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Information on EC 2.4.1.69 - type 1 galactoside alpha-(1,2)-fucosyltransferase and Organism(s) Sus scrofa and UniProt Accession Q10982
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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
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lewisa
-
hyperacute
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fucosidase
- 2'-fucosyllactose
- n-acetyllactosamine
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h-type
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bombay
- lactosamine
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xenoreactive
- psgl-1
-
fucose-containing
- fuct-vii
- analysis
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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: Sus scrofa
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
-
-
-
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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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-
-
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alpha1,2fucosyltransferase
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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-
-
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fucosyltransferase, guanosine diphosphofucose-lactose
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-
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FucT
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-
-
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galactoside 2-alpha-L-fucosyltransferase
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-
-
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GDP fucose-lactose fucosyltransferase
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-
-
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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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-
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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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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-R = GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-R
either a rapid equilibrium random kinetic mechanism or a steady state ordered mechanism with GDP-L-fucose binding first
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
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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 + D-Galbeta(1-2)D-Xylalpha(1-6)D-Glcbeta(1-4)D-Glc
GDP + L-Fucalpha(1-2)-D-Galbeta1-2-D-Xylalpha1-6-D-Glcbeta1-4-D-Glc
-
-
-
?
GDP-L-fucose + GalalphaCH3
GDP + L-Fucalpha(1-2)GalalphaCH3
-
0.1% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-2)D-Xyl
GDP + L-Fucalpha(1-2)D-Galbeta(1-2)D-Xyl
-
-
-
?
GDP-L-fucose + Galbeta(1-3)Ara
GDP + L-Fucalpha(1-2)Galbeta(1-3)Ara
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3.3% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-3)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-3)GalNAc
-
-
-
-
?
GDP-L-fucose + Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
GDP + L-Fucalpha(1-2)Galbeta(1-3)GlcNAcbeta(1-3)Galbeta(1-4)Glc
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84% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-4)Glc
GDP + L-Fucalpha(1-2)Galbeta(1-4)Glc
-
4.2% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-4)GlcNAc
GDP + L-Fucalpha(1-2)Galbeta(1-4)GlcNAc
-
7.5% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-4)GlcNAc(1-3)Galbeta(1-4)Glc
GDP + L-Fucalpha(1-2)Galbeta(1-4)GlcNAc(1-3)Glabeta(1-4)Glc
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2.8% of the activity with Galbeta(1-3)GalNAc
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-
?
GDP-L-fucose + Galbeta(1-4)Man
GDP + L-Fucalpha(1-2)Galbeta(1-4)Man
-
2.7% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + Galbeta(1-6)GalNAc
GDP + L-Fucalpha(1-2)Galbeta(1-6)GalNAc
-
4.8% of the activity with Galbeta1-3GalNAc
-
-
?
GDP-L-fucose + GalbetaCH3
GDP + L-Fucalpha(1-2)GalbetaCH3
-
2.6% of the activity with Galbeta1-3GalNAc
-
-
?
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 enzyme forms the Fuc(1-2)Gal linkage with oligosaccharides, glycoproteins, and glycolipids which contain nonreducing terminal galactose residues and shows no absolute specificity for a particular penultimate residue or for the linkage between the galactose and the penultimate residue. The enzyme fucosylates human Bombay" erythrocytes which lack cell surface Fucalpha1-2Gal structures
-
-
?
GDP-L-fucose + beta-D-galactosyl-R
GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
-
the enzyme forms exclusively L-Fucalpha(1-2)Gal linkage with a variety of acceptor substrates
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
the enzyme is active in absence of divalent metal ions, but is stimulated by Mn2+, Mg2+, Ca2+ or Co2+
Co2+
-
the enzyme is active in absence of divalent metal ions, but is stimulated by Mn2+, Mg2+, Ca2+ or Co2+
Mg2+
-
the enzyme is active in absence of divalent metal ions, but is stimulated by Mn2+, Mg2+, Ca2+ or Co2+
Mn2+
-
the enzyme is active in absence of divalent metal ions, but is stimulated by Mn2+, Mg2+, Ca2+ or Co2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
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
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.
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_PIG
340
1
38987
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
two enzyme species of 55000 Da and 60000 Da detected by SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
subcloned in COS-7 or CHOP cells (Chinese hamster ovary cells transformed with Polyoma large T antigen)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beyer, T.A.; Sadler, J.E.; Hill, R.L.
Purification to homogeneity of H blood group beta-galactoside alpha 1->2 fucosyltransferase from porcine submaxillary gland
J. Biol. Chem.
255
5364-5372
1980
Sus scrofa
Beyer, T.A.; Hill, R.L.
Enzymatic properties of the beta-galactoside alpha 1->2 fucosyltransferase from porcine submaxillary gland
J. Biol. Chem.
255
5373-5379
1980
Sus scrofa
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
Druzhinina, T.N.; Sizova, O.V.; Shibaev, V.N.
Fucosylation of synthetic oligosaccharides - plant xyloglucan fragments - by mammalian and amphibian fucosyltransferases
Biochemistry (Moscow)
62
62-65
1997
Rana temporaria, Rattus norvegicus, Sus scrofa, Xenopus laevis
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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