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Information on EC 2.7.7.30 - fucose-1-phosphate guanylyltransferase
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2.7.7.30 fucose-1-phosphate guanylyltransferaseSpecify your search results
Word Map
- 2.7.7.30
-
fucosylated
-
salvage
- glycans
- glycolipids
-
fucosyltransferase
- monosaccharide
- synthesis
- gdp-beta-l-fucose
- fragilis
- polysaccharides
-
nucleotide-sugars
-
bacteroides
-
lewis
-
n-linked
- gdp-d-mannose
- xyloglucans
-
fucose-containing
-
sialyl
- glycoconjugates
-
rhamnogalacturonan-ii
-
boric
-
photoaffinity
-
pectic
-
chemoenzymatic
-
alpha1,3
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
gdp-l-fucose pyrophosphorylase, atfkgp, gdp-l-fuc pyrophosphorylase, l-fucokinase/gdp-fucose pyrophosphorylase, gdp-fucose pyrophosphorylase, gdp-l-fucose pyrophosphorylase (fpgt), gtp fucose pyrophosphorylase (gfpp), gdp-l-fucose-synthesizing enzymes, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtFKGP
-
bifunctional enzyme with L-fucokinase and GDP-L-Fuc pyrophosphorylase
FKP
GDP-fucose pyrophosphorylase
GDP-L-Fuc pyrophosphorylase
GDP-L-fucose pyrophosphorylase
GDP-L-fucose-synthesizing enzymes
GDPfucose pyrophosphorylase
-
-
-
-
GFPP
guanosine diphosphate L-fucose pyrophosphorylase
-
-
-
-
FKP
-
bifunctional enzyme with fucokinase and GDP-L-fucose pyrophosphorylase activities
FKP
-
bifunctional enzyme with L-fucokinase and GDP-fucose pyrophosphorylase activities
FKP
-
bifunctional enzyme with L-fucokinase and guanosine 5'-diphosphate-L-fucose pyrophosphorylase activities
FKP
-
bifunctional enzyme with L-fucokinase and GDP-fucose pyrophosphorylase activities
-
GDP-fucose pyrophosphorylase
-
-
-
-
GDP-L-fucose pyrophosphorylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + beta-L-fucose 1-phosphate = diphosphate + GDP-L-fucose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
nucleotidyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
GTP:beta-L-fucose-1-phosphate guanylyltransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9033-14-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-6-chloropurine-beta-D-riboside 5'-triphosphate + L-fucose 1-phosphate
diphosphate + 2-amino-6-chloropurine-beta-D-riboside 5'-(alpha-L-fucosyl)diphosphate
-
-
-
-
?
2-aminoadenosine triphosphate + L-fucose 1-phosphate
diphosphate + (2-aminoadenosine diphosphate)-L-fucose
-
-
-
-
?
7-deazaguanosine triphosphate + L-fucose 1-phosphate
diphosphate + (7-deazaguanosine diphosphate)-L-fucose
-
-
-
-
?
8-oxoguanosine triphosphate + L-fucose 1-phosphate
diphosphate + (8-oxoguanosine diphosphate)-L-fucose
-
-
-
-
?
GTP + 6,7-dideoxy-beta-L-galacto-hept-6-enopyranose 1-phosphate
GDP-6,7-dideoxy-beta-L-galacto-hept-6-enopyranose + diphosphate
-
-
-
-
?
GTP + 6-azido-6-deoxy-beta-L-galactopyranose 1-phosphate
GDP-6-azido-6-deoxy-beta-L-galactopyranose + diphosphate
-
-
-
-
?
GTP + 6-deoxy-6-fluoro-beta-L-galactopyranose 1-phosphate
GDP-6-deoxy-6-fluoro-beta-L-galactopyranose + diphosphate
-
-
-
-
?
GTP + 6-O-methyl-beta-L-galactopyranose 1-phosphate
GDP-6-O-methyl-beta-L-galactopyranose + diphosphate
-
-
-
-
?
GTP + alpha-D-(5-cyano)arabinopyranose 1-phosphate
GDP-alpha-D-(5-cyano)arabinopyranose + diphosphate
-
-
-
-
?
