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GDP-beta-L-fucose + 2-nitrophenyl beta-D-galactopyranoside
GDP + 2-nitrophenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
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Substrates: -
Products: 137% of the activity with phenyl beta-D-galactopyranoside
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GDP-beta-L-fucose + beta-D-Gal-(1->3)-beta-D-GlcNAc-2-anthranilic acid aglycone
GDP + alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-beta-D-GlcNAc-2-anthranilic acid aglycone
Substrates: -
Products: -
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GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosamine
Substrates: residues of H type 3 epitopes, reaction of EC 2.4.1.69
Products: -
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GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosamine
Substrates: residues of H type 1 epitopes, reaction of EC 2.4.1.69
Products: -
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GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acteyl-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
-
Substrates: i.e. lacto-N-tetraose, residues of H type 1 epitopes, reaction of EC 2.4.1.69
Products: 131% of the activity with phenyl beta-D-galactopyranoside
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GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-galactosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-galactosamine
Substrates: residues of H type 3 epitopes, reaction of EC 2.4.1.69
Products: -
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GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: residues of H type 2 epitopes
Products: -
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GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R
-
Substrates: -
Products: -
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GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine
GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
-
Substrates: i.e. lacto-N-neotetraose, residues of H type 2 epitopes
Products: 113% of the activity with phenyl beta-D-galactopyranoside
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GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-glucosylceramide
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-glucosylceramide
-
Substrates: -
Products: -
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GDP-beta-L-fucose + freezing point-depressing glycoprotein
GDP + alpha-L-fucosyl-freezing point-depressing glycoprotein
-
Substrates: -
Products: -
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GDP-beta-L-fucose + H2O
GDP + beta-L-fucose
GDP-beta-L-fucose + lacto-N-biose
GDP + alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine
GDP-beta-L-fucose + lactose
GDP + alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranoside
GDP-beta-L-fucose + methyl 2-acetamido-2-deoxy-3-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + methyl alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->3)-2-acetamido-2-deoxy-beta-D-glucopyranoside
GDP-beta-L-fucose + N-acetyllactosamine
GDP + alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->4)-N-acetyl-beta-D-glucosamine
GDP-beta-L-fucose + p-nitrophenyl-lactose
p-nitrophenyl-O-alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl (1->4)-D-glucopyranoside
Substrates: no acttivity with p-nitrophenyl-alpha-galactose, p-nitrophenyl-alpha-glucose, p-nitrophenyl-beta-N-acetylgalactosamine, p-nitrophenyl-beta-galactose, p-nitrophenyl-beta-glucose, p-nitrophenyl-alpha-N-acetylglucosamine, p-nitrophenyl-beta-N-acetylglucosamine, lacto-N-biose, galacto-N-biose, N-acetylactosamine and Galbeta1,6GalNAc
Products: -
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GDP-beta-L-fucose + phenyl beta-D-galactopyranoside
GDP + phenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
GDP-L-Fuc + xyloglucan
GDP + alpha-L-Fuc-xyloglucan
Substrates: acceptor is nonlabeled XLLG oligosaccharide
Products: -
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GDP-L-Gal + xyloglucan
GDP + alpha-L-Gal-xyloglucan
Substrates: acceptor is nonlabeled XLLG oligosaccharide
Products: -
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additional information
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GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine

GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
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Substrates: i.e. lacto-N-biose I, reaction of EC 2.4.1.69
Products: 82% of the activity with phenyl beta-D-galactopyranoside
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GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine
-
Substrates: i.e. lacto-N-biose I
Products: reaction of EC 2.4.1.69
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GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine

GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine
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Substrates: i.e. N-acetyllactosamine
Products: 80% of the activity with phenyl beta-D-galactopyranoside
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GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine
GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine
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Substrates: i.e. N-acetyllactosamine
Products: -
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GDP-beta-L-fucose + H2O

GDP + beta-L-fucose
Substrates: -
Products: -
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GDP-beta-L-fucose + H2O
GDP + beta-L-fucose
Substrates: -
Products: -
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GDP-beta-L-fucose + lacto-N-biose

