Information on EC 5.1.3.29 - L-fucose mutarotase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
5.1.3.29
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RECOMMENDED NAME
GeneOntology No.
L-fucose mutarotase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-L-fucopyranose = beta-L-fucopyranose
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fucose degradation
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SYSTEMATIC NAME
IUBMB Comments
L-fucose 1-epimerase
This enzyme shows no 1-epimerase activity with D-glucose, L-rhamnose and D-fucose (cf. EC 5.1.3.3, aldose 1-epimerase) [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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reduced level of anteroventral periventricular nucleus in FucM-/- mouse, presumably resulting from the reduced fucosylation, is responsible for the male-like sexual behavior observed in the FucM knock-out female mouse
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-L-fucopyranose
beta-L-fucopyranose
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-L-fucopyranose
beta-L-fucopyranose
show the reaction diagram
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27.9
alpha-L-fucopyranose
Escherichia coli
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pH 7.5, temperature not specified in the publication
9520
65.1
beta-L-fucopyranose
Escherichia coli
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pH 7.5, temperature not specified in the publication
90054
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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marginal expression
Manually annotated by BRENDA team
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marginal expression
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of in complex with L-fucose
hanging-drop vapour diffusion at 18°C, enzyme in complex with L-fucose. The structure shows a complex decameric quaternary structure
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli, cloned into pcDNA3.1 plasmid and transfected into HepG2 cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D64N
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binding affinity of mutant enzyme is similar to that of wild-type enzyme
H22A
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binding affinity of mutant enzyme is similar to that of wild-type enzyme
Y111F
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reduced binding affinity
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