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Information on EC 2.7.1.52 - fucokinase
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2.7.1.52 fucokinaseIUBMB Comments
Requires a divalent cation for activity, with Mg2+ and Fe2+ giving rise to the highest enzyme activity. Forms part of a salvage pathway for reutilization of L-fucose. Can also phosphorylate D-arabinose, but more slowly.
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Word Map
- 2.7.1.52
-
salvage
-
fucosyltransferase
-
3hfucose
-
reutilization
- gdp-alpha-d-mannose
- gdp-beta-l-fucose
- synthesis
- analysis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
fucokinase, l-fucokinase, fucose kinase, l-fucose kinase, fucokinase/l-fucose-1-p-guanylyltransferase, l-fucokinase:gdp-fucose pyrophosphorylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP:6-deoxy-beta-L-galactose 1-phosphotransferase
ATP:6-deoxy-L-galactose 1-phospho transferase
FKP
fucokinase
fucose kinase
-
-
-
-
Fuk
kinase, fuco- (phosphorylating)
-
-
-
-
L-fucokinase
L-fucokinase/guanosine 5'-diphosphate-L-fucose pyrophosphorylase
L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase
L-fucose kinase
-
-
-
-
additional information
FKP
-
the enzyme shows L-fucokinase and guanosine 5'-diphosphate-L-fucose pyrophosphorylase activities
FKP
bifunctional enzyme with L-fucokinase/GDP-fucose diphosphorylase activities
FKP
bifunctional enzyme with L-fucokinase/GDP-fucose diphosphorylase activities
-
fucokinase
-
-
-
-
L-fucokinase/guanosine 5'-diphosphate-L-fucose pyrophosphorylase
-
-
additional information
two splicing variants with slightly different molecular weights, only long variant was found to be active
additional information
two splicing variants with slightly different molecular weights, only long variant was found to be active
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-fucose = ADP + beta-L-fucose 1-phosphate
the mechanism involves anomeric oxygen retention
-
ATP + L-fucose = ADP + beta-L-fucose 1-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP:beta-L-fucose 1-phosphotransferase
Requires a divalent cation for activity, with Mg2+ and Fe2+ giving rise to the highest enzyme activity. Forms part of a salvage pathway for reutilization of L-fucose. Can also phosphorylate D-arabinose, but more slowly.
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CAS REGISTRY NUMBER
COMMENTARY
37278-00-5
-
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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
ATP + L-galactose
ADP + beta-L-galactose 1-phosphate
-
the enzyme shows a 45times lower affinity towards L-galactose compared to L-fucose
-
-
?
ITP + 6-deoxy-L-galactose
IDP + 6-deoxy-L-galactose 1-phosphate
-
2.5% of the activity with L-fucose
-
-
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
highly specific for ATP
beta-L-fucose 1-phosphate
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
highly specific for L-fucose
beta-L-fucose 1-phosphate
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
i.e. L-fucose, serves to utilize free L-fucose for glycoprotein synthesis
-
-
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
-
beta-L-fucose 1-phosphate
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
-
beta-L-fucose 1-phosphate
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
highly specific for ATP
-
-
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
beta-L-fucose isomer required
-
-
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
highly specific for L-fucose
-
-
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
enzyme is part of a salvage pathway for reutilization of L-fucose
-
-
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
i.e. L-fucose, serves to utilize free L-fucose for glycoprotein synthesis
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
involved in GDP-L-fucose salvage pathway
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
involved in GDP-L-fucose salvage pathway
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
involved in GDP-L-fucose salvage pathway
-
-
?
CTP + 6-deoxy-L-galactose
CDP + 6-deoxy-L-galactose 1-phosphate
-
no activity
-
-
?
CTP + 6-deoxy-L-galactose
CDP + 6-deoxy-L-galactose 1-phosphate
-
60% of the activity with ATP
-
-
?
GTP + 6-deoxy-L-galactose
GDP + 6-deoxy-L-galactose 1-phosphate
-
no activity
-
-
?
GTP + 6-deoxy-L-galactose
GDP + 6-deoxy-L-galactose 1-phosphate
-
56% of the activity with ATP
-
-
?
UTP + 6-deoxy-L-galactose
UDP + 6-deoxy-L-galactose 1-phosphate
-
no activity
-
-
?
UTP + 6-deoxy-L-galactose
UDP + 6-deoxy-L-galactose 1-phosphate
-
59% of the activity with ATP
-
-
?
additional information
?
