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Enzyme Nomenclature
Information on EC 3.2.1.8 - endo-1,4-beta-xylanase
for references in articles please use BRENDA:EC3.2.1.8
Word Map on EC 3.2.1.8
- 3.2.1.8
- xylans
- xylanases
- xylose
- trichoderma
-
arabinoxylans
- reesei
- xylooligosaccharides
- xylotriose
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birchwood
- spelt
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xylanolytic
-
straw
- xylotetraose
- beta-xylosidase
- endoglucanase
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carbohydrate-binding
-
lignocellulosic
-
bran
-
saccharification
-
hemicellulases
- cellulosa
- arabinofuranosidase
-
bagasse
- cellulomonas
-
cellulose-binding
-
avicel
- alpha-l-arabinofuranosidase
- cellulases
- thermomyces
- paper production
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hemicellulolytic
-
cellulase-free
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kraft
-
endo-acting
- nutrition
- biotechnology
- glucuronoxylans
- beta-d-xylopyranoside
-
thermoascus
- degradation
- neocallimastix
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biobleaching
- xylosidase
- biofuel production
- agriculture
- synthesis
- industry
- arabinan
- cellulosome
- mannanase
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water-extractable
- halodurans
-
taxi
-
corncob
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lignocellulolytic
- food industry
-
dockerin
- lanuginosus
- longibrachiatum
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.2.1.8
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RECOMMENDED NAME
GeneOntology No.
endo-1,4-beta-xylanase
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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
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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
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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
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Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
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Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
(beta/alpha)8 barrel with 2 catalytic functions, the acid/base and the nucleophile, at the C-terminal side
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Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
mode of action and hydrolysis pattern
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Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
a lysine residue is involved in substrate binding and is located at the binding site
Thermomonospora sp.
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Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
histidine, tryptophan residues and carboxylic groups are involved in substrate binding or catalysis
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Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
mode of action, substrate specificity, substrate binding mechanism
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Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
substrate recognition and sites of hydrolysis on the xylan substrates
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Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
the O-glycoside hydrolase catalyzes the random hydrolysis of internal beta-1,4-D-xylosidic linkages of xylan and xylooligosaccharides of maximal 4 residue chain length, inverse stereoselectivity
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
mode of attack on substrates
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Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
role of the thermostabilizing N-terminal domain XBD on enzyme activity, overview
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
induced fit mechanism upon ligand binding
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
mode of action and hydrolysis pattern
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
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endohydrolysis
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
aff. phaeospermum, GenBank Accession: HQ630967; aff. sacchari, GenBank Accession: HQ630961
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isolated from soil samples collected from different areas of Syria, cereal fields, olive fields, forests, and gardens
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isolated from soil samples collected from different areas of Syria, cereal fields, olive fields, forests, and gardens
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isolated from soil samples collected from different areas of Syria, cereal fields, olive fields, forests, and gardens
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xylanase II, minor enzyme form, growth in 1% wheat bran as carbon source
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bacterium enrichment culture clone Xyl8B8
UniProt
; fragment of 387 bp, part of the gene cxo; CDBB-531
UniProt
aff. salmonis, GenBank Accession: HQ630990; aff. spinifera, GenBank Accession: HQ631027
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aff. aethiopicum, GenBank Accession: HQ630964; aff. avenacea, Genbank Accession: HQ630977; aff. equiseti, GenBank Accession: HQ630976; aff. moniliformis, GenBank Accession: HQ630966; aff. proliferatum, GenBank Accession: HQ630965
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isozymes: Ia, Ib, Ic, IIa, IIb, IIc, IId, only isozyme Ic is constitutive
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aff. glomerata, GenBank Accession: HQ630999; aff. herbarum, GenBank Accession: HQ630963
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rumen bacteria, strain Mz5T, DSM14809, enzyme XynT, 2 isozymes
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isolated from the gut of a grass-feeding termite
UniProt
isolated from the gut of a grass-feeding termite
