Any feedback?
Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Niallia circulans and UniProt Accession P09850
for references in articles please use BRENDA:EC3.2.1.8Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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
-
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: Niallia circulans
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
-
-
-
-
1,4-beta-D-xylan xylanohydrolase
-
-
-
-
1,4-beta-D-xylan xylanohydrolase 22
-
-
-
-
1,4-beta-xylan xylanohydrolase
34 kDa xylanase
-
-
-
-
beta-1,4-D-xylanase
-
-
-
-
beta-1,4-xylan xylanohydrolase
-
-
-
-
beta-1,4-xylanase
-
-
-
-
beta-D-xylanase
-
-
-
-
beta-xylanase
-
-
-
-
endo-(1--> 4)-beta-xylanase
-
-
-
-
endo-1,4-beta-D-xylanase
-
-
-
-
endo-1,4-beta-xylanase
-
-
-
-
endo-1,4-xylanase
-
-
-
-
endo-beta-1,4-xylanase
-
-
-
-
endoxylanase
-
-
-
-
FIA-xylanase
-
-
-
-
ORF4
-
-
-
-
TAXI
-
-
-
-
X34
-
-
-
-
XYLA
-
-
-
-
xylanase
Xylanase 22
-
-
-
-
xylanase, endo-1,4-
-
-
-
-
XYLD
-
-
-
-
XYLY
-
-
-
-
1,4-beta-xylan xylanohydrolase
-
-
-
-
xylanase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
the catalytic residues are two conserved Glu residues, which are located opposite to each other in an open active site cleft. The catalytic mechanism resembles that of lysozyme. The role of one glutamate is to act as an acid/base catalyst whereas the other is a nucleophile and stabilizes the reaction intermediate
-
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-xylan xylanohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9025-57-4
-
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
additional information
?
-
the proximal sugar-ring of the substrate distorts from 4C1 chair to 2,5B boat conformation. Key role of Tyr69 in stabilizing the boat in preference to the 4C1 chair conformation
-
-
?
1,4-beta-D-xylan + H2O
additional information
-
-
-
xylose + xylobiose + xylotriose + xylotetraose are products formed by endo-beta-D-xylanase A. Xylobiose, xylotriose + xylotetraose are formed by endo-beta-D-xylanase B
?
NATURAL SUBSTRATE
NATURAL 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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-dinitrophenyl 2-deoxy-2-fluoro-beta-D-xylobioside
2,4-dinitrophenolate is released, due to covalent inactivation of the active enzyme, used for active site titrations
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.4
2,5-dinitrophenyl-beta-D-xylobioside
recombinant wild-type enzyme, pH 7.2, 22°C
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics of recombinant wild-type and mutant enzymes, overview
-
additional information
additional information
-
Michaelis-Menten kinetics of recombinant wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
34
2,5-dinitrophenyl-beta-D-xylobioside
recombinant wild-type enzyme, pH 7.2, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
14
2,5-dinitrophenyl-beta-D-xylobioside
recombinant wild-type enzyme, pH 7.2, 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.087
-
crude extract, using birchwood xylan in 100 mM sodium acetate buffer pH 5.0 as the substrate
37.22
-
after 427.83fold purification, using birchwood xylan in 100 mM sodium acetate buffer pH 5.0 as the substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Bcx possesses a beta-jellyroll fold that places its N- and C-termini in salt bridge contact. Mutant enzyme structure determination and analysis by X-ray diffraction and by NMR spectroscopy, overview. Overall conformation of Bcx changes very little in response to circular permutation, with effects largely being limited to increased local mobility near the new and the linked old termini and to a decrease in global stability against thermal denaturation
additional information
-
Bcx possesses a beta-jellyroll fold that places its N- and C-termini in salt bridge contact. Mutant enzyme structure determination and analysis by X-ray diffraction and by NMR spectroscopy, overview. Overall conformation of Bcx changes very little in response to circular permutation, with effects largely being limited to increased local mobility near the new and the linked old termini and to a decrease in global stability against thermal denaturation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutant enzyme, hanging drop method, 4°C, equilibration of 2 ml of protein solution, with 25-30 mg/ml protein in 20 mM sodium phosphate buffer, pH 7.0, against an equal volume of 13-20% saturated (NH4)2SO4 in 40 mM Tris-HCl, pH 8.0, X-ray diffraction structure determination and analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D101N/G103F/R132A/R136A