-
-
enzyme generates GDP-L-fucose from L-fucose 1-phosphate and GTP. No substrates for fucokinase activity are: L-arabinose, glucose, galactose, mannose, xylose, L-rhamnose, galactosamine, glucosamine, N-acetylglucosamine
-
-
?
additional information
?
-
-
development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview
-
-
?
additional information
?
-
-
fucokinase:GDP-fucose pyrophosphorylase is a dual activity enzyme metabolizing fucose and nucleotide-sugar
-
-
?
additional information
?
-
-
GDP-L-fucose and diphosphate are formed from L-fucose 1-phosphate and GTP by the GDP-L-Fuc pyrophosphorylase activity of the enzyme
-
-
-
additional information
?
-
-
the enzyme also acts as GDP-L-fucose pyrophosphorylase
-
-
-
additional information
?
-
-
fucokinase:GDP-fucose pyrophosphorylase is a dual activity enzyme metabolizing fucose and nucleotide-sugar
-
-
?
additional information
?
-
-
development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview
-
-
?
additional information
?
-
-
the enzyme also acts as GDP-L-fucose pyrophosphorylase
-
-
-
additional information
?
-
-
less than 5% of the activity with L-fucose is observed with: D-mannose, D-galactose, D-xylose, L-xylose, D-fucose and L-fucolose
-
-
?
additional information
?
-
-
fucokinase:GDP-fucose pyrophosphorylase is a dual activity enzyme metabolizing fucose and nucleotide-sugar
-
-
?
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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
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
i.e. L-fucose, serves to utilize free L-fucose for glycoprotein synthesis
-
-
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
enzyme is part of a salvage pathway for reutilization of L-fucose
-
-
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
-
i.e. L-fucose, serves to utilize free L-fucose for glycoprotein synthesis
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
involved in GDP-L-fucose salvage pathway
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
involved in GDP-L-fucose salvage pathway
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
involved in GDP-L-fucose salvage pathway
-
-
?
additional information
?
-
-
development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview
-
-
?
additional information
?
-
-
development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview
-
-
?
additional information
?
-
-
fucokinase:GDP-fucose pyrophosphorylase is a dual activity enzyme metabolizing fucose and nucleotide-sugar
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
absolute requirement for a divalent cation, 85% of the activation with Mg2+
Co2+
Fe2+
Mg2+
Mn2+
additional information
-
not influenced by Ca2+, Cu2+, K+, Hg2+, Ni2+ and Zn2+
Co2+
-
divalent cation required, CoSO4 exhibits 12% of the activity with MgSO4
Co2+
-
absolute requirement for a divalent cation, 15% of the activation with Mg2+
Co2+
-
divalent cation required, Co2+ stimulates with maximal activity at 3-5 mM, maximal activity is about 35-30% compared to activation by Mg2+
Fe2+
-
absolute requirement for a divalent cation, 29% of the activation with Mg2+
Fe2+
-
divalent cation required, Fe2+ stimulates nearly to the same degree as Mg2+, optimum activity at 10 mM
Mg2+
-
divalent cation required Mg2+ is slightly more effective than Mn2+
Mn2+
-
Mn2+ is the best suitable divalent cation of the L-fucokinase activity
Mn2+
-
divalent cation required, MnSO4 exhibits 90% of the activity with MgSO4
Mn2+
-
absolute requirement for a divalent cation, 87% of the activation with Mg2+
Mn2+
-
divalent cation required, Mn2+ stimulates with maximal activity at 3-5 mM, maximal activity is about 35-30% compared to activation by Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1,1-trichlorethyl 6-deoxy-alpha-L-galactopyranoside
-
10 mM, 87% inhibition
methyl 6-deoxy-2-O-dodecanoyl-alpha-L-galactopyranoside
-
10 mM, 37% inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Pathogenic Variants in Fucokinase Cause a Congenital Disorder of Glycosylation.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06629
L-fucose
pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.39
L-fucose
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
-
