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Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Bispora sp. MEY-1 and UniProt Accession D0QF43

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Bispora sp. MEY-1
UNIPROT: D0QF43 not found.
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The taxonomic range for the selected organisms is: Bispora sp. MEY-1
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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-
-
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beta-1,4-D-xylanase
-
-
-
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beta-1,4-xylan xylanohydrolase
-
-
-
-
beta-1,4-xylanase
-
-
-
-
beta-D-xylanase
-
-
-
-
beta-xylanase
-
-
-
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endo-(1--> 4)-beta-xylanase
-
-
-
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endo-1,4-beta-D-xylanase
-
-
-
-
endo-1,4-beta-xylanase
-
-
-
-
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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-
-
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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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-
-
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XYLY
-
-
-
-
additional information
PATHWAY SOURCE
PATHWAYS
-
-, -
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
beta-1,4-xylan + H2O
?
show the reaction diagram
4-nitrophenyl beta-D-xylose + H2O
4-nitrophenol + D-xylose
show the reaction diagram
-
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
?
show the reaction diagram
-
-
-
?
beta-1,4-xylan + H2O
?
show the reaction diagram
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
beta-1,4-xylan + H2O
?
show the reaction diagram
-
-
-
?
beta-1,4-xylan + H2O
?
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
activates 66.5% at 1 mM
Cr3+
activates 19% at 10 mM
additional information
no effect by EDTA, Li+, Na+, and K+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SDS
complete inhibition at 5 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
activates 16% at 10 mM
2-mercaptoethanol
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18830
purified recombinant Xyl10C
1429
recombinant enzyme, substrate oat spelt xylan
2020
recombinant enzyme, substrate 4-O-methyl-D-glucuronoxylan
2144
recombinant enzyme, substrate birchwood xylan
2463
recombinant enzyme, substrate beechwood xylan
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 5
recombinant Xyl10C
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 7
first peak at pH 3.0 with 63% of maximal activity, and second peak with maximal activity at pH 4.5-5.0, profile, overview
1.5 - 4
60% of maximal activity at pH 1.5 and pH 4.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
recombinant Xyl10C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 100
activity range, 80% of maximal activity at 75-90°C, 20% at 100°C, and 10% at 40°C, profile, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CGMCC 2500, gene xyl10C
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
grown on wheat bran
Manually annotated by BRENDA team
additional information
cultured in wheat bran medium, optimal growth occurs at pH 2.5-3.0
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
D0QF43_9HELO
424
0
46589
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
449000
x * 449000, Xyl10C, sequence calculation, x * 90000, about, glycosylated recombinant Xyl10C, SDS-PAGE, x * 55000, deglycosylated recombinant Xyl10C, SDS-PAGE
55000
x * 449000, Xyl10C, sequence calculation, x * 90000, about, glycosylated recombinant Xyl10C, SDS-PAGE, x * 55000, deglycosylated recombinant Xyl10C, SDS-PAGE
90000
x * 449000, Xyl10C, sequence calculation, x * 90000, about, glycosylated recombinant Xyl10C, SDS-PAGE, x * 55000, deglycosylated recombinant Xyl10C, SDS-PAGE
49800
x * 49800, about, sequence calculation, mature enzyme protein
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 449000, Xyl10C, sequence calculation, x * 90000, about, glycosylated recombinant Xyl10C, SDS-PAGE, x * 55000, deglycosylated recombinant Xyl10C, SDS-PAGE
?
x * 49800, about, sequence calculation, mature enzyme protein
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1 - 6
purified recombinantg enzyme, 37°C, stable
707258
8
and above, 60 min, complete inactivation
707258
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
purified recombinant Xyl10C, 60 min, completely stablem half-life is 45 h
85
purified recombinant Xyl10C, half-life is 3 h
90
purified recombinant Xyl10C, 10 min, 87% remaining activity
60
purified recombinant enzyme, 60 min, pH 3.0, 98% remaining activity
80
purified recombinant enzyme, 5 min, pH 3.0, 25% remaining activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant Xyl10C 1.1fold from Pichia pastoris by anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene xyl10C from genomic DNA, DNA and amino acid sequence determination and analysis, sequence comparisons, overexpression in Pichia pastoris
gene xylD, DNA and amino acid sequence determination and analysis, phylogenetic tree, subcloning in Escherichia coli strain DH10B, expression in Pichia pastoris GS115
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Luo, H.; Yang, J.; Li, J.; Shi, P.; Huang, H.; Bai, Y.; Fan, Y.; Yao, B.
Molecular cloning and characterization of the novel acidic xylanase XYLD from Bispora sp. MEY-1 that is homologous to family 30 glycosyl hydrolases
Appl. Microbiol. Biotechnol.
86
1829-1839
2010
Bispora sp. MEY-1 (D6MYS9)
Manually annotated by BRENDA team
Luo, H.; Li, J.; Yang, J.; Wang, H.; Yang, Y.; Huang, H.; Shi, P.; Yuan, T.; Fan, Y.; Yao, B.
A thermophilic and acid stable family-10 xylanase from the acidophilic fungus Bispora sp. MEY-1
Extremophiles
13
849-857
2009
Bispora sp. MEY-1 (D0QF43)
Manually annotated by BRENDA team