site-directed mutagenesis, the mutant is expressed in inclusion bodies
F48Y
site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme
F48Y/R49A/T50V/T147L
site-directed mutagenesis, the half-life of the mutant is 4fold increased compared to the wild-type enzyme
F48Y/T147L
site-directed mutagenesis, the half-life of the mutant is 7.5fold increased compared to the wild-type enzyme
F48Y/T50V
site-directed mutagenesis, the half-life of the mutant is increased compared to the wild-type enzyme
F48Y/T50V/T147L
site-directed mutagenesis, the half-life of the mutant is 15fold increased compared to the wild-type enzyme
G103F
site-directed mutagenesis, the mutation introduced a bulky hydrophobic residue causing a clash with the neighbouring residues that results in destabilization
T147L
site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme
T50V
site-directed mutagenesis, the mutant shows increased thermostability and activity compared to the wild-type enzyme
T50V/T147L
site-directed mutagenesis, the half-life of the mutant is increased compared to the wild-type enzyme
Y69F
the barrier for conversion of the 4C1 chair to the more-stable 2,5B boat in the wild-type enzyme-substrate complex is significantly lower than it is for the mutant. The mutation reduces the degree of oxacarbenium-ion character in the proximal xylose ring of the enzyme-substrate complex
additional information
additional information
construction of a library of circular permutants, generated by random circular permutation of Bcx, random DNase cleavage of the circularized Bcx gene, to introduce new termini in loop regions while linking its native termini directly or via one or two glycines, qualitative analysis, overview. Several permutations place key catalytic residues at or near the new termini with minimal deleterious effects on activity, up to 4fold increased activity. Mutant structure determination and analysis by X-ray diffraction and by NMR spectroscopy. Detailed stability and activity studies on three selected permutants, cpN35G2', cpY94G2', and cpY174G2', overview
additional information
-
construction of a library of circular permutants, generated by random circular permutation of Bcx, random DNase cleavage of the circularized Bcx gene, to introduce new termini in loop regions while linking its native termini directly or via one or two glycines, qualitative analysis, overview. Several permutations place key catalytic residues at or near the new termini with minimal deleterious effects on activity, up to 4fold increased activity. Mutant structure determination and analysis by X-ray diffraction and by NMR spectroscopy. Detailed stability and activity studies on three selected permutants, cpN35G2', cpY94G2', and cpY174G2', overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
thermal denaturation measurements, circular dichroism, overview
additional information
-
thermal denaturation measurements, circular dichroism, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(lambdaDE3) by cation exchange chromatography and gel filtration
ammonium sulfate saturation, CM-Sepharose FF column chromatography, and Sephacryl S-200 HR gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(lambdaDE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Esteban, R.; Villanueva, J.R.; Villa, T.G.
beta-D-Xylanases of Bacillus circulans WL-12
Can. J. Microbiol.
28
733-739
1982
Niallia circulans, Niallia circulans WL-12
-
Toerroenen, A.; Rouvinen, J.
Structural and functional properties of low molecular weight endo-1,4-beta-xylanases
J. Biotechnol.
57
137-149
1997
Niallia circulans, Trichoderma harzianum, Trichoderma reesei
Heck, J.X.; Soares, L.H.; Hertz, P.F.; Ayub, M.A.
Purification and properties of a xylanase produced by Bacillus circulans BL53 on solid-state cultivation
Biochem. Eng. J.
32
179-184
2006
Niallia circulans, Niallia circulans BL53
-
Soliman, M.E.; Ruggiero, G.D.; Pernia, J.J.; Greig, I.R.; Williams, I.H.
Computational mutagenesis reveals the role of active-site tyrosine in stabilising a boat conformation for the substrate: QM/MM molecular dynamics studies of wild-type and mutant xylanases
Org. Biomol. Chem.
7
460-468
2009
Niallia circulans (P09850)
Reitinger, S.; Yu, Y.; Wicki, J.; Ludwiczek, M.; DAngelo, I.; Baturin, S.; Okon, M.; Strynadka, N.C.; Lutz, S.; Withers, S.G.; McIntosh, L.P.
Circular permutation of Bacillus circulans xylanase: a kinetic and structural study
Biochemistry
49
2464-2474
2010
Niallia circulans (P09850), Niallia circulans
EXTERNAL LINKS (specific for EC-Number 3.2.1.8)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
