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Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Acetivibrio thermocellus and UniProt Accession P51584

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Acetivibrio thermocellus
UNIPROT: P51584 not found.
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Word Map
The taxonomic range for the selected organisms is: Acetivibrio thermocellus
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-D-xylanase
-
(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-xylanase
-
-
-
-
endo-1,4-beta-D-xylanase
-
-
-
-
endo-1,4-beta-xylanase
-
-
-
-
endo-1,4-xylanase
-
-
-
-
endo-beta-1,4-xylanase
-
-
-
-
endoxylanase
-
-
-
-
family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-beta-1,4-xylanase
-
-
FIA-xylanase
-
-
-
-
ORF4
-
-
-
-
TAXI
-
-
-
-
X34
-
-
-
-
XYLA
-
-
-
-
xylanase
Xylanase 22
-
-
-
-
xylanase, endo-1,4-
-
-
-
-
XYLD
-
-
-
-
XYLY
-
-
-
-
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
xylohexaose + H2O
?
show the reaction diagram
-
-
-
?
1,4-beta-D-xylan + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl alpha-L-arabinofuranoside + H2O
4-nitrophenol + alpha-L-arabinofuranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
show the reaction diagram
-
highest activity
-
-
?
4-O-methyl glucuronoxylan + H2O
?
show the reaction diagram
-
-
-
-
?
4-O-methyl-beta-D-glucuronoxylan + H2O
?
show the reaction diagram
-
-
-
-
?
arabinan + H2O
?
show the reaction diagram
-
from sugar beet, low activity
-
-
?
arabinogalactan + H2O
?
show the reaction diagram
-
low activity
-
-
?
arabinoxylan + H2O
?
show the reaction diagram
-
from rye or wheat, low activity
-
-
?
beechwood glucuronoxylan + H2O
?
show the reaction diagram
-
-
products are acidic xylo-oligosaccharides having methyl glucuronic acid moiety penultimate to the reducing end of xylan
-
?
beechwood xylan + H2O
?
show the reaction diagram
-
best substrate, TLC analysis of CtXynGH30 hydrolysis products from beechwood xylan. CtXynGH30 shows the release of a series of higher xylooligosaccharides, overview
-
-
?
beta-1,4-xylan + H2O
?
show the reaction diagram
birchwood xylan + H2O
?
show the reaction diagram
galactomannan + H2O
?
show the reaction diagram
oat spelt xylan + H2O
?
show the reaction diagram
-
-
-
-
?
wheat arabinoxylan + H2O
xylose + ?
show the reaction diagram
-
-
-
-
?
xyloglucan + H2O
?
show the reaction diagram
-
low activity
-
-
?
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
beta-1,4-xylan + H2O
?
show the reaction diagram
-
-
-
?
wheat arabinoxylan + H2O
xylose + ?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
more than 70% increase of activity at 20 mM
Fe3+
-
more than 20% increase of activity at 20 mM
additional information
-
Zn2+ and Mn2+ show almost no effect on enzyme activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
-
Ca2+
-
slight inhibition
Hg2+
-
complete inhibition at 1 mM
K+
-
about 80% residual activity at 20 mM
Na+
-
about 70% residual activity at 20 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 3
4-nitrophenyl alpha-L-arabinofuranoside
-
at pH 5.0 and 50°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
104
4-nitrophenyl alpha-L-arabinofuranoside
-
at pH 5.0 and 50°C
2008.3
beechwood xylan
-
pH 6.0, 37°C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.5
4-nitrophenyl alpha-L-arabinofuranoside
-
at pH 5.0 and 50°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
purified mutant XynC-BC
30
-
substrate 4-O-methyl-beta-D-glucuronoxylan, pH 6.0, 70°C
31
-
substrate birchwood xylan, pH 6.0, 70°C
34
-
substrate beechwood glucuronoxylan, pH 6.0, 70°C
39
purified mutant XynC-C
390
purified mutant XynZ-C
79
purified mutant XynZ-BDC
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 11.5
-
activity range, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 85
-
over 50% of maximal activity within this range, profile overview
37 - 60
-
more than 50% activity between 37 and 60°C
40 - 70
more than 95% of maximum activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
CtXynGH30 is a family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-beta-1,4-xylanase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
XYNY_ACETH
1077
1
119673
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
N-terminal moiety of Xyn10B (residues 32-551), comprising a carbohydrate-binding module (CBM22-1) and the GH10 E337A mutant crystallized in complex with xylohexaose, by the hanging-drop vapour-phase diffusion method, to beyond 2.0 A resolution. Crystals belong to space group P3221 and contain a dimer in the asymmetric unit
