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ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
ATP + D-ribose
?
-
87% of the activity with L-fucose
-
-
?
ATP + L-arabinose
?
-
31% of the activity with L-fucose
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
ATP + L-galactose
ADP + beta-L-galactose 1-phosphate
-
the enzyme shows a 45times lower affinity towards L-galactose compared to L-fucose
-
-
?
ATP + L-rhamnose
?
-
41% of the activity with L-fucose
-
-
?
CTP + 6-deoxy-L-galactose
CDP + 6-deoxy-L-galactose 1-phosphate
GTP + 6-deoxy-L-galactose
GDP + 6-deoxy-L-galactose 1-phosphate
ITP + 6-deoxy-L-galactose
IDP + 6-deoxy-L-galactose 1-phosphate
-
2.5% of the activity with L-fucose
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
UTP + 6-deoxy-L-galactose
UDP + 6-deoxy-L-galactose 1-phosphate
additional information
?
-
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
-
-
-
?
ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 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
-
-
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 + D-arabinose
?
-
28% of the activity with L-fucose
-
-
?
ATP + D-arabinose
?
-
9.3% of the activity with L-fucose
-
-
?
ATP + D-glucose
?
-
2.5% of the activity with L-fucose
-
-
?
ATP + D-glucose
?
-
107% of the activity with L-fucose
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
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
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
L-fucose + ATP
beta-L-fucose 1-phosphate + ADP
-
-
-
-
?
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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ATP + 6-deoxy-L-galactose
ADP + 6-deoxy-L-galactose 1-phosphate
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
additional information
?
-
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
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
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
-
-
?
ATP + L-fucose
ADP + beta-L-fucose 1-phosphate
-
-
-
-
?
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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Ca2+
-
absolute requirement for a divalent cation, 85% of the activation with Mg2+
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+
-
or Mn2+, absolutely required for fucokinase activity
Mg2+
-
divalent cation required Mg2+ is slightly more effective than Mn2+
Mg2+
-
best stimulation of activity in the presence of 2 mM Mg2+
Mg2+
-
absolute requirement for a divalent cation, Mg2+ is most efficient
Mg2+
-
absolute requirement for a divalent cation, best stimulation at 3 mM
Mn2+
-
or Mg2+, absolutely required for fucokinase activity
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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1,1,1-trichlorethyl 6-deoxy-alpha-L-galactopyranoside
-
10 mM, 87% inhibition
4,6-dideoxy-4-azido-alpha-L-glucopyranose
-
10 mM, 9% inhibition
4,6-dideoxy-4-fluoro-L-gluco-pyranose
-
10 mM, 30% inhibition
4,6-dideoxy-4-iodo-L-glucopyranose
-
10 mM, 75% inhibition
4,6-dideoxy-L-xylo-hexopyranose
-
10 mM, 74% inhibition
AMP
-
5.0 mM, 14% inhibition in presence of ATP
CDP
-
4.9 mM, 16% inhibition in presence of ATP
Co2+
-
complete inhibition at 20 mM
CTP
-
4.9 mM, 30% inhibition in presence of ATP
D-arabinose
-
0.5 mM, 20% inhibition. 10 mM, 84% inhibition
Fe2+
-
complete inhibition at 20 mM
methyl 3,6-dideoxy-alpha-L-xylo-hexopyranoside
-
10 mM, 17% inhibition
methyl 4,6-dideoxy-4-iodo-alpha-L-glucopyranoside
-
10 mM, 54% inhibition
methyl 4,6-dideoxy-alpha-L-xylo-hexopyranoside
-
10 mM, 9% inhibition
methyl 6-deoxy-2-O-dodecanoyl-alpha-L-galactopyranoside
-
10 mM, 37% inhibition
methyl 6-deoxy-alpha-L-galactopyranoside
-
10 mM, 89% inhibition
octyl 6-deoxy-alpha-L-galactopyranoside
-
10 mM, 40% inhibition
TTP
-
4.8 mM, 45% inhibition in presence of ATP
ADP
-
-
ADP
-
4.9 mM, 96% inhibition, competitive with ATP
GDP-L-fucose
-
less than 30% inhibition at 0.2 mM
GDP-L-fucose
-
competitive with L-fucose
GTP
-
-
GTP
-
0.1 mM, 59% inhibition in presence of ATP
L-fucose
-
substrate inhibition at high concentrations
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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
-
A0A1G4GAQ4_9BACT
951
0
106962
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)
D4VEK8_9BACE
950
0
105994
TrEMBL
-
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)
A0A0P0LBX3_PHOVU
767
0
85268
TrEMBL
-
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)
A0A174L5C1_BACUN
969
0
108793
TrEMBL
-
A0A6J4JQA0_9CHLR
100
0
11051
TrEMBL
-
A0A174UU20_BACUN
987
0
110903
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)
A0A174MLV6_BACUN
987
0
110878
TrEMBL
-
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)
Q58T34_BACFG
949
0
105660
TrEMBL
-
Q7TS31_MOUSE
312
0
35186
TrEMBL
-
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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
A723R
the fucokinase activity of the mutant is totally abolished
D594A
the mutant retains hardly any fucokinase activity
D601A
the mutant retains hardly any fucokinase activity
D762A
the mutant retains hardly any fucokinase activity
G597A
the mutant retains hardly any fucokinase activity
G598A
the mutant retains hardly any fucokinase activity
G713A
the fucokinase activity of the mutant is totally abolished
G715A
the fucokinase activity of the mutant is totally abolished
G717A
the fucokinase activity of the mutant is totally abolished
G757A
the mutant has greatly reduced fucokinase activity compared to the wild type enzyme
G758A
the mutant retains hardly any fucokinase activity
G759A
the mutant retains hardly any fucokinase activity
G899A
the mutant retains hardly any fucokinase activity
G901A
the mutant retains hardly any fucokinase activity
G902A
the mutant has greatly reduced fucokinase activity compared to the wild type enzyme
Q761A
the mutant retains hardly any fucokinase activity
R592A
the mutant retains hardly any fucokinase activity
S714A
the fucokinase activity of the mutant is totally abolished
S719A
the fucokinase activity of the mutant is totally abolished
S720A
the fucokinase activity of the mutant is totally abolished
T602A
the mutant has greatly reduced fucokinase activity compared to the wild type enzyme
D762A
-
the mutant retains hardly any fucokinase activity
-
G598A
-
the mutant retains hardly any fucokinase activity
-
G713A
-
the fucokinase activity of the mutant is totally abolished
-
R592A
-
the mutant retains hardly any fucokinase activity
-
S714A
-
the fucokinase activity of the mutant is totally abolished
-
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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-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
-
-20°C, in the presence of 2-mercaptoethanol and glycerol, quite stable
-
-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
-
4°C, 1 day, loss of 50% of GDP-L-fucose diphosphorylase activity
-
4°C, unstable in saline solution
-
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
-
frozen, unstable in saline solution
-
-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
-
-80C, crude extracts, at least 2 years, without significant loss of activity
-
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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