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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 5.3.1.25 - L-fucose isomerase and Organism(s) Aeribacillus pallidus and UniProt Accession C0SSE7

for references in articles please use BRENDA:EC5.3.1.25
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+). The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism . The enzyme from Escherichia coli can also convert D-arabinose to D-ribulose . The enzyme from the thermophilic bacterium Caldicellulosiruptor saccharolyticus also converts D-altrose to D-psicose and L-galactose to L-tagatose .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Aeribacillus pallidus
UNIPROT: C0SSE7
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: Aeribacillus pallidus
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
l-fucose isomerase, fucose isomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-Fucose isomerase
D-arabinose isomerase, bifunctional enzyme
D-Arabinose (L-Fucose) isomerase
-
-
-
-
D-Arabinose isomerase
-
-
-
-
Fucose isomerase
-
-
-
-
Isomerase, L-fucose
-
-
-
-
L-fucose ketol-isomerase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-fucose aldose-ketose-isomerase
Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+). The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism [3]. The enzyme from Escherichia coli can also convert D-arabinose to D-ribulose [1]. The enzyme from the thermophilic bacterium Caldicellulosiruptor saccharolyticus also converts D-altrose to D-psicose and L-galactose to L-tagatose [4].
CAS REGISTRY NUMBER
COMMENTARY hide
60063-83-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Fucose
L-Fuculose
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
L-Fucose
L-Fuculose
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C0SSE7_9BACI
595
0
66237
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
three X-ray structures of D-arabinose isomerase in complexes with 2-methyl-2,4-pentadiol, glycerol and L-fucitol are determined at resolutions of 1.77, 1.60 and 2.60 A, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using an anion-exchange column, Q Sepharose high performance, a hydrophobic interaction column, RESOURCE PHE, and an anion-exchange column, RESOURCE Q
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
for over-expression in Escherichia coli JM109 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takeda, K.; Yoshida, H.; Izumori, K.; Kamitori, S.
X-ray structures of Bacillus pallidus D-arabinose isomerase and its complex with L-fucitol
Biochim. Biophys. Acta
1804
1359-1368
2010
Aeribacillus pallidus (C0SSE7), Aeribacillus pallidus
Manually annotated by BRENDA team