UniProt
a symbiotic bacterium isolated from the gut of Batocera horsfieldi larvae, gene xynA19
UniProt
isolated from the gut of Batocera horsfieldi larvae collected from oak trees, gene xynA119
UniProt
isolated from the gut of Eisenia fetida, gene xylG
UniProt
isolated from the gut of Eisenia fetida, gene xylG
UniProt
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
isolated from a hot spring in Baoshan City, Yunnan Province, China, gene xynA4
UniProt
isolated from a hot spring in Baoshan City, Yunnan Province, China, gene xynA4
UniProt
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171597, 171598, 171599, 171633, 171634, 654892, 679573, 680984, 695678, 696821, 698405, 707403, 710686, 731024, 737497
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isolated from acidic wastewater of a uranium mine in Jiangxi, China, gene xylD
UniProt
isozymes: Ia, Ib, Ic, IIa, IIb, IIc, IId, only isozyme Ic is constitutive
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isoforms xynA, xynC, family 10 glycoside hydrolases, xynB, family 11 glycoside hydrolase
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gene xyl; psychrophilic enzyme, antarctic bacterium
SwissProt
hybrid gene from Thermomonospora fusca with N-terminal region of Bacillus subtilis
UniProt
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171617, 171643, 698373, 742131, 742165, 742214, 742227, 742400, 742550, 742636, 742766, 742958, 743197, 743886, 743887
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aff. atroviride, GenBank Accession: HQ630969; aff. koningii, GenBank Accession: HQ630959; aff. lixii, GenBank Accession: HQ630960; aff. spirale, GenBank Accession: HQ630962
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two wheat varieties, Legat and Astuce; varieties Legat and Astuce, additionally microbial washed off activity of endoxylanase is investigated
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from Bos mutus rumen; RuCelA, a bifunctional xylanase/endoglucanase, EC 3.2.1.8 and EC 3.2.1.73; isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
UniProt
isolated from alkaline wastewater sludge of a paper mill
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
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key enzyme in beta-1,4-xylan degradation, which involves several hydrolases, overview
metabolism
KU366607
optimization of xylanase production using agro-industrial substrates up to 132 U/ml. Pretreated rice straw yields 126.9 mg/g maximum fermentable sugars
metabolism
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optimization of xylanase production using agro-industrial substrates up to 132 U/ml. Pretreated rice straw yields 126.9 mg/g maximum fermentable sugars
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physiological function
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two roles of Xyn5, localized on the cell surface, in water-insoluble xylan utilization: generation of the xylo-oligosaccharide inducers of all the xyn genes from water-insoluble xylan and attachment of the cells to the substrate so that the generated inducers can be immediately taken up by cells to activate expression of the xyn system, overview. Cell surface-bound Xyn5 is crucial for growth of strain W-61 in the water-insoluble xylan medium
physiological function
the gene xyl1 is important for the nematode to complete its life cycle
physiological function
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the N-terminal domain A2 is responsible for both the thermostability and substrate-binding capacity of XynA
physiological function
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endoxylanase is the key enzyme for xylan depolymerization, which attacks the main chain of xylan
physiological function
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endo-beta-1,4-xylanase is one of the key enzymes of ethanol productivity during the consolidated bioprocessing of lignocellulosics
physiological function
deletion of the gene encoding xylanase 11A reduces the growth rate of the mutant on minimal medium with xylan to 0.09 per h compared to 0.10 per h of the wild-type. The deletion mutant reaches a final OD600 of 6.78 compared to 8.18 in the wild-type culture. The drop of the pH value from initially 5.7 to 3.4 is approximately 3 h delayed in comparison to wild-type. Also the maximal concentration of reducing sugars in the medium is lower, and occurs 9 h later than in the wildtype culture. Heterologous expression of xylanase 11A on the cell surface of a xylanase-negative strain of Saccharomyces cerevisiae enables the strain to almost completely degrade xylan to xylotriose
physiological function
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constitutive expression of enzyme gene in tall fescue in the vacuole, apoplast, and Golgi, results in only a small number of plants with low enzyme activities and in reduced plant growth in apoplast, and golgi targeted plants. Constitutive expression in the apoplast also results in increased levels of cell wall bound hydroxycinnamic acid monomers and dimers, but no significant effect on cell wall xylose or arabinose content. In situ constitutive xylanase expression in the Golgi also results in increased ferulate dimers. Senescence-induced xylanase expression in the apoplast is considerably higher and does not affect plant growth or the level of monomeric hydroxycinnamic acids or lignin in the cell walls. These plants also show increased levels of ferulate dimers, and decreased levels of xylose with increased levels of arabinose in their cell walls
physiological function
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highest xylanase production (208 IU/ml) in 96 h occurs using 1% rice bran as the only carbon source
physiological function