GDP + alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine
Substrates: high activity
Products: -
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GDP-beta-L-fucose + lacto-N-biose
GDP + alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine
Substrates: high activity
Products: -
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GDP-beta-L-fucose + lactose

GDP + alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranoside
Substrates: low activity
Products: -
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GDP-beta-L-fucose + lactose
GDP + alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->4)-beta-D-glucopyranoside
Substrates: low activity
Products: -
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GDP-beta-L-fucose + methyl 2-acetamido-2-deoxy-3-O-beta-D-galactopyranosyl-beta-D-glucopyranoside

GDP + methyl alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->3)-2-acetamido-2-deoxy-beta-D-glucopyranoside
Substrates: high activity
Products: -
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GDP-beta-L-fucose + methyl 2-acetamido-2-deoxy-3-O-beta-D-galactopyranosyl-beta-D-glucopyranoside
GDP + methyl alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->3)-2-acetamido-2-deoxy-beta-D-glucopyranoside
Substrates: high activity
Products: -
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GDP-beta-L-fucose + N-acetyllactosamine

GDP + alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: low activity
Products: -
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GDP-beta-L-fucose + N-acetyllactosamine
GDP + alpha-L-fucopyranosyl-(1->2)-beta-D-galactopyranosyl-(1->4)-N-acetyl-beta-D-glucosamine
Substrates: low activity
Products: -
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GDP-beta-L-fucose + phenyl beta-D-galactopyranoside

GDP + phenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
-
Substrates: -
Products: -
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GDP-beta-L-fucose + phenyl beta-D-galactopyranoside
GDP + phenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
Substrates: -
Products: -
?
GDP-beta-L-fucose + phenyl beta-D-galactopyranoside
GDP + phenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
Substrates: -
Products: -
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additional information

?
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Substrates: no L-galactosyltransferase activities are detected toward XLLG-2-aminopyridine and XXLG-2-aminopyridine
Products: -
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additional information
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-
-
Substrates: enzyme catalyzes the transfer of L-fucose from GDP-L-fucose to a tetraglycosylceramide to form the blood group H-related glycosphingolipid
Products: -
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additional information
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-
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Substrates: no substrates: glucosamine, UDP-N-acetyl-galactosamine, and CMP-sialic acid
Products: -
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additional information
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-
-
Substrates: enzyme transfers L-fucose from GDP-L-fucose to an acceptor containing a beta-D-galactopyranosyl group at the nonreducing terminal
Products: -
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additional information
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-
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Substrates: the enzyme transfers fucose equally well to type I (Galbeta-(1->3)-GIcNAc) and type 2 (Galbeta-(1->4)-GIcNAc) substrates but type 3 (Galbeta-(1->3)-GalNAc) structures are less efficient acceptors
Products: -
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additional information
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-
-
Substrates: enzyme accepts both precursors of type 1 and type 2 H epitopes, catalyzing reactions of EC 2.4.1.69 and EC 2.4.1.344. The enzyme does not display alpha-(1,3)-fucosyltransferase activity or alpha-(1, 4)-fucosyl transferase activity
Products: -
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additional information
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Substrates: enzyme works well with type I (Galbeta1-3GlcNAcbetaOR) and its derivative (Galbeta1-3GlcNAcalphaOR), Type III (Galbeta1-3GalNAcalphaOR), and type IV (Galbeta1-3GalNAcbetaOR) acceptors for adding a fucose alpha1-2-linked to the terminal galactose residue. Type II (Galbeta1-4GlcNAcbetaOR) and type V (Galbeta1-4GlcbetaOR) glycans are not good acceptors
Products: -
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additional information
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Substrates: the enzyme has a preference for a Galbeta1,3GlcNAcbeta1-O-R acceptor motif
Products: -
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drug target

