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) Geobacillus stearothermophilus and UniProt Accession B3EYM8

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:
Geobacillus stearothermophilus
UNIPROT: B3EYM8
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
endo-arabinanase, endo-arabinase, endoarabinanase, arase, abn-ts, abns1, abnase, endo-1,5-alpha-l-arabinanase, arb43a, cedaase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans
show the reaction diagram
three catalytic carboxylates: Asp27, the general base, Glu201, the general acid, and Asp147, the pKa modulator, substrate binding structure and catalytic mechanism, overview
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
linear arabinan + H2O
?
show the reaction diagram
-
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene abnB
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
IABN_GEOSE
315
0
35763
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type enzyme, and mutant enzyme E201A in complex with arabinotriose, hanging drop vapour diffusion, 0.0025-0.003 ml of protein solution with 6.5-13 mg/ml protein is mixed with an equal volume of precipitant solution containing 1.7 M lithium sulfate, 0.1 M Tris buffer, pH 7.5, and 15% v/v glycerol for the wild-type enzyme, and 1.9 M lithium sulfate, 0.1 M Tris buffer, pH 8.5, and 4% w/v PEG 400 for the mutant enzyme, X-ray diffraction structure determination and analysis, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D147A
site-directed mutagenesis, structure comparison with the wild-type enzyme
E201A
site-directed mutagenesis, structure comparison with the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene abnB, expression of wild-type and mutant enzymes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Alhassid, A.; Ben-David, A.; Tabachnikov, O.; Libster, D.; Naveh, E.; Zolotnitsky, G.; Shoham, Y.; Shoham, G.
Crystal structure of an inverting GH 43 1,5-alpha-L-arabinanase from Geobacillus stearothermophilus complexed with its substrate
Biochem. J.
422
73-82
2009
Geobacillus stearothermophilus (B3EYM8), Geobacillus stearothermophilus T-6 (B3EYM8)
Manually annotated by BRENDA team