pH 7: about 50% of maximal activity, pH 9.5: about 60% of maximal activity
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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
bifunctional enzyme, L-fucokinase and GDP-L-fucose diphosphorylase activities
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
the enzyme catalyzes the first step of the salvage pathway converting exogenous L-Fuc to GDP-L-Fuc
metabolism
-
the enzyme catalyzes the first step of the salvage pathway converting exogenous L-Fuc to GDP-L-Fuc
-
physiological function
-
the bifunctional L-Fuc pyrophosphorylase, FKP, converts L-Fuc into GDP-L-Fuc via an L-Fuc-1-phosphate intermediate
physiological function
-
the bifunctional L-Fuc pyrophosphorylase, FKP, converts L-Fuc into GDP-L-Fuc via an L-Fuc-1-phosphate intermediate
-
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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)
FCSK_HUMAN
1084
0
117623
Swiss-Prot
other Location (Reliability: 4)
FCSK_MOUSE
1090
0
119267
Swiss-Prot
other Location (Reliability: 3)
A0A1Z5KL61_FISSO
1182
0
130747
TrEMBL
other Location (Reliability: 2)
A0A151TY35_CAJCA
1059
0
116791
TrEMBL
Mitochondrion (Reliability: 4)
Q4CLY9_TRYCC
Trypanosoma cruzi (strain CL Brener)
176
0
19621
TrEMBL
other Location (Reliability: 2)
A0A3Q8I9C4_LEIDO
1186
0
126000
TrEMBL
other Location (Reliability: 3)
A0A422N961_TRYRA
207
3
23286
TrEMBL
other Location (Reliability: 2)
E6SQA0_BACT6
Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / CCUG 15421 / P 36-108)
951
0
106307
TrEMBL
-
I2CRJ3_NANGC
Nannochloropsis gaditana (strain CCMP526)
138
0
14653
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2H9ZTA8_9ASPA
1082
0
118743
TrEMBL
other Location (Reliability: 5)
F0SXR2_SYNGF
Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR)
1020
0
113869
TrEMBL
-
B9SBD4_RICCO
873
0
95714
TrEMBL
Secretory Pathway (Reliability: 5)
A0A8B6H0N6_MYTGA
1087
0
119916
TrEMBL
other Location (Reliability: 3)
A0A0B2RQM5_GLYSO
984
0
107882
TrEMBL
other Location (Reliability: 5)
F0R672_PHOSB
Phocaeicola salanitronis (strain DSM 18170 / JCM 13657 / BL78)
957
0
107750
TrEMBL
-
A0A3S7WTT9_LEIDO
1186
0
126072
TrEMBL
other Location (Reliability: 3)
A0A088RLI5_9TRYP
1227
0
131626
TrEMBL
other Location (Reliability: 3)
A0A5B7CEM2_DAVIN
1138
0
125150
TrEMBL
other Location (Reliability: 4)
A0A381MFR4_LEIIN
1186
0
126158
TrEMBL
other Location (Reliability: 3)
A4HWU2_LEIIN
1186
0
126232
TrEMBL
other Location (Reliability: 3)
K8Z2Q3_NANGC
Nannochloropsis gaditana (strain CCMP526)
146
0
15582
TrEMBL
other Location (Reliability: 4)
A9UMM9_XENLA
1086
0
119111
TrEMBL
other Location (Reliability: 2)
Q4QEX6_LEIMA
1187
0
126532
TrEMBL
other Location (Reliability: 3)
A0A6J4JQA0_9CHLR
100
0
11051
TrEMBL
-
A0A1P8AL35_MORAP
439
0
46914
TrEMBL
other Location (Reliability: 3)
A0A8B6GZH5_MYTGA
1079
0
119019
TrEMBL
other Location (Reliability: 2)
A0A6J8CJM3_MYTCO
1012
1
111349
TrEMBL
other Location (Reliability: 3)
A0A1R3STZ0_9BACT
950
0
107657
TrEMBL
-
A0A812CYP5_SEPPH
992
0
109932
TrEMBL
other Location (Reliability: 2)
A4H8H4_LEIBR
1229
0
131952
TrEMBL
other Location (Reliability: 2)
Q4QEX2_LEIMA
1187
0
126539
TrEMBL
other Location (Reliability: 3)
A0A6J8CL73_MYTCO
999
1
109923
TrEMBL
other Location (Reliability: 3)
A0A3R7LA46_9TRYP
110
0
11955
TrEMBL
other Location (Reliability: 3)
A0A1Z5KDC3_FISSO
1182
0
130524
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
120000
440000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
homotrimer
3 * 105000, recombinant enzyme, calculated from amino acid sequence
tetramer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
peptide sequence does not contain a secretory signal or transmembrane domain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 as precipitant, 200 mM trisodium citrate pH 8.3
purified apo-enzyme, mixing of 10 mg/ml protein in 10 mM Tris-HCl pH 7.5 with 9% w/v PEG 6K, 5% v/v ethylene glycol, 5% v/v glycerol, 25 mM HEPES pH 7.5, 2% tert-butanol, 1 mM MgCl2, 1mM MnCl2, 24°C, 20-30 days, X-ray diffraction structure determination and analysis at 2.6 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G133A
-
mutation abolishes GDP-L-fucose diphosphorylase activity, hardly affects fucokinase activity
G830A
-