the enzyme is a promising target for anticancer drug discovery. Drug repurposing approach is deployed to identify new hits against fucosyltransferase 2. Enalaprilat dihydrate, ibuprofen, ascorbic acid, acarbose, and ceftriaxone sodium show high docking scores and binding energies against fucosyltransferase 2. Ceftriaxone sodium is identified as initial hit that can be proceeded for lead optimization against fucosyltransferase 2 (FUT2) via in-vitro, and pre-clinical studies
drug target
the enzyme catalyzes the biosynthesis of A, B, and H antigens and other important glycans, such as (Sialyl Lewisx) sLex, and (Sialyl Lewisy) sLey. The production of these glycans is increased in various cancers, hence to design and develop specific inhibitors of FUT2 is a therapeutic strategy. 3-Hydroxy-2-methyl-4H-pyran-4-one, 2-hydroxynaphthalene-1, 4-dione, 2-(carboxymethyl)-benzoic acid, 3-hydroxy-4-nitrobenzoic acid, and 4-(4'-hydroxyphenyl) butan-2-one that can be studied for further development as cancer therapeutic agents
drug target
the enzyme may have therapeutic potential across trypanosomatids
drug target
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the enzyme may have therapeutic potential across trypanosomatids
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malfunction

PvFUT2 knockdown with or without pathogen challenge reduces the expression of Pvbeta-catenin and antimicrobial peptides gene, particularly anti lipopolysaccharide factor and lysozyme. The knockdown of PvFUT2 increases Vibrio abundance in hemolymph and results in an increase in shrimp cumulative mortality rate. During pathogen challenge, the expression of PvFUT2 is induced to regulate beta-catenin and subsequently antimicrobial peptides expression to augment shrimp antimicrobial immune response
malfunction
overexpression of fucosyltransferase 2 (FUT2) is linked to inflammation and cancer
malfunction
null mutants of TbFUT1 demonstrate that it is essential for both the mammalian-infective bloodstream form and the insect vector-dwelling procyclic form. Deletion of TbFUT1 disturbs mitochondrial activity
malfunction
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null mutants of TbFUT1 demonstrate that it is essential for both the mammalian-infective bloodstream form and the insect vector-dwelling procyclic form. Deletion of TbFUT1 disturbs mitochondrial activity
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physiological function

