Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.4.1.65 - 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase and Organism(s) Pongo pygmaeus and UniProt Accession Q8HYJ4

for references in articles please use BRENDA:EC2.4.1.65
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This enzyme is the product of the Lewis blood group gene. Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. Although it is a 4-fucosyltransferase, it has a persistent 3-fucosyltransferase activity towards the glucose residue in free lactose. This enzyme fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3, unlike EC 2.4.1.152, 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase, which fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4. Enzymes catalysing the 4-alpha-fucosylation of the GlcNAc in beta-D-Gal-(1->3)-beta-GlcNAc sequences (with some activity also as 3-alpha-fucosyltransferases) are present in plants, where the function in vivo is the modification of N-glycans. In addition, the fucTa gene of Helicobacter strain UA948 encodes a fucosyltransferase with both 3-alpha- and 4-alpha-fucosyltransferase activities.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pongo pygmaeus
UNIPROT: Q8HYJ4
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Pongo pygmaeus
The enzyme appears in selected viruses and cellular organisms
Synonyms
fuc-t, fuc-tiii, alpha-1,3-fucosyltransferase, fucosyltransferase iv, fuct-iii, fuct-vi, fuct v, fuct iii, fucosyltransferase vi, ft-iv, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-3/4-FUT
-
fucosyltransferase 5
-
Lewis alpha-3/4-fucosyltransferase
-
(Lea)-dependent alpha-3/4-fucosyltransferase
-
-
-
-
alpha(1,3/1,4) fucosyltransferase III
-
-
-
-
alpha(1,3/4) fucosyltransferase
-
-
-
-
alpha-(1->4)-L-fucosyltransferase
-
-
-
-
alpha-3/4-FUT
-
alpha-4-L-fucosyltransferase
-
-
-
-
alpha4-fucosyltransferase
-
-
-
-
alpha4-FucT
-
-
-
-
beta-acetylglucosaminylsaccharide fucosyltransferase
-
-
-
-
blood group Lewis alpha-4-fucosyltransferase
-
-
-
-
blood-group substance Lea-dependent fucosyltransferase
-
-
-
-
Fuc-TIII
-
-
-
-
fucosyltransferase 3
-
fucosyltransferase, guanosine diphosphofucose-beta-acetylglucosaminylsaccharide 4-alpha-L-
-
-
-
-
fucosyltransferase, guanosine diphosphofucose-glycoprotein 4-alpha-
-
-
-
-
FucT-II
-
-
-
-
FucTIII
-
-
-
-
guanosine diphosphofucose-glycoprotein 4-alpha-L-fucosyltransferase
-
-
-
-
Lewis alpha-3/4-fucosyltransferase
Lewis alpha1-3/4 fucosyltransferase
-
-
-
-
Lewis blood group alpha1-3/4 fucosyltransferase
-
-
-
-
Lewis(Le) blood group gene-dependent alpha-3/4-L-fucosyltransferase
-
-
-
-
SFT3
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
hexosyl group transfer
SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R 4I-alpha-L-fucosyltransferase
This enzyme is the product of the Lewis blood group gene. Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. Although it is a 4-fucosyltransferase, it has a persistent 3-fucosyltransferase activity towards the glucose residue in free lactose. This enzyme fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3, unlike EC 2.4.1.152, 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase, which fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4. Enzymes catalysing the 4-alpha-fucosylation of the GlcNAc in beta-D-Gal-(1->3)-beta-GlcNAc sequences (with some activity also as 3-alpha-fucosyltransferases) are present in plants, where the function in vivo is the modification of N-glycans. In addition, the fucTa gene of Helicobacter strain UA948 encodes a fucosyltransferase with both 3-alpha- and 4-alpha-fucosyltransferase activities.
CAS REGISTRY NUMBER
COMMENTARY hide
37277-69-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GDP-fucose + Fuc-alpha-1,2Gal-beta-1,3GlcNAc-sp-biotin
GDP + Fuc-alpha-1,2Gal-beta-1,3(Fuc-alpha-1,4)GlcNAc-sp-biotin
show the reaction diagram
type 1 reaction
-
-
?
GDP-fucose + Fuc-alpha-1,2Gal-beta-1,4GlcNAc-sp-biotin
GDP + Fuc-alpha-1,2Gal-beta-1,4(Fuc-alpha-1,3)GlcNAc-sp-biotin
show the reaction diagram
type 2 reaction
-
-
?
GDP-fucose + Fuc-alpha-1,2Gal-beta-1,3GlcNAc-sp-biotin
GDP + Fuc-alpha-1,2Gal-beta-1,3(Fuc-alpha-1,4)GlcNAc-sp-biotin
show the reaction diagram
type 1 reaction
-
-
?
GDP-fucose + Fuc-alpha-1,2Gal-beta-1,4GlcNAc-sp-biotin
GDP + Fuc-alpha-1,2Gal-beta-1,4(Fuc-alpha-1,3)GlcNAc-sp-biotin
show the reaction diagram
type 2 reaction
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FUT5_PONPY
374
0
43035
Swiss-Prot
Secretory Pathway (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dupuy, F.; Germot, A.; Julien, R.; Maftah, A.
Structure/function study of Lewis alpha3- and alpha3/4-fucosyltransferases: the alpha1,4 fucosylation requires an aromatic residue in the acceptor-binding domain
Glycobiology
14
347-356
2004
Homo sapiens (P21217), Homo sapiens (P51993), Homo sapiens (Q11128), Hylobates lar (Q8HYJ3), Pongo pygmaeus (Q8HYJ4), Pongo pygmaeus (Q8HYJ5), Gorilla gorilla (Q8HYJ6), Gorilla gorilla (Q8HYJ7)
Manually annotated by BRENDA team