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Information on EC 5.4.99.59 - dTDP-fucopyranose mutase and Organism(s) Escherichia coli and UniProt Accession Q6E7F1

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.59 dTDP-fucopyranose mutase
IUBMB Comments
The enzyme is involved in the biosynthesis of the Escherichia coli O52 O antigen.
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This record set is specific for:
Escherichia coli
UNIPROT: Q6E7F1
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
Fcf2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
dTDP-alpha-D-fucopyranose furanomutase
The enzyme is involved in the biosynthesis of the Escherichia coli O52 O antigen.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dTDP-alpha-D-fucopyranose
dTDP-beta-D-fuco-(1->4)-furanose
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
dTDP-alpha-D-fucopyranose
dTDP-beta-D-fuco-(1->4)-furanose
show the reaction diagram
the enzyme is involved in the biosynthesis of dTDP-D-fucofuranose, a component of the Escherichia coli O52 O antigen
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Fcf2 is an divalent cation-independent enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
5 mM, complete inhibition
Mn2+
5 mM, 43% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.43
dTDP-alpha-D-fucopyranose
pH 7.4, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.056
dTDP-alpha-D-fucopyranose
pH 7.4, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
dTDP-alpha-D-fucopyranose
pH 7.4, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 50
4°C: 17% of maximal activity, 50°C: 49% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutant strains H1863 lacking fcf2. The mutant strain produces semirough lipopolysaccharide with only one O unit attached to the core-lipid A moiety while the wild type strain produces normal lipopolysaccharide. The result indicates that fcf2 is required for the synthesis of the O antigen in Escherichia coli O52
physiological function
the enzyme is involved in the biosynthesis of dTDP-D-fucofuranose, a component of the Escherichia coli O52 O antigen
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FCF2_ECOLX
377
0
44195
Swiss-Prot
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 50% glycerol, stable for at least 2 months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His6-tagged fusion protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, Q.; Ding, P.; Perepelov, A.V.; Xu, Y.; Wang, Y.; Knirel, Y.A.; Wang, L.; Feng, L.
Characterization of the dTDP-D-fucofuranose biosynthetic pathway in Escherichia coli O52
Mol. Microbiol.
70
1358-1367
2008
Escherichia coli (Q6E7F1), Escherichia coli O52 (Q6E7F1)
Manually annotated by BRENDA team