GTP + alpha-D-mannose 1-phosphate
diphosphate + GDP-alpha-D-mannopyranose
-
17.5% of activity with GDP-L-fucose
-
?
GTP + beta-L-galactopyranose 1-phosphate
GDP-beta-L-galactopyranose + diphosphate
-
-
-
-
?
GTP + D-arabinose 1-phosphate
GDP-D-arabinopyranoside + diphosphate
-
5-10% of activity with L-fucose
-
?
N1-methylguanosine triphosphate + L-fucose 1-phosphate
diphosphate + (N1-methylguanosine diphosphate)-L-fucose
-
-
-
-
?
N2-methylguanosine triphosphate + L-fucose 1-phosphate
diphosphate + (N2-methylguanosine diphosphate)-L-fucose
-
-
-
-
?
O6-methylguanosine triphosphate + L-fucose 1-phosphate
diphosphate + (O6-methylguanosine diphosphate)-L-fucose
-
-
-
-
?
tricyclic guanosine triphosphate + L-fucose 1-phosphate
diphosphate + (tricyclic guanosine diphosphate)-L-fucose
-
-
-
-
?
UTP + L-fucose 1-phosphate
diphosphate + UDP-L-fucose
-
18.7% of activity with GTP
-
?
xanthosine triphosphate + L-fucose 1-phosphate
diphosphate + (xanthosine diphosphate)-L-fucose
-
-
-
-
?
ATP + L-fucose 1-phosphate
diphosphate + ADP-L-fucose
-
approx. 50% of activity with
-
?
GTP + alpha-D-arabinopyranose 1-phosphate
GDP-alpha-D-arabinopyranose + diphosphate
-
-
-
-
?
GTP + alpha-D-arabinopyranose 1-phosphate
GDP-alpha-D-arabinopyranose + diphosphate
-
-
-
?
GTP + alpha-D-arabinopyranose 1-phosphate
GDP-alpha-D-arabinopyranose + diphosphate
-
-
-
?
GTP + beta-L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
-
-
-
?
GTP + beta-L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
-
-
-
r
GTP + beta-L-fucose 1-phosphate
GDP-L-fucose + diphosphate
-
-
-
?
GTP + beta-L-fucose 1-phosphate
GDP-L-fucose + diphosphate
-
-
-
?
GTP + L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
the monosaccharide L-fucose is found as a constituent of cell wall polysaccharides and sugar moieties of glycoproteins and has important physiological functions in seed plants
-
-
?
GTP + L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
strict substrate specificity, no activity with L-Ara-1-P, Gal-1-P, Glc-1-P, Man-1-P, Xyl-1-P, GlcA-1-P, and Glc-NAc-1-P as glycosyl donor, and it uses specifically GTP as the nucleotide donor
-
-
?
GTP + L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
the enzyme is involved in the salvage pathway of GDP-L-fucose
-
-
?
GTP + L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
specific for GTP
-
r
GTP + L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
pathway of fucose production, an important component of complex heterooligosaccharides
-
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + beta-L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
-
-
-
?
GTP + beta-L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
-
-
-
r
GTP + L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
the monosaccharide L-fucose is found as a constituent of cell wall polysaccharides and sugar moieties of glycoproteins and has important physiological functions in seed plants
-
-
?
GTP + L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
the enzyme is involved in the salvage pathway of GDP-L-fucose
-
-
?
