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Information on EC 2.4.1.344 - type 2 galactoside alpha-(1,2)-fucosyltransferase and Organism(s) Homo sapiens and UniProt Accession P19526
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2.4.1.344 type 2 galactoside alpha-(1,2)-fucosyltransferaseIUBMB Comments
The enzyme acts on a glycoconjugates where R (see reaction) is a glycoprotein or glycosphingolipid. The recognized moiety of the substrate is known as a type 2 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 2 antigen. Humans possess two enzymes able to catalyse this reaction, encoded by the FUT1 and FUT2 genes (also known as the H and Secretor genes, respectively), but only FUT1 is expressed in red blood cells. cf. EC 2.4.1.69, type 1 galactoside alpha-(1,2)-fucosyltransferase.
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
gdp-l-fucose:beta-d-galactoside alpha-2-l-fucosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FUT1
FUT2
guanosine diphosphofucose-glycoprotein 2-alpha-fucosyltransferase
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-
-
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guanosine diphosphofucose-lactose fucosyltransferase
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-
-
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H-gene-encoded beta-galactoside alpha(1->2)fucosyltransferase
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-
-
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FUT1
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-
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FUT2
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-
PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R alpha-(1,2)-L-fucosyltransferase (configuration-inverting)
The enzyme acts on a glycoconjugates where R (see reaction) is a glycoprotein or glycosphingolipid. The recognized moiety of the substrate is known as a type 2 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 2 antigen. Humans possess two enzymes able to catalyse this reaction, encoded by the FUT1 and FUT2 genes (also known as the H and Secretor genes, respectively), but only FUT1 is expressed in red blood cells. cf. EC 2.4.1.69, type 1 galactoside alpha-(1,2)-fucosyltransferase.
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
GDP-beta-L-fucose + 2-nitrophenyl beta-D-galactopyranoside
GDP + 2-nitrophenyl alpha-L-fucosyl-(1->2)-beta-D-galactopyranoside
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-
137% of the activity with phenyl beta-D-galactopyranoside
-
?
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
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i.e. lacto-N-tetraose, residues of H type 1 epitopes, reaction of EC 2.4.1.69
131% of the activity with phenyl beta-D-galactopyranoside
-
?
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
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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
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i.e. lacto-N-neotetraose, residues of H type 2 epitopes
113% of the activity with phenyl beta-D-galactopyranoside
-
?
GDP-beta-L-fucose + freezing point-depressing glycoprotein
GDP + alpha-L-fucosyl-freezing point-depressing glycoprotein
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-
-
-
?
GDP-beta-L-fucose + phenyl beta-D-galactopyranoside
GDP + phenyl alpha-L-fucosyl-(1->2)-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
-
i.e. lacto-N-biose I
reaction of EC 2.4.1.69
-
?
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
-
i.e. lacto-N-biose I, reaction of EC 2.4.1.69
82% of the activity with phenyl beta-D-galactopyranoside
-
?
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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i.e. N-acetyllactosamine
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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
-
i.e. N-acetyllactosamine
80% of the activity with phenyl beta-D-galactopyranoside
-
?
additional information
?
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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
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-
?
additional information
?
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enzyme transfers L-fucose from GDP-L-fucose to an acceptor containing a beta-D-galactopyranosyl group at the nonreducing terminal
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?
additional information
?
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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
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
Mg2+
Mn2+
additional information
-
divalent cation is absolutely required, no activation with Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
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i.e. lacto-N-tetraose, competitive with respect to N-acetyllactosamine
beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
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i.e. lacto-N-neotetraose, competitive with respect to lacto-N-biose I
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.4
beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
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pH 7.0, 37°C
5
beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
-
pH 7.0, 37°C
1.1
beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine
-
pH 7.2, temperature not specified in the publication
13
phenyl beta-D-galactopyranoside
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pH 7.2, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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de novo expression of a H type a-(1,2)-fucosyltransferase transfected into COS-1 cells
physiological function
-
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
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). FUT1_HUMAN
365
1
41251
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the COOH-terminal domain predicted to be Golgi-resident in COS-1 cells as a catalytically active, secreted, and soluble protein A fusion peptide
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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FUT1 transcript is expressed in some of tumor cell lines. The FUT1 transcript has several forms generated by two distinct transcription start sites and alternative splicing. Two transcription initiation sites of the FUT1 have been identified in gastric cancer cells and in ovarian cancer cells. Only exon 1A is a transcription start site in one more gastric cancer cell line, two colonic cancer cell lines, and in K562 cells, whereas only exon 2A has been identified in HEL cells and in bone marrow cells
medicine
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transcript level for beta-D-galactoside alpha-2-L-fucosyltransferase is 40- and 340fold increased in all adenocarcinomas and tumor cell lines, respectively, compared to normal colon mucosa where a low level of mRNA transcript is detected. A variable increase in mRNA transcript levels is observed in 50% of adenomatous polyps. There are no tumor-associated allelic variations found within the H beta-D-galactoside alpha-2-Lfucosyltransferase cDNA
medicine
FUT2 SNPs rs601338 and rs602662 are associated with the risks of respiratory and diarrheal illnesses, as well as vomiting and nocturnal cough, from birth to 24 months of age in infants. The risk of diarrheal infections is significantly higher among infants possessing the G allele as compared to those with the A alleles in FUT2 SNPs. Longer breastfeeding duration predicted a lower risk of diarrhea, independent of infant FUT2 genotype
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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)
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
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)
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