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Information on EC 2.4.1.69 - type 1 galactoside alpha-(1,2)-fucosyltransferase and Organism(s) Mus musculus and UniProt Accession Q9JL27
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2.4.1.69 type 1 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 1 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 1 antigen. In humans the main enzyme performing this reaction is encoded by the FUT2 gene (also known as the Secretor gene), which is also able to act on type 2 substrates (see EC 2.4.1.344). The enzyme from the bacterium Helicobacter pylori cannot act on type 2 substrates.
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Word Map
- 2.4.1.69
-
fucosylation
- oligosaccharide
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sialylated
- glycans
- glycosyltransferases
- epitope
- lectin
-
sialyltransferase
- glycolipids
- selectins
- glycoconjugates
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histo-blood
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n-acetylglucosaminyltransferase
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fucts
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e-selectin
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nonsecretors
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sialyl-lewis
- asialofetuin
- alpha-l-fucosidase
- xyloglucan
-
lewisa
-
hyperacute
-
fucosidase
- 2'-fucosyllactose
- n-acetyllactosamine
-
h-type
-
bombay
- lactosamine
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xenoreactive
- psgl-1
-
fucose-containing
- fuct-vii
- analysis
-
difucosylated
- gnt-iii
-
hbgas
-
alpha1-6
- medicine
- noroviruses
-
1-3glcnac
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xenoantigens
-
xylosyltransferase
-
glycomic
- lacnac
- synthesis
- neuac
- alpha-gal
-
alpha1,3-galactosyltransferase
- tamarind
- lacto-n-biose
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
fucosyltransferase, alpha1,2-fucosyltransferase, alpha(1,2)fucosyltransferase, fucosyltransferase 2, alpha1,2-ft, alpha(1,2)-fucosyltransferase, alpha-2-l-fucosyltransferase, fucosyltransferase 1, alpha-1,2-fucosyltransferase, alpha1,2ft, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-(1->2)-L-fucosyltransferase
-
-
-
-
alpha-2-fucosyltransferase
alpha-2-L-fucosyltransferase
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-
-
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alpha-L-fucosyltransferase
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-
-
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alpha1,2FT
-
-
-
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alpha1-2FucT
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-
-
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beta-galactoside alpha1-2fucosyltransferase
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-
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blood group H alpha-2-fucosyltransferase
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-
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blood-group substance H-dependent fucosyltransferase
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-
-
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fucosyltransferase, guanosine diphosphofucose-galactoside 2-L-
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-
-
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fucosyltransferase, guanosine diphosphofucose-glycoprotein 2-alpha-
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-
-
-
fucosyltransferase, guanosine diphosphofucose-lactose
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-
-
-
FucT
-
-
-
-
galactoside 2-alpha-L-fucosyltransferase
-
-
-
-
GDP fucose-lactose fucosyltransferase
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-
-
-
GDP-beta-L-fucose:beta-D-galactosyl-R 2-alpha-L-fucosyltransferase
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-
-
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GDP-fucose:GM1 alpha1-2fucosyltransferase
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-
-
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GDP-L-fucose:beta-D-galactosyl-R-alpha-L-fucosyltransferase
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-
-
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GDP-L-fucose:lactose fucosyltransferase
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-
-
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GDPFuc:beta-D-galactoside alpha1,2-fucosyltransferase
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-
-
-
guanosine diphospho-L-fucose-lactose fucosyltransferase
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-
-
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guanosine diphosphofucose-beta-D-galactosyl-alpha-2-L-fucosyltransferase
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-
-
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guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide alpha-L-fucosyltransferase
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-
-
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guanosine diphosphofucose-glycoprotein 2-alpha-L-fucosyltransferase
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-
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H gene-encoded beta-galactoside alpha1->2 fucosyltransferase
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-
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H-gene-encoded beta-galactoside alpha1-2fucosyltransferase
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-
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Se gene-encoded beta-galactoside alpha1->2 fucosyltransferase
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-
-
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secretor-type beta-galactoside alpha1-2fucosyltransferase
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-
-
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alpha-2-fucosyltransferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:beta-D-galactosyl-(1->3)-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 1 histo-blood group antigen precursor disaccharide, and the action of the enzyme produces an H type 1 antigen. In humans the main enzyme performing this reaction is encoded by the FUT2 gene (also known as the Secretor gene), which is also able to act on type 2 substrates (see EC 2.4.1.344). The enzyme from the bacterium Helicobacter pylori cannot act on type 2 substrates.