structure of a truncated derivative of comprising exclusively the enzyme catalytic module. The enzyme displays a (beta/alpha)8 TIM-barrel core with a side-associated beta-sheet domain. In mutant E225A, solved in the presence of xylotetraose, xylotetraose-cleavage oligosaccharides partially occupy subsites -3 to +2. The sugar ring at the +1 subsite is held in place by hydrophobic stacking interactions between Tyr139 and Tyr200 and hydrogen bonds to the OH group of Tyr227. The xylopyranosyl ring at the -1 subsite appears in the alpha-anomeric configuration
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E337A
capture of the substrate xylohexaose in the inactivated site
E225A
mutation in catalytic residue, crystallization data
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11
-
completely stable at pH 7.0, over 50% activity remaining at pH 4.0-11.0, inactivation at pH 12.0 and pH below 2.0
751347
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 60
-
the enzyme activity remains stable after 16 h at 50°C. At 60°C, the enzyme shows less than 40% activity after 3 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant purified by immobilized metal-ion affinity chromatography and gel-filtration
HisTrap column chromatography and Mono-Q column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into pGEM T-easy and pET-21a vector, expressed in Escherichia coli XL10-Gold and BL21 (DE3)
CtXynGH30, recombinant overexpression in Escherichia coli strain BL21
-
expressed in Escherichia coli BL21(DE3) cells
-
gene xynC, subcloning in Escherichia coli strain DH5alpha, expression of wild-type and mutant enzymes in Escherichia coli
gene xynZ, subcloning in Escherichia coli strain DH5alpha, expression of wild-type and mutant enzymes in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
during degradation of bagasse, hemicellulose content, especially arabinan, and the cellulose crystallinity of bagasse affects the synergism of degrading enzymes cellulase and xylanase. Higher synergism (above 3.4) is observed for glucan conversion, at low levels of arabinan (0.9%), during the hydrolysis of peracetic acid pretreated bagasse. In contrast, 1-ethyl-3-methylimidazolium acetate pretreated bagasse shows lower cellulose crystallinity and achieves higher synergism (over 1.9) for xylan conversion. The combination of Thermobidfida endoglucanase Cel6A and xylanase Xyn11A results in higher synergism for glucan conversion than the combination of Cel6A with Clostridium thermocellum XynZ-C
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
Najmudin, S.; Pinheiro, B.A.; Romao, M.J.; Prates, J.A.; Fontes, C.M.
Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-beta-D-xylanase 10B in complex with xylohexaose
Acta Crystallogr. Sect. F
64
715-718
2008
Acetivibrio thermocellus (P51584), Acetivibrio thermocellus
Manually annotated by BRENDA team
Sajjad, M.; Khan, M.I.; Akbar, N.S.; Ahmad, S.; Ali, I.; Akhtar, M.W.
Enhanced expression and activity yields of Clostridium thermocellum xylanases without non-catalytic domains
J. Biotechnol.
145
38-42
2010
Acetivibrio thermocellus (O32374), Acetivibrio thermocellus (P10478)
Manually annotated by BRENDA team
Freire, F.; Verma, A.; Bule, P.; Alves, V.; Fontes, C.; Goyal, A.; Najmudin, S.
Conservation in the mechanism of glucuronoxylan hydrolysis revealed by the structure of glucuronoxylan xylanohydrolase (CtXyn30A) from Clostridium thermocellum
Acta Crystallogr. Sect. D
72
1162-1173
2016
Acetivibrio thermocellus (A3DJS9), Acetivibrio thermocellus DSM 1237 (A3DJS9)
Manually annotated by BRENDA team
Jia, L.; Goncalves, G.A.; Takasugi, Y.; Mori, Y.; Noda, S.; Tanaka, T.; Ichinose, H.; Kamiya, N.
Effect of pretreatment methods on the synergism of cellulase and xylanase during the hydrolysis of bagasse
Biores. Technol.
185
158-164
2015
Acetivibrio thermocellus (P10478), Thermobifida fusca (Q47QL8), Acetivibrio thermocellus DSM 1237 (P10478)
Manually annotated by BRENDA team
Verma, A.; Goyal, A.
A novel member of family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-beta-1,4-xylanase (CtXynGH30) from Clostridium thermocellum orchestrates catalysis on arabinose decorated xylans
J. Mol. Catal. B
129
6-14
2016
Acetivibrio thermocellus
-
Manually annotated by BRENDA team
de Camargo, B.R.; Claassens, N.J.; Quirino, B.F.; Noronha, E.F.; Kengen, S.W.M.
Heterologous expression and characterization of a putative glycoside hydrolase family 43 arabinofuranosidase from Clostridium thermocellum B8
Enzyme Microb. Technol.
109
74-83
2018
Acetivibrio thermocellus, Acetivibrio thermocellus B8
Manually annotated by BRENDA team
Verma, A.; Goyal, A.
A novel member of family 30 glycoside hydrolase subfamily 8 glucuronoxylan endo-beta-1,4-xylanase (CtXynGH30) from Clostridium thermocellum orchestrates catalysis on arabinose decorated xylans
J. Mol. Catal. B
129
6-14
2016
Acetivibrio thermocellus
-
Manually annotated by BRENDA team