isoform Fta allows synthesis of H type 2 and H type 3 histo-blood group antigen epitopes at the cell surface. In Chinese hamster ovary cells transfected by FTA, FTA is able to synthesize H type 2 epitopes on a large set of glycoproteins
physiological function
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transfected human DNA sequences in mouse L-cells determine expression of the (alpha-1,2)fucosyltransferases in the mouse transfectants. Primary transfectants express cell surface type II blood group H antigen and (alpha-l,2)fucosyltransferase activity
physiological function
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de novo expression of a H type a-(1,2)-fucosyltransferase transfected into COS-1 cells
physiological function
on allergen inhalation, lung epithelial cells are heavily alpha(1,2)fucosylated by Fut2, which is induced by the IL-13-signal transducer and activator of transcription 6 pathway. Fut2-deficient mice lack lung epithelial fucosylation and show significantly attenuated eosinophilic inflammation and airway hyperresponsiveness in house dust mite-induced asthma models. Complement C3 is accumulated in fucosylated areas. Fut2-/- mice show significantly reduced levels of C3a and impaired accumulation of C3a receptor-expressing monocyte-derived dendritic cells in the lung on house dust mite challenge
physiological function
the enzyme plays an important regulatory role in inflammation, bacterial or viral infection, and tumor metastasis
physiological function
PvFUT2 is induced in the main immune organs (hemocytes and hepatopancreas) of shrimp by Gram-positive (Vibrio parahaemolyticus), Gram-negative (Streptococcus iniae) bacteria and virus (White Spot Syndrome Virus), indicating the involvement of PvFUT2 in shrimp antimicrobial response
physiological function
fucosyltransferase 2 (FUT2) plays a key role in cell adhesion, cell signaling, and tumor growth. Fucosyltransferase 2 (FUT2) is responsible for the production of A, B, and H antigens, as well as alpha-1,2-linked fucosylated glycans (Globo H, and Lewisy, are glycan products of 1, 2-fucosyltransferases, which are highly expressed on malignant tissues)
physiological function
the enzyme catalyzes the biosynthesis of A, B, and H antigens and other important glycans, such as (Sialyl Lewisx) sLex, and (Sialyl Lewisy) sLey. The production of these glycans is increased in various cancers
physiological function
the enzyme is is essential to procyclic and bloodstream form
physiological function
-
the enzyme is is essential to procyclic and bloodstream form
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Basu, S.; Basu, M.; Chien, J.L.
Enzymatic synthesis of a blood group H-related glycosphingolipid by an alpha-fucosyltransferase from bovine spleen
J. Biol. Chem.
250
2956-2962
1975
Bos taurus
brenda
Thurin, J.; Blaszczyk-Thurin, M.
Porcine submaxillary gland GDP-L-fucose: beta-D-galactoside alpha-2-L-fucosyltransferase is likely a counterpart of the human Secretor gene-encoded blood group transferase
J. Biol. Chem.
270
26577-26580
1995
Sus scrofa (Q10982), Sus scrofa
brenda
Masutani, H.; Kimura, H.
Purification and characterization of secretory-type GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase from human gastric mucosa
J. Biochem.
118
541-545
1995
Homo sapiens
brenda
Bureau, V.; Marionneau, S.; Cailleau-Thomas, A.; Le Moullac-Vaidye, B.; Liehr, T.; Le Pendu, J.
Comparison of the three rat GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferases FTA, FTB and FTC
Eur. J. Biochem.
268
1006-1019
2001
Rattus norvegicus (Q10980), Rattus norvegicus (Q10984)
brenda
Carvalho, A.; Harduin-Lepers, A.; Magalhaes, A.; Machado, E.; Mendes, N.; Costa, L.; Matthiesen, R.; Almeida, R.; Costa, J.; Reis, C.
Differential expression of alpha-2,3-sialyltransferases and alpha-1,3/4-fucosyltransferases regulates the levels of sialyl Lewis a and sialyl Lewis x in gastrointestinal carcinoma cells
Int. J. Biochem. Cell Biol.
42
80-89
2010
Homo sapiens (P19526), Homo sapiens (Q10981)
brenda
Cheng, P.W.; DeVries, A.
Mucin biosynthesis. Enzymic properties of human-tracheal epithelial GDP-L-fucose:beta-D-galactoside alpha-(1->2)-L-fucosyltransferase
Carbohydr. Res.
149
253-261
1986
Homo sapiens
brenda
Kyprianou, P.; Betteridge, A.; Donald, A.S.; Watkins, W.M.