GTP + L-fucose 1-phosphate
diphosphate + GDP-L-fucose
-
pathway of fucose production, an important component of complex heterooligosaccharides
-
r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
additional information
Mg2+
-
maximum activity at 4 mM. No activity can be detected when the Mg2+ concentration is below 1 nM
Mn2+
-
has only a poor effect on the GDP-L-Fuc pyrophosphorylase activity of rAtFKGP compared with Mg2+
additional information
-
requires the presence of divalent metal cations at the active site
additional information
-
K+, Mn2+, Co2+, Ca2+, Cu2+, Zn2+, Ni2+, Hg2+, and Fe2+ have little effect on the enzyme activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diphosphate
-
addition of diphosphate strongly inhibits the formation of GDP-L-Fuc by rAtFKGPi
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Neoplasms
Differential gene expression of GDP-L-fucose-synthesizing enzymes, GDP-fucose transporter and fucosyltransferase VII.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
ATP
pH not specified in the publication, temperature not specified in the publication
0.2
GTP
pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.22
ATP
pH not specified in the publication, temperature not specified in the publication
1.55
GTP
pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9.5
-
approx. 85% of maximal activity at pH 6.0, approx. 70% of maximal activity at pH 9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
mature plant, relatively high expression of AtFKGP mRNA
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FKGP_ARATH
1055
0
116351
Swiss-Prot
Mitochondrion (Reliability: 2)
FPGT_HUMAN
607
0
68010
Swiss-Prot
Mitochondrion (Reliability: 2)
FPGT_MOUSE
590
0
65362
Swiss-Prot
Mitochondrion (Reliability: 4)
K9M5T4_9CETA
486
0
54624
TrEMBL
other Location (Reliability: 5)
A0A6B9LZK3_CAPPY
243
0
26763
TrEMBL
other Location (Reliability: 1)
A0A6B9LQX9_CAPPY
243
0
26763
TrEMBL
other Location (Reliability: 1)
B5X3U7_SALSA
576
0
63670
TrEMBL
other Location (Reliability: 2)
B7PV57_IXOSC
307
0
33910
TrEMBL
other Location (Reliability: 2)
A0A6B9M1T2_CAPCA
243
0
26777
TrEMBL
other Location (Reliability: 1)
A0A812D550_SEPPH
459
7
53720
TrEMBL
other Location (Reliability: 2)
A0A8M1N6G7_DANRE
573
0
64102
TrEMBL
other Location (Reliability: 2)
A0A1R7T311_MORAP
608
0
67025
TrEMBL
other Location (Reliability: 2)
K9M701_CAPCA
486
0
54490
TrEMBL
other Location (Reliability: 5)
A0A2G9I475_9LAMI
1077
0
118295
TrEMBL
Mitochondrion (Reliability: 2)
A0A1B8Y0M8_XENTR
583
0
63821
TrEMBL
other Location (Reliability: 4)
A0A6J8BJC4_MYTCO
603
0
67705
TrEMBL
other Location (Reliability: 1)
K9M690_CAPPY
486
0
54497
TrEMBL
other Location (Reliability: 5)
A0A8B6BGU2_MYTGA
603
0
67771
TrEMBL
other Location (Reliability: 2)
A0A6B9M499_CAPCA
243
0
26747
TrEMBL
other Location (Reliability: 1)
A0A6B9LSQ0_CAPCA
243
0
26704
TrEMBL
other Location (Reliability: 1)
A0A6B9LSZ0_CAPPY
243
0
26749
TrEMBL
other Location (Reliability: 1)
A0A2U3KM12_9BACT
564
0
60340
TrEMBL
-
Q58T34_BACFG
949
0
105660
TrEMBL
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.6 A resolution. Space group P41212, a single enzyme monomer per asymmetric unit
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A723R
-
the mutant shows about 75% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
D594A
-
the mutant shows about 55% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
D601A
-
the mutant shows about 40% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
D762A
-
the mutant shows about 85% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
G597A
-
the mutant shows about 20% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
G598A
-
the mutant shows about 90% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
G713A
-
the mutant shows about 125% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
G715A
-
the mutant shows wild type GDP-fucose pyrophosphorylase activity
G717A
-
the mutant shows wild type GDP-fucose pyrophosphorylase activity
G757A
-
the mutant shows wild type GDP-fucose pyrophosphorylase activity
G758A
-
the mutant shows wild type GDP-fucose pyrophosphorylase activity
G759A
-
the mutant shows about 85% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
G75A
-
the mutant shows about 60% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