CAS REGISTRY NUMBER
COMMENTARY
56093-23-3
-
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-L-fucose + lacto-N-biose 1
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAc
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-
-
-
?
GDP-L-fucose + N-acetyllactosamine
GDP + alpha-L-fucosyl-1,2-N-acetyllactosamine
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-
-
-
?
GDP-L-fucose + phenyl-beta-D-galactoside
GDP + phenyl 2-O-(alpha-L-fucopyranosyl)-beta-D-galactopyranoside
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-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
-
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
the galactoside 2-alpha-L-fucosyltransferase gene determines the expression of terminal L-Fucalpha(1-2)Galbeta epitopes
-
-
?
additional information
?
-
P97327
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
additional information
?
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
additional information
?
-
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
additional information
?
-
P97327
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
additional information
?
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
additional information
?
-
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
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
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
the galactoside 2-alpha-L-fucosyltransferase gene determines the expression of terminal L-Fucalpha(1-2)Galbeta epitopes
-
-
?
additional information
?
-
P97327
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
additional information
?
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
additional information
?
-
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
additional information
?
-
P97327
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
additional information
?
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
additional information
?
-
-
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.079
GDP-L-fucose
-
reaction with phenyl-beta-D-galactoside, recombinant enzyme
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.
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). FUT2_MOUSE
347
1
39243
Swiss-Prot
Secretory Pathway (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
P97327, Q9JL27
transfection of the mouse Fut1 and Fut2, and human FUT1 genes into human ovarian carcinoma-derived RMG-1 cells results in 2030fold increases in cellular alpha1,2-fucosyltransferase activity, and in alteration of the glycolipid composition, including not only fucosylated products, but also precursor glycolipids
P97327, Q9JL27
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Fut4 mRNA expression is increased following coculture of epithelial cells with macrophages for 24 h (1.3fold) or 48 h (1.2fold)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Domino, S.E.; Hiraiwa, N.; Lowe, J.B.
Molecular cloning, chromosomal assignment and tissue-specific expression of a murine alpha-(1,2)fucosyltransferase expressed in thymic and epididymal epithelial cells
Biochem. J.
327
105-115
1997
Homo sapiens, Mus musculus
-
Iwamori, M.; Tanaka, K.; Kubushiro, K.; Lin, B.; Kiguchi, K.; Ishiwata, I.; Tsukazaki, K.; Nozawa, S.
Alterations in the glycolipid composition and cellular properties of ovarian carcinoma-derived RMG-1 cells on transfection of the alpha1,2-fucosyltransferase gene
Cancer Sci.
96
26-30
2005
Homo sapiens (P19526), Homo sapiens, Mus musculus (P97327), Mus musculus (Q9JL27), Mus musculus
Abrantes, J.; Posada, D.; Guillon, P.; Esteves, P.J.; Le Pendu, J.
Widespread gene conversion of alpha-2-fucosyltransferase genes in mammals
J. Mol. Evol.
69
22-31
2009
Bos taurus (A4IFH1), Bos taurus (Q28113), Bos taurus (Q9TTY3), Chlorocebus sabaeus, Chlorocebus sabaeus (O77711), Chlorocebus sabaeus (O77712), Gorilla gorilla (O77486), Gorilla gorilla (Q9TUD4), Homo sapiens (P19526), Homo sapiens (Q10981), Homo sapiens (Q5XLR8), Homo sapiens, Hylobates agilis (Q6LA46), Hylobates lar (Q9TTC7), Macaca fascicularis (Q9N266), Monodelphis domestica, Mus musculus (O09160), Mus musculus (P97353), Oryctolagus cuniculus (Q10979), Oryctolagus cuniculus (Q10983), Oryctolagus cuniculus (Q29505), Oryctolagus cuniculus, Pan troglodytes (O77485), Pan troglodytes (Q9TUD6), Pongo pygmaeus (O77487), Pongo pygmaeus (Q6LA45), Rattus norvegicus (Q10980), Rattus norvegicus (Q10984), Rattus norvegicus (Q9WUE6), Sus scrofa (Q10982), Sus scrofa (Q29043), Xenopus tropicalis
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