Purification of the blood group H gene associated alpha-2-L-fucosyltransferase from human plasma
Glycoconj. J.
7
573-588
1990
Homo sapiens
brenda
Rajan, V.; Larsen, R.; Ajmera, S.; Ernst, L.; Lowe, J.
A cloned human DNA restriction fragment determines expression of a GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase in transfected cells. Evidence for isolation and transfer of the human H blood group locus
J. Biol. Chem.
264
11158-11167
1989
Homo sapiens
brenda
Ernst, L.; Rajan, V.; Larsen, R.; Ruff, M.; Lowe, J.
Stable expression of blood group H determinants and GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase in mouse cells after transfection with human DNA
J. Biol. Chem.
264
3436-3447
1989
Homo sapiens
brenda
Koda, Y.; Soejima, M.; Kimura, H.
Structure and expression of H-type GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase gene (FUT1). Two transcription start sites and alternative splicing generate several forms of FUT1 mRNA
J. Biol. Chem.
272
7501-7505
1997
Homo sapiens
brenda
Larsen, R.; Ernst, L.; Nair, R.; Lowe, J.
Molecular cloning, sequence, and expression of a human GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase cDNA that can form the H blood group antigen
Proc. Natl. Acad. Sci. USA
87
6674-6678
1990
Homo sapiens (P19526)
brenda
Sun, J.; Thurin, J.; Cooper, H.S.; Wang, P.; Mackiewicz, M.; Steplewski, Z.; Blaszczyk-Thurin, M.
Elevated expression of H type GDP-L-fucose:beta-D-galactoside alpha-2-L-fucosyltransferase is associated with human colon adenocarcinoma progression
Proc. Natl. Acad. Sci. USA
92
5724-5728
1995
Homo sapiens
brenda
Ohashi, H.; Ohashi, T.; Misaki, R.; Fujiyama, K.
Arabidopsis thaliana alpha1,2-l-fucosyltransferase catalyzes the transfer of l-galactose to xyloglucan oligosaccharides
FEBS Lett.
593
187-194
2019
Arabidopsis thaliana (Q9SWH5)
brenda
Rocha, J.; Ciceron, F.; Lerouxel, O.; Breton, C.; de Sanctis, D.
The galactoside 2-alpha-L-fucosyltransferase FUT1 from Arabidopsis thaliana crystallization and experimental MAD phasing
Acta Crystallogr. Sect. F
72
564-568
2016
Arabidopsis thaliana (Q9SWH5)
brenda
Zhao, C.; Wu, Y.; Yu, H.; Shah, I.; Li, Y.; Zeng, J.; Liu, B.; Mills, D.; Chen, X.
One-pot multienzyme (OPME) synthesis of human blood group H antigens and a human milk oligosaccharide (HMOS) with highly active Thermosynechococcus elongatus alpha1-2-fucosyltransferase
Chem. Commun. (Camb.)
52
3899-3902
2016
Thermosynechococcus vestitus (Q8DK72)
brenda
Saku, A.; Hirose, K.; Ito, T.; Iwata, A.; Sato, T.; Kaji, H.; Tamachi, T.; Suto, A.; Goto, Y.; Domino, S.; Narimatsu, H.; Kiyono, H.; Nakajima, H.
Fucosyltransferase 2 induces lung epithelial fucosylation and exacerbates house dust mite-induced airway inflammation
J. Allergy Clin. Immunol.
144
698-709.e9
2019
Mus musculus (Q9JL27)
brenda
Barton, S.; Murray, R.; Lillycrop, K.; Inskip, H.; Harvey, N.; Cooper, C.; Karnani, N.; Zolezzi, I.; Sprenger, N.; Godfrey, K.; Binia, A.
FUT2 genetic variants and reported respiratory and gastrointestinal illnesses during infancy
J. Infect. Dis.
219
836-843
2019
Homo sapiens (Q10981)
brenda
Liu, Y.; Jiang, M.; Zheng, Z.; Yao, D.; Yang, S.; Yang, C.; Zhang, Y.; Aweya, J.
Fucosyltransferase 2 is involved in immune-related functions in Penaeus vannamei by modulating antimicrobial peptides’ expression
Dev. Comp. Immunol.
140
104611
2023
Penaeus vannamei (A0A423SVZ3)
brenda
Zemkollari, M.; Ruprecht, C.; Blaukopf, M.; Grabherr, R.; Staudacher, E.
Cloning, expression and characterisation of a novel mollusc alpha-1,2-fucosyltransferase from Crassostrea gigas (CgFUT2)
Glycoconj. J.
41
255-265
2024
Magallana gigas (X4YT24)
brenda
Polanco, G.; Scott, N.; Lye, L.; Beverley, S.
Expanded proteomic survey of the human parasite Leishmania major focusing on changes in null mutants of the Golgi GDP-mannose/fucose/arabinopyranose transporter LPG2 and of the mitochondrial fucosyltransferase FUT1
Microbiol. Spectr.
10
e70272
2022
Trypanosoma brucei brucei (Q38FH1), Trypanosoma brucei brucei 927/4 (Q38FH1)
brenda
Zafar, H.; Atif, M.; Choudhary, M.
Fucosyltransferase 2 inhibitors identification via docking and STD-NMR studies
PLoS ONE
16
e0257623
2021
Homo sapiens (Q10981)
brenda
Atif, M.; Zafar, H.; Wahab, A.; Choudhary, M.
Drug repurposing against fucosyltransferase-2 via docking, STD-NMR, and molecular dynamic simulation studies
PLoS ONE
19
e0308517
2024
Homo sapiens (Q10981)
brenda