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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 5.1.3.29 - L-fucose mutarotase and Organism(s) Escherichia coli and UniProt Accession P0AEN8

for references in articles please use BRENDA:EC5.1.3.29
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.29 L-fucose mutarotase
IUBMB Comments
This enzyme shows no 1-epimerase activity with D-glucose, L-rhamnose and D-fucose (cf. EC 5.1.3.3, aldose 1-epimerase) .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0AEN8
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
spfcsu, l-fucose mutarotase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -
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].
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
?
-
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
alpha-L-fucopyranose
beta-L-fucopyranose
show the reaction diagram
-
-
-
r
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27.9
alpha-L-fucopyranose
pH 7.5, temperature not specified in the publication
65.1
beta-L-fucopyranose
pH 7.5, temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
crystallograpic data, FucU forms a decameric toroid with each active site formed by two adjacent subunits
additional information
FucU seems to require multimeric or dimeric structures for its enzymatic activity, because the N-terminally His-tagged FucU is an inactive monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of in complex with L-fucose
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D64N
binding affinity of mutant enzyme is similar to that of wild-type enzyme
H22A
binding affinity of mutant enzyme is similar to that of wild-type enzyme
Y111F
reduced binding affinity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ryu, K.S.; Kim, C.; Kim, I.; Yoo, S.; Choi, B.S.; Park, C.
NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration
J. Biol. Chem.
279
25544-25548
2004
Escherichia coli (P0AEN8)
Manually annotated by BRENDA team
Lee, K.H.; Ryu, K.S.; Kim, M.S.; Suh, H.Y.; Ku, B.; Song, Y.L.; Ko, S.; Lee, W., Oh, B.H.
Crystal structures and enzyme mechanisms of a dual fucose mutarotase/ribose pyranase
J. Mol. Biol.
391
178-191
2009
Escherichia coli (P0AEN8), Mus musculus (Q8R2K1)
Manually annotated by BRENDA team