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enzyme consists of a family 22 carbohydrate-binding module, a glycoside hydrolase family 10 catalytic domain, two fibronectin type III (Fn3) domains, and a family 3 carbohydrate-binding module at the C-terminus. The family 22 carbohydrate-binding module has an important role not only in binding to xylan and beta-glucan but also in feeding both polysaccharides into the neighboring GH10 catalytic domain
physiological function
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expression in a leaky outer membrane mutant of Gluconobacter oxydans created by deleting the TolB encoding gene gox1687. More than 70% of the total XynA activity (0.91 mmol per h and l culture) is detected in the culture supernatant of the TolB mutant and only 10% of endoxylanase activity is observed in the supernatant of wild-type Gluconobacter oxydans expressing XynA
physiological function
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coexpression of vacuole- or apoplast-targeted ferulic acid esterase from Aspergillus niger and senescence-induced and apoplast-targeted beta-1,4 endo-xylanase from Trichoderma reesei in Festuca arundinacea. Xylanase activity in senescent leaves increases and ferulic acid esterase activity decreases after tillering. Plants coexpressing both enzymes in the apoplast, with the lowest levels of ferulate monomers and dimers and the lowest levels of cell wall arabinoxylans, release ten times more cell wall hydroxycinnamic acids and five times more arabinoxylan from the cell wall on autodigestion compared to expression of ferulic acid esterase or xylanase alone. These plants also show a 31% increase in cellulase-mediated release of reducing sugars, a 5% point increase in in vitro dry matter digestibility and a 23% increase in acetyl bromide-soluble lignin
physiological function
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strain grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
physiological function
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strain grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
physiological function
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highest titer of xylanase (5.5 IU/ml) is obtained b y growth on oat spelt xylan
physiological function
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growth on oat spelt xylan is the most effective for xylanase production followed by beech wood or birch wood xylan
physiological function
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maximum peaks of xylanase production and specific activity occurr after 96 hours of cultivation in liquid medium using 3% (w/v) corncob as substrate
physiological function
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strain produces 7238 U/g of carboxymethylcellulase in medium composed of a sugarcane bagasse and wheat bran mixture in 192 h of fermentation
physiological function
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strain produces 1044 U/g of carboxymethylcellulase in medium composed of a sugarcane bagasse and wheat bran mixture in 192 h of fermentation
physiological function
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strain produces considerable amounts of extracellular hydrolytic enzymes on lignocellulosic substrates at 55°C incubated for 8 days in 150 ml shake flask experiments. The maximum enzyme activities on wheat straw and guayule bagasse are: xylanase 130.1 U/mg, inulinase 34.1 U/mg, carboxymethylcellulase 4.8 U/mg, filter paper assay (FPase) 5.5 FPU/g and pectinase 3.2 U/mg, respectively
physiological function
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in solid state fermentation using lignocellulosic materials as substrates, Myceliophthora thermophila JCP 1-4 is the best producer of endoglucanase (357,51 U/g), beta-glucosidase (45.42 U/g), xylanase (93,11 U/g) and avicelase (3.58 U/g) among the strain tested
physiological function
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strain produces beta-xylanase activity of 59600 nkat/ml when cultivated on a medium containing corn cobs as substrate and yeast extract as nitrogen source, at pH 6.5 and 50°C. Lower beta-xylanase activities are produced after growth on other xylan substrates, sugars and soluble starch
physiological function
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strain produces 7238 U/g of carboxymethylcellulase in medium composed of a sugarcane bagasse and wheat bran mixture in 192 h of fermentation
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physiological function
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highest xylanase production (208 IU/ml) in 96 h occurs using 1% rice bran as the only carbon source
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physiological function
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expression in a leaky outer membrane mutant of Gluconobacter oxydans created by deleting the TolB encoding gene gox1687. More than 70% of the total XynA activity (0.91 mmol per h and l culture) is detected in the culture supernatant of the TolB mutant and only 10% of endoxylanase activity is observed in the supernatant of wild-type Gluconobacter oxydans expressing XynA
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physiological function
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strain grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
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physiological function
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endo-beta-1,4-xylanase is one of the key enzymes of ethanol productivity during the consolidated bioprocessing of lignocellulosics
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physiological function
-
strain grows well on locust bean galactomannan, Solka floc, wheat bran and pectin and at 45°C
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physiological function
-