mutation reduces fucokinase activity by more than 90%, while preserving the GDP-L-fucose diphosphorylase activity
G757A
the mutant has greatly reduced fucokinase activity compared to the wild type enzyme
G902A
the mutant has greatly reduced fucokinase activity compared to the wild type enzyme
T602A
the mutant has greatly reduced fucokinase activity compared to the wild type enzyme
additional information
additional information
deletion mutant lacking the first 363 amino acids of the N-terminus expressed in Escherichia coli BL21 cells display fucokinase activity
additional information
-
deletion mutant lacking the first 363 amino acids of the N-terminus expressed in Escherichia coli BL21 cells display fucokinase activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 12
-
After 30 min at pH 3,0, 5.0, 7.0, 8.0, 10.0, and 12.0, the enzyme shows about 25%, 50%, 90%, 100%, 75%, and 35% activity, respectively
738343
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 37
-
the enzyme is stable for 2 h at 4 and 12°C. At 20°C, the enzyme shows 80% activity after 1 h and less than 20% activity after 2 h incubation. At 28°C, the enzyme is stable for 30 min, while at 37°C, the enzyme activity drops to about 37% after 30 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
instability of the enzyme occurs through chemical reduction in disulfide bonds of FKP protein, resulting in degradation
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-16°C, about 30% loss of activity within 24 h and about 60% loss of activity within 72 h
-
-16°C, in the presence of stabilizing ovalbumin, about 30% loss of activity within 48 h
-
-20°C, 50% glycerol, 1 mM PMSF, 0.2 M NaCl, 50 mM Tris-HCl buffer, pH 7.5, stable for 1 month
-
-80C, crude extracts, at least 2 years, without significant loss of activity
2-4°C, most stable in the presence of glycerol and a sulfhydryl reagent
-
frozen, in the presence of glycerol or sucrose and a sulfhydryl reagent, up to 1 week
-
frozen, rapid loss of activity, glycerol or sucrose and DTT or 2-mercaptoethanol stabilize, no stabilization by Mg2+, EDTA, KCl or ovalbumin
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-affinity column chromatography and Superdex G200 gel filtration
recombinant maltose-binding protein fusion protein from Escherichia coli strain BL21(DE3) by amylose affinity chromatography, cleavage of the tag by Genease I protease, followed by guanosine affinity chromatography and ultrafiltration
-
recombinant protein with His-tag and fused to thioredoxin, partial purification
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression as fusion protein with maltose-binding protein in Escherichia coli strain BL21 (DE3)
-
expression of full-length protein and a deletion mutant lacking the first 363 amino acids of the N-terminus are expressed in Escherichia coli BL21 cells. Both proteins display fucokinase activity. Identification of amino acid sequence
functional expression of HA-tagged FKP in Saccharomyces cerevisiae strain W303-1A, the biosynthesis of GDP-D-Ara in the recombinant Saccharomyces cerevisiae strain harboring the FKP gene can occur through a mechanism akin to that of GDP-L-Fuc via the salvage pathway. Expression of a loss-of-function FKP mutant in yeast
-
two different transcripts of 3057 and 3270 base pairs expressed in COS-7 cells, only the longer splice variant is enzymatically active
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme transcript level is up-regulated 4.3fold by nitrogen exhaustion when Mortierella alpina starts to accumulate lipid
the enzyme transcript level is up-regulated 4.3fold by nitrogen exhaustion when Mortierella alpina starts to accumulate lipid
-
the enzyme transcript level is up-regulated 4.3fold by nitrogen exhaustion when Mortierella alpina starts to accumulate lipid
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
synthesis
-
the enzyme is a valuable biochemical tool to prepare activated L-fucose derivatives for fucosylation reactions, enzyme is valuable for the formation of radiolabeled fucose 1-phosphate
analysis
-
development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview
analysis
-
development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ishihara, H.; Massaro, D.J.; Heath, E.C.
