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Information on EC 5.3.1.5 - xylose isomerase and Organism(s) Bacteroides thetaiotaomicron and UniProt Accession Q8A9M2

for references in articles please use BRENDA:EC5.3.1.5
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IUBMB Comments
Contains two divalent metal ions, preferably magnesium, located at different metal-binding sites within the active site. The enzyme catalyses the interconversion of aldose and ketose sugars with broad substrate specificity. The enzyme binds the closed form of its sugar substrate (in the case of xylose and glucose, only the alpha anomer ) and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism.
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This record set is specific for:
Bacteroides thetaiotaomicron
UNIPROT: Q8A9M2
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Word Map
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The taxonomic range for the selected organisms is: Bacteroides thetaiotaomicron
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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alpha-D-xylopyranose
=
alpha-D-xylufuranose
=
alpha-D-xylufuranose
Synonyms
xylose isomerase, glucose isomerase, d-xylose isomerase, spezyme, xylose (glucose) isomerase, glucose/xylose isomerase, sdxyi, tthxi, tcaxi, sweetzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-xylose aldose-ketose-isomerase
-
-
-
-
D-xylose isomerase
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-
-
-
D-Xylose ketoisomerase
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-
-
-
D-xylulose keto-isomerase
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-
-
-
Isomerase, xylose
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-
-
-
Swetase
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-
-
-
XI
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha-D-xylopyranose aldose-ketose-isomerase
Contains two divalent metal ions, preferably magnesium, located at different metal-binding sites within the active site. The enzyme catalyses the interconversion of aldose and ketose sugars with broad substrate specificity. The enzyme binds the closed form of its sugar substrate (in the case of xylose and glucose, only the alpha anomer [4]) and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-82-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
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
D-Glucose
D-Fructose
show the reaction diagram
-
-
-
r
D-Xylose
D-Xylulose
show the reaction diagram
-
-
-
r
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
x * 50000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 100 mM sodium chloride, 100 mM bicine pH 9.0, 20% (v/v) PEG MME 550
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Ni-NTA column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta2 (DE3)pLysS cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cho, J.W.; Han, B.G.; Park, S.Y.; Kim, S.J.; Kim, M.D.; Lee, B.I.
Overexpression, crystallization and preliminary X-ray crystallographic analysis of a putative xylose isomerase from Bacteroides thetaiotaomicron
Acta Crystallogr. Sect. F
69
1127-1130
2013
Bacteroides thetaiotaomicron (Q8A9M2), Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron DSM 2079 (Q8A9M2)
Manually annotated by BRENDA team