2O
?
show the reaction diagram
-
GH 10 enzyme produces smaller oligosaccharides than GH 11. GH 11 produces oligosaccharides with unsubstituted xylopyranose at the reducing- and non-reducing ends
-
-
?
beechwood xylan + H2O
xylooligosaccharides + ?
show the reaction diagram
-
-
-
?
oat spelt xylan + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.166
4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside]
pH 6.0, 50°C
15
4-nitrophenyl-beta-D-xylobioside
in 12 mM sodium citrate, 50 mM sodium phosphate buffer (pH 6.5)
2.1
4-nitrophenyl-beta-D-xylotrioside
in 12 mM sodium citrate, 50 mM sodium phosphate buffer (pH 6.5)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1983
toward oat spelt xylan
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
both wild-type and mutant N38Y/F52W/G56Y/G201L
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
mutant N38Y/F52W/G56Y/G201L
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
XYNA_NEOPA
607
0
66175
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
sequence analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 25827, mutant N38Y/F52W/G56Y/G201L, calculated, x * 25800, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme bound to ferulic acid-1,5-arabinofuranose-alpha-1,3-xylotriose, hanging drop vapour diffusion method, with 0.1 M cadmium chloride, 0.1 M sodium acetate (pH 4.6) and 30% (w/v) polyethylene glycol 400
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G201L
increase in melting temperature by 8.5 degrees
N38Y/F52W/G56Y/G201L
increase in melting temperature by 14 degrees
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
when pH is below 4.0 or above 7.0, less than 60% of the optimal activity is retained and the enzyme shows no activity at pH 9.0
695791
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 55
at temperatures below 30°C and above 55°C, enzyme activity is less than 50% of that at the optimal temperature
65
20 min, wild-type, 70% loss of activity, mutant N38Y/F52W/G56Y/G201L, about 10% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q10 anion exchange column chromatography
affinity-purified by formation of artificial oil bodies
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
DNA fragments of xynS20 genes subcloned into vector pOSP2. XynS20 expressed as a recombinant protein fused to the N-terminus of oleosin by a linker polypeptide, intein M, in Escherichia coli
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
enzyme coupled assay procedure, using substrate 4-nitrophenyl 4,6-O-(3-oxobutylidene)-beta-D-glucosyl-(1->4)-[(1->4)-beta-D-xylopentaoside] and release of 4-nitrophenol by beta-xylosidase
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Maslen, S.L.; Goubet, F.; Adam, A.; Dupree, P.; Stephens, E.
Structure elucidation of arabinoxylan isomers by normal phase HPLC-MALDI-TOF/TOF-MS/MS
Carbohydr. Res.
342
724-735
2007
Cellvibrio japonicus, Neocallimastix patriciarum
Manually annotated by BRENDA team
Vardakou, M.; Dumon, C.; Murray, J.W.; Christakopoulos, P.; Weiner, D.P.; Juge, N.; Lewis, R.J.; Gilbert, H.J.; Flint, J.E.
Understanding the structural basis for substrate and inhibitor recognition in eukaryotic GH11 xylanases
J. Mol. Biol.
375
1293-1305
2008
Neocallimastix patriciarum (P29127), Neocallimastix patriciarum
Manually annotated by BRENDA team
Liu, J.R.; Duan, C.H.; Zhao, X.; Tzen, J.T.; Cheng, K.J.; Pai, C.K.
Cloning of a rumen fungal xylanase gene and purification of the recombinant enzyme via artificial oil bodies
Appl. Microbiol. Biotechnol.
79
225-233
2008
Neocallimastix patriciarum (A8TGA1), Neocallimastix patriciarum
Manually annotated by BRENDA team
Bu, Y.; Cui, Y.; Peng, Y.; Hu, M.; Tian, Y.; Tao, Y.; Wu, B.
Engineering improved thermostability of the GH11 xylanase from Neocallimastix patriciarum via computational library design
Appl. Microbiol. Biotechnol.
102
3675-3685
2018
Neocallimastix patriciarum (Q9UV68), Neocallimastix patriciarum
Manually annotated by BRENDA team
Mangan, D.; Cornaggia, C.; Liadova, A.; McCormack, N.; Ivory, R.; McKie, V.A.; Ormerod, A.; McCleary, B.V.
Novel substrates for the automated and manual assay of endo-1,4-beta-xylanase
Carbohydr. Res.
445
14-22
2017
Cellvibrio mixtus (O68541), Neocallimastix patriciarum (P29127), Aspergillus niger (P55329)
Manually annotated by BRENDA team