Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.1.99 - arabinan endo-1,5-alpha-L-arabinanase and Organism(s) Thermotoga petrophila and UniProt Accession A5IKD4

for references in articles please use BRENDA:EC3.2.1.99
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Acts best on linear 1,5-alpha-L-arabinan. Also acts on branched arabinan, but more slowly.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Thermotoga petrophila
UNIPROT: A5IKD4
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Thermotoga petrophila
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
endo-arabinanase, arase, endo-arabinase, endoarabinanase, abn-ts, abns1, abnase, endo-1,5-alpha-l-arabinanase, cedaase, arb43a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endo-1,5-alpha-L-arabinanase
-
araban 5-alpha-L-arabinohydrolase
-
-
-
-
arabinase, endo-1,5-alpha-L-
-
-
-
-
endo-(1->5)-alpha-L-arabinanase
-
-
-
-
endo-1,5-alpha-arabinanase
-
-
-
-
endo-1,5-alpha-L-arabinanase
endo-1,5-alpha-L-arabinase
-
-
-
-
endo-alpha-(1->5)-L-arabinanase
-
-
-
-
endo-alpha-1,5-arabanase
-
-
-
-
endo-arabanase
-
-
-
-
endo-arabinanase
-
-
-
-
endo-arabinase
-
-
-
-
endo-L-arabinanase
-
-
-
-
endoarabinase
-
-
-
-
additional information
-
the enzyme belongs to the glycoside hydrolase family 43, GH43
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
5-alpha-L-arabinan 5-alpha-L-arabinanohydrolase
Acts best on linear 1,5-alpha-L-arabinan. Also acts on branched arabinan, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
75432-96-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1->5)-L-alphaarabinan + H2O
(1->5)-L-arabinooligosaccharides
show the reaction diagram
-
-
-
?
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
additional information
?
-
-
the enzyme shows the ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
152.1
purified protein, using L-arabinan as substrate, at pH 6.0 and 70°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
the enzyme retains more than 75% activity over a pH range from 4.0 to 7.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62 - 80
the enzyme shows relative activity ranging from 77% to 78% at temperatures of 62°C and 80°C, respectively
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
1 * 49000, small angle X-ray scattering
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 49000, small angle X-ray scattering
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization is performed by the sitting-drop vapour-diffusion method. Single crystals are obtained from a solution containing 0.1 M MES buffer pH 6.5, 0.8 M ammonium sulfate, 0.1 M EDTA, 0.1 M L-proline and 5% (v/v) dioxane. X-ray diffraction data are collected to a resolution of 2.86 A using synchrotron radiation. The diffraction pattern is indexed in the tetragonal space group P422, with unit-cell parameters a = b = 83.71, c = 408.25 A
purified recombinant His-tagged enzyme, 0.0005 ml of protein solution containing 30 mg/ml in 25 mM Tris-HCl buffer, pH 7, 5, is mixed with 0.0005 ml of reservoir solution containing 0.1 M MES buffer, pH 6.5, 0.8 M ammonium sulfate, 0.1 M EDTA, 0.1 M L-proline and 5% v/v dioxane, X-ray diffraction structure determination and analysis at 2.86 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90 - 95
the enzyme is fully heat-stable (up to 10 h) and retains activity at temperatures up to 90°C. The enzyme loses its activity only after 90 min when incubated at 95°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+-chelating affinity column chromatography and Superdex 75 gel filtration
recombinant His-tagged enzyme from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 cells
overexpressed in Escherichia coli Top10
overexpression of His-tagged enzyme in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biofuel production
conversion of lignocellulosic biomass to biofuels. Endo-1,5-alpha-L-arabinanase hydrolyzes alpha-1,5-arabinofuranosidic bonds in hemicelluloses such as arabinoxylan and arabinan as well as in other arabinose-containing polysaccharides
industry
-
endo-1,5-alpha-L-arabinanases belonging to glycoside hydrolase family 43 are of great industrial interest for use in food technology, organic synthesis and biofuel production owing to their ability to catalyze the hydrolysis of alpha-1,5-arabinofuranosidic bonds in arabinose-containing polysaccharides
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Squina, F.M.; Prade, R.A.; Wang, H.; Murakami, M.T.
Expression, purification, crystallization and preliminary crystallographic analysis of an endo-1,5-alpha-L-arabinanase from hyperthermophilic Thermotoga petrophila
Acta Crystallogr. Sect. F
65
902-905
2009
Thermotoga petrophila
Manually annotated by BRENDA team
Squina, F.M.; Santos, C.R.; Ribeiro, D.A.; Cota, J.; de Oliveira, R.R.; Ruller, R.; Mort, A.; Murakami, M.T.; Prade, R.A.
Substrate cleavage pattern, biophysical characterization and low-resolution structure of a novel hyperthermostable arabinanase from Thermotoga petrophila
Biochem. Biophys. Res. Commun.
399
505-511
2010
Thermotoga petrophila (A5IKD4), Thermotoga petrophila
Manually annotated by BRENDA team
Squina, F.; Prade, R.; Wang, H.; Murakami, M.
Expression, purification, crystallization and preliminary crystallographic analysis of an endo-1,5-alpha-L-arabinanase from hyperthermophilic Thermotoga petrophila
Acta Crystallogr. Sect. F
65
902-905
2009
Thermotoga petrophila (A5IKD4), Thermotoga petrophila, Thermotoga petrophila DSM 13995 (A5IKD4)
Manually annotated by BRENDA team