G76A
-
the mutant almost completely loses its GDP-fucose pyrophosphorylase activity
G88A
-
the mutant almost completely loses its GDP-fucose pyrophosphorylase activity
G899A
-
the mutant shows about 90% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
G901A
-
the mutant shows about 87% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
G902A
-
the mutant shows about 80% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
H73A
-
the mutant shows about 40% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
I721A
-
the mutant shows about 90% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
K89A
-
the mutant almost completely loses its GDP-fucose pyrophosphorylase activity
L722A
-
the mutant shows about 120% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
P711A
-
the mutant shows about 120% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
R592A
-
the mutant shows about 110% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
R80A
-
the mutant almost completely loses its GDP-fucose pyrophosphorylase activity
R82A
-
the mutant shows about 50% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
S714A
-
the mutant shows about 130% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
S719A
-
the mutant shows about 90% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
S720A
-
the mutant shows about 75% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
S78A
-
the mutant shows about 80% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
T602A
-
the mutant shows about 90% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
T718A
-
the mutant shows wild type GDP-fucose pyrophosphorylase activity
G75A
-
the mutant shows about 60% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
-
H73A
-
the mutant shows about 40% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
-
K89A
-
the mutant almost completely loses its GDP-fucose pyrophosphorylase activity
-
R80A
-
the mutant almost completely loses its GDP-fucose pyrophosphorylase activity
-
R82A
-
the mutant shows about 50% GDP-fucose pyrophosphorylase activity compared to the wild type enzyme
-
D184A
-
the ratio of turnover number to Km-value (for GTP) is 1.02fold higher than the wild-type ratio
D299A
-
the ratio of turnover number to Km-value (for GTP) is 1.04fold higher than the wild-type ratio
D427A
-
the ratio of turnover number to Km-value (for GTP) is 1.06fold lower than the wild-type ratio
D77A
-
the ratio of turnover number to Km-value (for GTP) is 16600fold lower than the wild-type ratio
E289A
-
the ratio of turnover number to Km-value (for GTP) is 1.1fold lower than the wild-type ratio
E297A
-
the ratio of turnover number to Km-value (for GTP) is 19.5fold lower than the wild-type ratio
E297A/E432A
-
the ratio of turnover number to Km-value (for GTP) is 24900fold lower than the wild-type ratio
E432A
-
the ratio of turnover number to Km-value (for GTP) is 113fold lower than the wild-type ratio
E566A
-
the ratio of turnover number to Km-value (for GTP) is 1.06fold higher than the wild-type ratio
E574A
-
the ratio of turnover number to Km-value (for GTP) is 1.05fold lower than the wild-type ratio
K478A
-
the ratio of turnover number to Km-value (for GTP) is 1.13fold lower than the wild-type ratio
K479A
-
the ratio of turnover number to Km-value (for GTP) is 1.15fold lower than the wild-type ratio
K482A
-
the ratio of turnover number to Km-value (for GTP) is 166fold lower than the wild-type ratio
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 12
-
less than 30% enzyme activity is retained after incubation at pH 3.0 and pH 12.0 at 4°C for 2 h
762385
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12 - 50
-
the enzyme retains 40% of its initial activity after 1.5 h of exposure at 12°C, and loses more than 50% of its initial activity after 1 h of exposure at 20°C, 28°C and 37°C. The enzyme loses nearly 100% of its activity after 30 min of exposure above 50°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% (w/v) glycerol, 1 mM PMSF, 0.2 M NaCl, 50 mM Tris-HCl buffer, pH 7.5, 1 month, no loss of activity
-
-20°C, recombinant protein with maltose-binding protein affinity tag, stable for at least three months
4°C, 1mM PMSF, 0.2 M NaCl, 50 mM Tris-HCl buffer, pH 7.5, 1 day, loss of more than 50% activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