enzyme consists of a family 22 carbohydrate-binding module, a glycoside hydrolase family 10 catalytic domain, two fibronectin type III (Fn3) domains, and a family 3 carbohydrate-binding module at the C-terminus. The family 22 carbohydrate-binding module has an important role not only in binding to xylan and beta-glucan but also in feeding both polysaccharides into the neighboring GH10 catalytic domain
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physiological function
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endoxylanase is the key enzyme for xylan depolymerization, which attacks the main chain of xylan
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physiological function
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maximum peaks of xylanase production and specific activity occurr after 96 hours of cultivation in liquid medium using 3% (w/v) corncob as substrate
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physiological function
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strain produces beta-xylanase activity of 59600 nkat/ml when cultivated on a medium containing corn cobs as substrate and yeast extract as nitrogen source, at pH 6.5 and 50°C. Lower beta-xylanase activities are produced after growth on other xylan substrates, sugars and soluble starch
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physiological function
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strain produces considerable amounts of extracellular hydrolytic enzymes on lignocellulosic substrates at 55°C incubated for 8 days in 150 ml shake flask experiments. The maximum enzyme activities on wheat straw and guayule bagasse are: xylanase 130.1 U/mg, inulinase 34.1 U/mg, carboxymethylcellulase 4.8 U/mg, filter paper assay (FPase) 5.5 FPU/g and pectinase 3.2 U/mg, respectively
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physiological function
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in solid state fermentation using lignocellulosic materials as substrates, Myceliophthora thermophila JCP 1-4 is the best producer of endoglucanase (357,51 U/g), beta-glucosidase (45.42 U/g), xylanase (93,11 U/g) and avicelase (3.58 U/g) among the strain tested
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physiological function
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strain produces 1044 U/g of carboxymethylcellulase in medium composed of a sugarcane bagasse and wheat bran mixture in 192 h of fermentation
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physiological function
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deletion of the gene encoding xylanase 11A reduces the growth rate of the mutant on minimal medium with xylan to 0.09 per h compared to 0.10 per h of the wild-type. The deletion mutant reaches a final OD600 of 6.78 compared to 8.18 in the wild-type culture. The drop of the pH value from initially 5.7 to 3.4 is approximately 3 h delayed in comparison to wild-type. Also the maximal concentration of reducing sugars in the medium is lower, and occurs 9 h later than in the wildtype culture. Heterologous expression of xylanase 11A on the cell surface of a xylanase-negative strain of Saccharomyces cerevisiae enables the strain to almost completely degrade xylan to xylotriose
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additional information
several sequence and structure modifications appears to be responsible for the acidophilic characteristic of XYL1p 1. The presence of an aspartic acid H bonded to the acid/base catalyst 2. the nature of specifically conserved residues in the active site 3. the negative potential at the surface 4. the decreased number of salt bridges and H bonds in comparison with highly alkaline enzymes
additional information
the N-terminal domain of the enzyme is required for catalytic activity
additional information
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specific activity of purified recombinant XynS14, expressed in Pichia pastoris, is 2.4fold higher than recombinant XynS14, expressed in Escherichia coli
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
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specific activity of purified recombinant XynS14, expressed in Pichia pastoris, is 2.4fold higher than recombinant XynS14, expressed in Escherichia coli
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additional information
Bacillus sp. (in: Bacteria) NTU-06
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the enzyme shows a high salt tolerance
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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
2-nitrophenyl xylopyranoside + H2O
2-nitrophenol + xylopyranose
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?
4-methylumbelliferyl beta-D-cellobioside + H2O
?
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?
4-methylumbelliferyl-beta-xylobiose + H2O
?
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enzyme cleaves at the second glycosidic bond adjacent to the aglycon
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?
4-methylumbelliferyl-beta-xylotriose + H2O
?
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highly preferred substrate, enzyme cleaves at the second glycosidic bond adjacent to the aglycon
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?
4-methylumbelliferyl-xylobiose + H2O
?
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hydrolysis at the glycosidic linkage
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?
4-methylumbelliferyl-xylotriose + H2O
?
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hydrolysis at the glycosidic linkage
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?
4-nitrophenyl 4-O-beta-D-xylopyranosyl-beta-D-xylopyranoside + H2O
4-nitrophenol + 4-O-beta-D-xylopyranosyl-beta-D-xylopyranose
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?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
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?
4-nitrophenyl alpha-L-arabinopyranoside + H2O
4-nitrophenol + alpha-L-arabinopyranose
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