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Fucokinase

fucokinase, Fuk, L-Fucose kinase
The protein encoded by this gene belongs to the GHMP (galacto-, homoserine, mevalonate and phosphomevalonate) kinase family and catalyzes the phosphorylation of L-fucose to form beta-L-fucose 1-phosphate. This enzyme catalyzes the first step in the utilization of free L-fucose in glycoprotein and glycolipid synthesis. L-fucose may be important in mediating a number of cell-cell interactions such as blood group antigen recognition, inflammation, and metastatis. While several transcript variants may exist for this gene, the full-length nature of only one has been described to date. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: fucosyltransferase, CAN, V1a, ACID, CD45
Papers on fucokinase
Biochemical characterization of an α1,2-colitosyltransferase from Escherichia coli O55:H7.
New
Li et al., Shijiazhuang, China. In Glycobiology, Jan 2016
In this study, starting with chemically prepared colitose, 94.6 mg of GDP-colitose was prepared via a facile and efficient one-pot two-enzyme system involving an L-fucokinase/GDP-L-Fuc pyrophosphorylase (FKP) and an inorganic pyrophosphatase (EcPpA).
The transcription factor ATF2 promotes melanoma metastasis by suppressing protein fucosylation.
Ronai et al., Los Angeles, United States. In Sci Signal, 2014
PKCε-dependent phosphorylation of ATF2 promoted its transcriptional repression of the gene encoding fucokinase (FUK), which mediates the fucose salvage pathway and thus global cellular protein fucosylation.
Crystallization, preliminary X-ray crystallographic and cryo-electron microscopy analysis of a bifunctional enzyme fucokinase/L-fucose-1-P-guanylyltransferase from Bacteroides fragilis.
Liu et al., Melbourne, Australia. In Acta Crystallogr Sect F Struct Biol Commun, 2014
Fucokinase/L-fucose-1-P-guanylyltransferase (FKP) is a bifunctional enzyme which converts L-fucose to Fuc-1-P and thence to GDP-L-fucose through a salvage pathway.
WbgL: a novel bacterial α1,2-fucosyltransferase for the synthesis of 2'-fucosyllactose.
Elling et al., Aachen, Germany. In Glycobiology, 2014
Based on its excellent kinetic efficiency for lactose, we present here a sequential reaction strategy for the synthesis of α1,2-fucosyllactose in one pot including the synthesis of the donor substrate 3,3'-Diaminobenzidine (GDP)-β-l-fucose by the bifunctional l-fucokinase/GDP-β-l-Fuc pyrophosphorylase of Bacteroides fragilis 9343.
The flowering repressor SVP underlies a novel Arabidopsis thaliana QTL interacting with the genetic background.
Alonso-Blanco et al., Madrid, Spain. In Plos Genet, 2012
To find novel A. thaliana flowering QTL, we developed introgression lines from the Japanese accession Fuk, which was selected based on the substantial transgression observed in an F(2) population with the reference strain Ler.
Side population cells from human melanoma tumors reveal diverse mechanisms for chemoresistance.
Fujita et al., Aurora, United States. In J Invest Dermatol, 2012
In addition, gene profiling studies identified three signaling pathways (NF-κB, α6-β4-integrin, and IL-1) as differentially upregulated in melanoma SP cells, and there was a significant increase of PCDHB11 and decrease of FUK and TBX2 in these cells.
Crystallization and preliminary X-ray characterization of the Vitis vinifera fucokinase:GDP-fucose pyrophosphorylase.
Quirk, Roswell, United States. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012
The Vitis vinifera dual-activity fucose and nucleotide-sugar metabolizing enzyme L-fucokinase:GDP-fucose pyrophosphorylase (FKP) has been purified to homogeneity and the 118.8 kDa monomeric protein has been crystallized by vapor diffusion in Zeppezauer tubes at 277 K. Crystals of the apoenzyme diffracted to 2.6 Å resolution and belonged to the tetragonal space group P4(1)2(1)2.
One-pot multienzyme synthesis of Lewis x and sialyl Lewis x antigens.
Chen et al., Davis, United States. In Curr Protoc Chem Biol, 2012
In this system, GDP-Fuc is generated from L-fucose, adenosine 5'-triphosphate (ATP), and guanosine 5'-triphosphate (GTP) by a bifunctional L-fucokinase/GDP-fucose pyrophosphorylase (FKP).
A chemoenzymatic approach toward the identification of fucosylated glycoproteins and mapping of N-glycan sites.
Narimatsu et al., Tsukuba, Japan. In Glycobiology, 2012
In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human α1,3-fucosyltransferase 9 are combined in a Namalwa cellular model.
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.
Narimatsu et al., Tsukuba, Japan. In Glycobiology, 2011
This method exploits l-fucokinase/guanosine 5'-diphosphate (GDP)-l-fucose (L-Fuc) pyrophosphorylase (FKP), a bifunctional enzyme isolated from Bacteroides fragilis 9343, which converts l-Fuc into GDP-L-Fuc via an L-Fuc-1-phosphate intermediate.
Chemoenzymatic synthesis of GDP-L-fucose and the Lewis X glycan derivatives.
Wu et al., United States. In Proc Natl Acad Sci U S A, 2009
This method exploits l-fucokinase/GDP-fucose pyrophosphorylase (FKP), a bifunctional enzyme isolated from Bacteroides fragilis 9343, which converts l-fucose into GDP-fucose via a fucose-1-phosphate (Fuc-1-P) intermediate.
Enzymatic activity of alpha-L-fucosidase and L-fucokinase across vertebrate animal species.
Wiese et al., Hays, United States. In Comp Biochem Physiol B Biochem Mol Biol, 2009
As part of a program to determine the controls on protein L-fucosylation, we have systematically determined the tissue distribution of the enzymes L-fucokinase and alpha-L-fucosidase in species across the vertebrate animal kingdom.
A bifunctional enzyme with L-fucokinase and GDP-L-fucose pyrophosphorylase activities salvages free L-fucose in Arabidopsis.
Tsumuraya et al., Saitama, Japan. In J Biol Chem, 2008
For this study we have identified, in the genomic data base of Arabidopsis, the gene (designated AtFKGP) of a bifunctional enzyme with similarity to both L-fucokinase and GDP-L-Fuc pyrophosphorylase.
Differential gene expression of GDP-L-fucose-synthesizing enzymes, GDP-fucose transporter and fucosyltransferase VII.
Renkonen et al., Helsinki, Finland. In Apmis, 2006
In the alternative biosynthetic pathway, in the salvage metabolism, L-fucokinase (Fuk) synthesizes L-fucose-1-phosphate from free fucose.
Tissue distribution of L-fucokinase in rodents.
Wiese et al., Hays, United States. In Comp Biochem Physiol B Biochem Mol Biol, 2005
The utilization of fucose in the salvage pathway begins with phosphorylation by fucokinase.
Cloning and expression of murine enzymes involved in the salvage pathway of GDP-L-fucose.
GeneRIF
Renkonen et al., Helsinki, Finland. In Eur J Biochem, 2004
cloning, expression and tissue distribution of murine L-fucokinase and GDP-L-fucose pyrophosphorylase
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