polyethylene glycol, DE-52, Phenyl-Sepharose, hydroxylapatite, Sephacryl S-300, Red-Sepharose, chromatofocusing
-
protamine sulfate, ammonium sulfate, calcium phosphate gel, Sephadex G-100, DEAE-cellulose, alumina C-gamma
-
Sepharose FF column, the recombinant protein fused to thioredoxin and His tags is partially purified by chelating chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of cDNA in murine myeloma cell line, i.e. NSO cells, and in Sf9 cells
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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a chemoenzymatic model for the preparative-scale synthesis of a diverse array of GDP-fucose derivatives is reported
synthesis
functional expression of enzyme gene in Saccharomyces cerevisiae. The yeast cells synthesize GDP-L-fucose or GDP-D-arabinose upon exogenous addition of L-fucose or D-arabinose, respectively
synthesis
engineering of Escherichia coli for efficient production of 2'-fucosyllactose by introduction of the fkp gene coding for fucokinase/GDP-L-fucose diphosphorylase from Bacteroides fragilis and the fucT2 gene encoding alpha-1,2-fucosyltransferase from Helicobacter pylori to produce 2'-fucosyllactose from fucose, lactose and glycerol. The yield and productivity are further improved by deletion of the fucI-fucK gene cluster coding for fucose isomerase and fuculose kinase. Fed-batch fermentation of the final strain results in 23.1 g/l of extracellular 2'-fucosyllactose and a productivity of 0.39 g/l/h
synthesis
-
functional expression of enzyme gene in Saccharomyces cerevisiae. The yeast cells synthesize GDP-L-fucose or GDP-D-arabinose upon exogenous addition of L-fucose or D-arabinose, respectively
-
synthesis
-
engineering of Escherichia coli for efficient production of 2'-fucosyllactose by introduction of the fkp gene coding for fucokinase/GDP-L-fucose diphosphorylase from Bacteroides fragilis and the fucT2 gene encoding alpha-1,2-fucosyltransferase from Helicobacter pylori to produce 2'-fucosyllactose from fucose, lactose and glycerol. The yield and productivity are further improved by deletion of the fucI-fucK gene cluster coding for fucose isomerase and fuculose kinase. Fed-batch fermentation of the final strain results in 23.1 g/l of extracellular 2'-fucosyllactose and a productivity of 0.39 g/l/h
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ishihara, H.; Heath, E.C.
The metabolism of L-fucose. IV. The biosynthesis of guanosine diphosphate L-fucose in porcine liver
J. Biol. Chem.
243
1110-1115
1968
Sus scrofa
brenda
Coates, S.W.; Gurney, T.; Sommers, L.W.; Yeh, M.; Hirschberg, C.B.
Subcellular localization of sugar nucleotide synthetases
J. Biol. Chem.
255
9225-9229
1980
Mus musculus
brenda
Stiller, R.; Thiem, J.
Enzymatic synthesis of beta-L-fucose-1-phosphate and GDP-fucose
Liebigs Ann. Chem.
1992
461-466
1992
Sus scrofa
-
brenda
Pastuszak, I.; Ketchum, C.; Hermanson, G.; Sjoberg, E.J.; Drake, R.; Elbein, A.D.
GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme
J. Biol. Chem.
273
30165-30174
1998
Cricetulus griseus, Sus scrofa, Homo sapiens (O14772), Homo sapiens
brenda
Druzhinina, T.N.; Utkina, N.S.; Chan, K.; Strecker, G.; Shibaev, V.N.
Activity of enzymes catalyzing formation of b-L-fucosyl phosphate and GDP-b-L-fucose in amphibian tissues and their application in chemo-enzymic synthesis of GDP-b-L-fucose
Biochemistry (Moscow)
64
783-787
1999
Bufo bufo, Pleurodeles waltl
brenda
Quirk, S.; Seley, K.L.
Substrate discrimination by the human GTP fucose pyrophosphorylase
Biochemistry
44
10854-10863
2005
Homo sapiens
brenda
Quirk, S.; Seley, K.L.
Identification of catalytic amino acids in the human GTP fucose pyrophosphorylase active site
Biochemistry
44
13172-13178
2005
Homo sapiens
brenda
Niittymaki, J.; Mattila, P.; Roos, C.; Huopaniemi, L.; Sjoblom, S.; Renkonen, R.
Cloning and expression of murine enzymes involved in the salvage pathway of GDP-L-fucose
Eur. J. Biochem.
271
78-86
2004
Mus musculus
brenda
Niittymaki, J.; Mattila, P.; Renkonen, R.
Differential gene expression of GDP-L-fucose-synthesizing enzymes, GDP-fucose transporter and fucosyltransferase VII
APMIS
114
539-548
2006
Mus musculus, Rattus norvegicus
brenda
Quirk, S.; Seley-Radtke, K.L.
