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Information on EC 1.1.1.271 - GDP-L-fucose synthase and Organism(s) Escherichia coli and UniProt Accession P32055

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     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.271 GDP-L-fucose synthase
IUBMB Comments
Both human and Escherichia coli enzymes can use NADH in place of NADPH to a slight extent.
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This record set is specific for:
Escherichia coli
UNIPROT: P32055
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
tsta3, fx protein, gdp-l-fucose synthase, gdp-fucose synthetase, transplantation antigen p35b, gdp-4-keto-6-deoxy-d-mannose epimerase/reductase, gdp-fucose synthase, gdp-4-keto-6-deoxy-d-mannose-3,5-epimerase-4-reductase, gdp-4-keto-6-deoxymannose-3,5-epimerase-4-reductase, gdp-keto-6-deoxymannose 3,5-epimerase/4-reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GDP-4-keto-6-deoxy-D-mannose epimerase/reductase
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GDP-4-keto-6-deoxymannose-3,5-epimerase-4-reductase
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GDP-fucose synthase
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FX protein
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-
-
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GDP-4-keto-6-D-deoxymannose epimerase-reductase
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-
-
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GDP-4-keto-6-deoxy-D-mannose epimerase-reductase
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-
-
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GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase
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-
-
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GDP-4-keto-6-deoxymannose 3,5-epimerase 4-reductase
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-
-
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GDP-4-keto-6-deoxymannose epimerase-reductase
-
-
-
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GDP-fucose synthetase
-
-
-
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GDP-L-fucose synthetase
-
-
-
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guanosine diphosphofucose synthetase
-
-
-
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Red cell NADP(H)-binding protein
-
-
-
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Transplantation antigen P35B
-
-
-
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Tum-P35B antigen
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
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-
-
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reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:NADP+ 4-oxidoreductase (3,5-epimerizing)
Both human and Escherichia coli enzymes can use NADH in place of NADPH to a slight extent.
CAS REGISTRY NUMBER
COMMENTARY hide
113756-18-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GDP-4-dehydro-alpha-D-rhamnose + NADPH + H+
GDP-beta-L-fucose + NADP+
show the reaction diagram
-
-
-
?
GDP-4-keto-6-deoxy-D-mannose + NADPH + H+
GDP-L-fucose + NADP+
show the reaction diagram
-
-
-
?
GDP-4-dehydro-6-deoxy-alpha-D-mannose + NADH + H+
GDP-beta-L-fucose + NAD+
show the reaction diagram
-
-
-
-
r
GDP-4-keto-6-deoxy-D-mannose + NADPH
GDP-6-deoxy-L-galactose + NADP+
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
GDP-4-dehydro-alpha-D-rhamnose + NADPH + H+
GDP-beta-L-fucose + NADP+
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
enzyme has lower affinity for NADH as compared with NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GDP
-
competitive with respect to GDP-4-keto-6-deoxymannose
GDP-fucose
-
competitive with respect to NADPH and GDP-4-keto-6-deoxymannose
NADP
-
competitive inhibitor
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.109
NADH
-
-
0.009
NADPH
-
-
additional information
additional information
-
Km values for various mutants
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
values for various mutants
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.061
GDP
-
-
0.055
GDP-fucose
-
-
0.069
NADP+
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
-
2 * 34000
35000 - 36000
-
SDS-PAGE
40000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 34000
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method, complexed with NADP+
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C109S
active site mutant, produces GDP-6-deoxy-D-altrose as its major product (75%) besides GDP-L-fucose (25%) out of GDP-4-keto-6-deoxy-D-mannose
H179Q
the mutant catalyzes isotope exchange into starting material indicates that its active site has not been dramatically perturbed and it is still able to bind substrate and catalyze deprotonation events
C109A
-
lower Km than wild-type enzyme
H179N
-
lower Km than wild-type enzyme
K140R
-
higher Km than wild-type enzyme
K140S
-
higher Km than wild-type enzyme
R187A
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lower Km than wild-type enzyme
S107A
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lower Km than wild-type enzyme
Y136E
-
no enzymatic activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
wild type enzyme is stable for several weeks in phosphate buffered saline at concentrations higher than 10 mg/ml, stability of mutants differ from wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
four genes (manB, manC, gmd, and wcaG) cloned from Escherichia coli are expressed in Lactococcus lactis
expressed in Saccharomyces cerevisiae
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
four genes (manB, manC, gmd, and wcaG) cloned from Escherichia coli are expressed in Lactococcus lactis. The one-pot reaction of ManB, ManC, Gmd, and WcaG with mannose-6-P results in the successful production of GDP-L-fucose
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mattila, P.; Rabina, J.; Hortling, S.; Helin, J.; Renkonen, R.
Functional expression of Escherichia coli enzymes synthesizing GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces cerevisiae
Glycobiology
10
1041-1047
2000
Escherichia coli
Manually annotated by BRENDA team
Menon, S.; Stahl, M.; Kumar, R.; Xu, G.Y.; Sullivan, F.
Stereochemical course and steady state mechanism of the reaction catalyzed by the GDP-fucose synthetase from Escherichia coli
J. Biol. Chem.
274
26743-26750
1999
Escherichia coli
Manually annotated by BRENDA team
Rizzi, M.; Tonetti, M.; Vigevani, P.; Sturla, L.; Bisso, A.; De Flora, A.; Bordo, D.; Bolognesi, M.
GDP-4-keto-6-deoxy-D-mannose epimerase/reductase from Escherichia coli, a key enzyme in the biosynthesis of GDP-L-fucose, displays the structural characteristics of the RED protein homology superfamily
Structure
6
1453-1465
1998
Escherichia coli
Manually annotated by BRENDA team
Rosano, C.; Bisso, A.; Izzo, G.; Tonetti, M.; Sturla, L.; De Flora, A.; Bolognesi, M.
Probing the catalytic mechanism of GDP-4-keto-6-deoxy-D-mannose epimerase/reductase by kinetic and crystallographic characterization of site-specific mutants
J. Mol. Biol.
303
77-91
2000
Escherichia coli
Manually annotated by BRENDA team
Lau, S.T.; Tanner, M.E.
Mechanism and active site residues of GDP-fucose synthase
J. Am. Chem. Soc.
130
17593-17602
2008
Escherichia coli K-12, Escherichia coli (P32055)
Manually annotated by BRENDA team
Li, L.; Kim, S.; Heo, J.; Kim, T.; Seo, J.; Han, N.
One-pot synthesis of GDP-L-fucose by a four-enzyme cascade expressed in Lactococcus lactis
J. Biotechnol.
264
1-7
2017
Escherichia coli (P32055), Escherichia coli K12 (P32055)
Manually annotated by BRENDA team