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Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Thermoclostridium stercorarium and UniProt Accession Q8GJ44

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Thermoclostridium stercorarium
UNIPROT: Q8GJ44 not found.
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The taxonomic range for the selected organisms is: Thermoclostridium stercorarium
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
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(1--> 4)-beta-xylan 4-xylanohydrolase
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-
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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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-
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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
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Xylanase 22
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xylanase, endo-1,4-
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XYLD
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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
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-57-4
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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
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-
-
?
1,4-beta-D-xylan + H2O
?
show the reaction diagram
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catabolite repression with glucose and other readily metabolizable substrates
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-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
show the reaction diagram
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no hydrolysis
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
p-nitrophenyl beta-D-cellobioside + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-xylopyranoside
?
show the reaction diagram
-
-
-
-
?
xylobiose + H2O
?
show the reaction diagram
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low activity, xylanase A
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-
?
xylotriose + H2O
xylobiose + xylose
show the reaction diagram
-
xylanase A
xylanase A
?
1,4-beta-D-xylan + H2O
additional information
-
NATURAL SUBSTRATE
NATURAL 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
-
catabolite repression with glucose and other readily metabolizable substrates
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fe2+
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1 mM FeSO4, complete inhibition, xylanase A
PCMB
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1 mM, complete inhibition, xylanase A
Zn2+
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1 mM ZnCl2, patial inhibition, xylanase A
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
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pH 5.0: about 80% of maximal activity, pH 8.0: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 90
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60°C: about 50% of maximal activity, 90°C: about 20% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
endo-1,4-beta-xylanase A precursor
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
XYNA1_THEST
651
1
70151
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
44000
44377
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x * 44377, calculation from nucleotide sequence
54000
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x * 54000, recombinant xylanase A produced in Escherichia coli, SDS-PAGE
64000
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xylanase C, disc gel electrophoresis
73000
-
xylanase B, disc gel electrophoresis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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xylanase A contains 19% carbohydrate, xylanase B contains 3% carbohydrate, xylanase C contains 4% carbohydrate
proteolytic modification
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32 amino acids are removed from the N-terminus of Xyn B by proteolysis, resulting in the formation of a protein species with a predicted molecular weight of 40805 Da
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
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4°C, 24 h, xylanase B and C lose 50% of their activity
171615
4
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4°C, 24 h, complete inactivation of xylanase A
171615
5 - 12
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4°C, 24 h, stable
171661
5.5
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4°C, 24 h, xylanase A loses 50% of its activity
171615
7 - 12
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4°C, 24 h, stable
171615
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
-
15 days, stable
75
-
1 h, xylanase A and C are stable, xylanase B retains 85% of its activity
80
-
enzyme begins to denature at around 80°C
81
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half-life of xylanase A is 90 min, half-life of xylanase B is 2 min 30 s, half-life of xylanase C is 8 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant xylanase A produced in Escherichia coli
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xylanase A, B and C
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
the enzyme begins to denature at around 80°C and is completely denatured at 100°C. After 5 min at 100°C a large quantity of precipitate without any activity is formed. Aggregated xylanase B is disentangled and dissolved by urea treatment. The native structure is restored by rapid refolding after dilution of urea. Irreversible denaturation of the protein is caused by the same mechanism in solution and in aggregate. The remaining activity detected at 60°C after incubation at pH 7.0 and 100°C is due to the activity of the enzyme that recovers its native structure by correct protein refolding from the denatured state during chilling on ice
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sakka, K.; Kojima, Y.; Kondo, T.; Karita, S.; Shimada, K.; Ohmiya, K.
Purification and characterization of xylanase A from Clostridium stercorarium F-9 and a recombinant Escherichia coli
Biosci. Biotechnol. Biochem.
58
1496-1499
1994
Thermoclostridium stercorarium, Thermoclostridium stercorarium F-9
Manually annotated by BRENDA team
Berenger, J.F.; Frixon, C.; Bigliardi, J.; Creuzet, N.
Production, purification, and properties of thermostable xylanase from Clostridium stercorarium
Can. J. Microbiol.
31
635-643
1985
Thermoclostridium stercorarium
-
Manually annotated by BRENDA team
Sakka, K.; Fukumura, M.; Tanaka, A.; Ohmiya, K.
Characterization of thermostability of Clostridium stercorarium xylanase
Ann. N. Y. Acad. Sci.
799
341-345
1996
Thermoclostridium stercorarium, Thermoclostridium stercorarium F-9
Manually annotated by BRENDA team
Fukumura, M.K.; Sakka, K.; Shimida, K.; Ohmiya, K.
Nucleotide sequence of the Clostridium stercorarium xynB gene encoding an extremely thermostable xylanase and characterization of the translated product
Biosci. Biotechnol. Biochem.
59
40-46
1995
Thermoclostridium stercorarium
Manually annotated by BRENDA team
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