The metabolism of L-fucose. 3. The enzymatic synthesis of beta-L-fucose 1-phosphate
J. Biol. Chem.
243
1103-1109
1968
Sus scrofa
brenda
Richards, W.L.; Serif, G.S.
Canine thyroid fucokinase
Biochim. Biophys. Acta
484
353-367
1977
Canis lupus familiaris
brenda
Kilker, R.D.; Shuey, D.K.; Serif, G.S.
Isolation and properties of porcine thyroid fucokinase
Biochim. Biophys. Acta
570
271-283
1979
Sus scrofa
brenda
Butler, W.; Serif, G.S.
Fucokinase, its anomeric specificity and mechanism of phosphate group transfer
Biochim. Biophys. Acta
829
238-243
1985
Sus scrofa
brenda
Park, S.H.; Pastuszak, I.; Drake, R.; Elbein, A.D.
Purification to apparent homogeneity and properties of pig kidney L-fucose kinase
J. Biol. Chem.
273
5685-5691
1998
Sus scrofa
brenda
Zeitler, R.; Danneschewski, S.; Lindhorst, T.; Thiem, J.; Reutter, W.
Inhibition of L-fucokinase from rat liver by L-fucose analogues in vitro
J. Enzyme Inhib.
11
265-273
1997
Rattus norvegicus
brenda
Hinderlich, S.; Berger, M.; Blume, A.; Chen, H.; Ghaderi, D.; Bauer, C.
Identification of human L-fucose kinase amino acid sequence
Biochem. Biophys. Res. Commun.
294
650-654
2002
Homo sapiens (Q8N0W3), Homo sapiens
brenda
Miller, E.N.; Rupp, A.L.; Lindberg, M.K.; Wiese, T.J.
Tissue distribution of L-fucokinase in rodents
Comp. Biochem. Physiol. B
140
513-520
2005
Mus musculus, Rattus rattus
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 (Q7TMC8), Mus musculus (Q7TS31), 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
Rattus norvegicus, Mus musculus (Q7TMC8), Mus musculus
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
Honas, B.J.; Glassman, U.M.; Wiese, T.J.
Enzymatic activity of alpha-L-fucosidase and L-fucokinase across vertebrate animal species
Comp. Biochem. Physiol. B
153
359-364
2009
Cyprinus carpio, Chelydra serpentina, Colinus virginianus, Columba livia, Ictalurus punctatus, Lithobates catesbeianus, Micropterus salmoides, Sylvilagus floridanus, Pituophis catenifer sayi, Lepus californicus, Phasianus colchicus, Odocoileus virginianus
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
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, no activity in Saccharomyces cerevisiae, Bacteroides fragilis 9343
brenda
Liu, T.W.; Kaji, H.; Togayachi, A.; Ito, H.; Sato, T.; Narimatsu, H.
A chemoenzymatic approach toward the identification of fucosylated glycoproteins and mapping of N-glycan sites
Glycobiology
22
630-637
2012
Bacteroides fragilis, Bacteroides fragilis 9343
brenda
Cheng, C.; Gu, J.; Su, J.; Ding, W.; Yin, J.; Liang, W.; Yu, X.; Ma, J.; Wang, P.G.; Xiao, Z.; Liu, Z.J.
Crystallization, preliminary X-ray crystallographic and cryo-electron microscopy analysis of a bifunctional enzyme fucokinase/L-fucose-1-P-guanylyltransferase from Bacteroides fragilis
Acta Crystallogr. Sect. F
70
1206-1210
2014
Bacteroides fragilis (Q58T34), Bacteroides fragilis
brenda
Wang, H.; Zhang, C.; Chen, H.; Yang, Q.; Zhou, X.; Gu, Z.; Zhang, H.; Chen, W.; Chen, Y.Q.
Characterization of an fungal L-fucokinase involved in Mortierella alpina GDP-L-fucose salvage pathway
Glycobiology
26
880-887
2016
Mortierella alpina, Mortierella alpina ATCC 32222
brenda
Villalobos, J.A.; Yi, B.R.; Wallace, I.S.
2-Fluoro-L-fucose is a metabolically incorporated inhibitor of plant cell wall polysaccharide fucosylation
PLoS ONE
10
e0139091
2015
Arabidopsis thaliana
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
Chin, Y.W.; Seo, N.; Kim, J.H.; Seo, J.H.
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, Bacteroides fragilis ATCC25285
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 (Q58T34), Bacteroides fragilis 9343 (Q58T34)
brenda
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