Purification, crystallization and preliminary X-ray characterization of the human GTP fucose pyrophosphorylase
Acta Crystallogr. Sect. F
62
392-394
2006
Homo sapiens
brenda
Moriwaki, K.; Noda, K.; Nakagawa, T.; Asahi, M.; Yoshihara, H.; Taniguchi, N.; Hayashi, N.; Miyoshi, E.
A high expression of GDP-fucose transporter in hepatocellular carcinoma is a key factor for increases in fucosylation
Glycobiology
17
1311-1320
2007
Homo sapiens
brenda
Kotake, T.; Hojo, S.; Tajima, N.; Matsuoka, K.; Koyama, T.; Tsumuraya, Y.
A bifunctional enzyme with L-fucokinase and GDP-L-fucose pyrophosphorylase activities salvages free L-fucose in Arabidopsis
J. Biol. Chem.
283
8125-8135
2008
Arabidopsis thaliana
brenda
Wang, W.; Hu, T.; Frantom, P.A.; Zheng, T.; Gerwe, B.; Del Amo, D.S.; Garret, S.; Seidel, R.D.; Wu, P.
Chemoenzymatic synthesis of GDP-L-fucose and the Lewis X glycan derivatives
Proc. Natl. Acad. Sci. USA
106
16096-16101
2009
Bacteroides fragilis
brenda
Quirk, S.
Crystallization and preliminary X-ray characterization of the Vitis vinifera fucokinase:GDP-fucose pyrophosphorylase
Acta Crystallogr. Sect. F
68
1109-1112
2012
Vitis vinifera (D7UCW9)
brenda
Liu, T.W.; Ito, H.; Chiba, Y.; Kubota, T.; Sato, T.; Narimatsu, H.
Functional expression of L-fucokinase/guanosine 5-diphosphate-L-fucose pyrophosphorylase from Bacteroides fragilis in Saccharomyces cerevisiae for the production of nucleotide sugars from exogenous monosaccharides
Glycobiology
21
1228-1236
2011
Bacteroides fragilis (Q58T34), Bacteroides fragilis 9343 (Q58T34)
brenda
Chin, Y.; Seo, N.; Kim, J.; Seo, J.
Metabolic engineering of Escherichia coli to produce 2'-fucosyllactose via salvage pathway of guanosine 5'-diphosphate (GDP)-l-fucose
Biotechnol. Bioeng.
113
2443-2452
2016
Bacteroides fragilis (Q58T34), Bacteroides fragilis ATCC 25285 (Q58T34)
-
brenda
Ohashi, H.; Wahl, C.; Ohashi, T.; Elling, L.; Fujiyama, K.
Effective synthesis of guanosine 5'-diphospho-beta-L-galactose using bacterial L-fucokinase/guanosine 5'-diphosphate-L-fucose pyrophosphorylase
Adv. Synth. Catal.
359
4227-4234
2017
Bacteroides fragilis
-
brenda
Liu, Y.; Hu, H.; Wang, J.; Zhou, Q.; Wu, P.; Yan, N.; Wang, H.; Wu, J.; Sun, L.
Cryo-EM structure of L-fucokinase/GDP-fucose pyrophosphorylase (FKP) in Bacteroides fragilis
Protein Cell
10
365-369
2019
Bacteroides fragilis, Bacteroides fragilis 9343
brenda
Jung, S.M.; Chin, Y.W.; Lee, Y.G.; Seo, J.H.
Enhanced production of 2'-fucosyllactose from fucose by elimination of rhamnose isomerase and arabinose isomerase in engineered Escherichia coli
Biotechnol. Bioeng.
116
2412-2417
2019
Bacteroides fragilis
brenda
Wang, H.; Zhang, C.; Yang, Q.; Feng, J.; Chen, H.; Gu, Z.; Zhang, H.; Chen, W.; Chen, Y.
Production of GDP-L-fucose from exogenous fucose through the salvage pathway in Mortierella alpina
RSC Adv.
6
46308-46316
2016
Mortierella alpina
-
brenda
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