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Information on EC 5.3.1.25 - L-fucose isomerase and Organism(s) Escherichia coli and UniProt Accession P69922

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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 .
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Escherichia coli
UNIPROT: P69922
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
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
D-Arabinose (L-Fucose) isomerase
-
-
-
-
D-Arabinose isomerase
-
-
-
-
Fucose isomerase
-
-
-
-
Isomerase, L-fucose
-
-
-
-
L-fucose ketol-isomerase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-fucopyranose = L-fuculose
show the reaction diagram
protein environment suggests strongly that the reaction belongs to the ene-diol type
-
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
D-Arabinose
?
show the reaction diagram
D-arabinose
D-ribulose
show the reaction diagram
-
-
-
-
?
L-Fucose
?
show the reaction diagram
-
enzyme of the metabolic pathway of L-fucose
-
-
?
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
D-Arabinose
?
show the reaction diagram
L-Fucose
?
show the reaction diagram
-
enzyme of the metabolic pathway of L-fucose
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
stimulates
Mn2+
-
stimulates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dulcitol
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-
L-arabitol
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ribitol
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sorbitol
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
170 - 280
D-arabinose
42 - 45
L-fucose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
63.3
-
Escherichia coli K-12
63.7
-
Escherichia coli B/r
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
-
7.0: sharp decrease in activity below, 8.0-10.0: maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
L-fucose induced culture of strain K-12 and D-arabinose-induced culture of strain B/r
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
342000
-
strain B/r, high-speed equilibrium sedimentation
355000
-
strain K-12, high-speed equilibrium sedimentation
390000
-
-
64976
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6 * 64976, crystallographic data
84600
-
4 * 84600, Escherichia coli B/r, high speed sedimentation of enzyme dissociated into subunits by protonation at pH 2 or dialysis against buffer containing 8 M urea
90900
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4 * 90900, Escherichia coli K-12, high speed sedimentation of enzyme dissociated into subunits by protonation at pH 2 or dialysis against buffer containing 8 M urea
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
6 * 64976, crystallographic data
tetramer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
nucleotide sequence of the gene fucI
-
organization of the fuc regulon specifying L-fucose dissimilation as determined by gene cloning
-
overexpression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
two-step enzymatic strategy for the synthesis of 6-deoxy-L-sorbose. First, the isomerization of L-fucose to L-fuculose,and the epimerization of L-fuculose to 6-deoxy-L-sorbose catalyzed by D-tagatose 3-epimerase are coupled with the targeted phosphorylation of 6-deoxy-L-sorbose by human fructose kinase in a one-pot reaction. In the second reaction step, the phosphate group of the 6-deoxy-L-sorbose 1-phosphate is hydrolyzed with acid phosphatase to produce 6-deoxy-L-sorbose in 81% yield with regard to L-fucose
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Garcia-Junceda, E.; Shen, G.J.; Alajarin, R.; Wong, C.H.
Cloning and overexpression of rhamnose isomerase and fucose isomerase
Bioorg. Med. Chem.
3
1349-1355
1995
Escherichia coli
Manually annotated by BRENDA team
Boulter, J.R.; Gielow, W.O.
Properties of D-arabinose isomerase purified from two strains of Escherichia coli
J. Bacteriol.
113
687-696
1973
Escherichia coli, Escherichia coli B/r
Manually annotated by BRENDA team
Bartkus, J.M.; Mortlock, R.P.
Isolation of a mutation resulting in constitutive synthesis of L-fucose catabolic enzymes
J. Bacteriol.
165
710-714
1986
Escherichia coli
Manually annotated by BRENDA team
Seemann, J.E.; Schulz, G.E.
Structure and mechanism of L-fucose isomerase from Escherichia coli
J. Mol. Biol.
273
256-268
1997
Escherichia coli
Manually annotated by BRENDA team
LeBlanc D.J.; Mortlock, R.P.
Metabolism of D-arabinose: a new pathway in Escherichia coli
J. Bacteriol.
106
90-96
1971
Escherichia coli
Manually annotated by BRENDA team
Lu, Z.; Lin, E.C.C.
The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation
Nucleic Acids Res.
17
4883-4884
1989
Escherichia coli
Manually annotated by BRENDA team
Chen, Y.M.; Zhu, Y.; Lin, E.C.C.
The organization of the fuc regulon specifying L-fucose dissimilation in Escherichia coli K12 as determined by gene cloning
Mol. Gen. Genet.
210
331-337
1987
Escherichia coli
Manually annotated by BRENDA team
Wen, L.; Huang, K.; Zheng, Y.; Liu, Y.; Zhu, H.; Wang, P.
A two-step strategy for the preparation of 6-deoxy-L-sorbose
Bioorg. Med. Chem. Lett.
26
4358-4361
2016
Escherichia coli (P69922)
Manually annotated by BRENDA team