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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
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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