Information on EC 2.4.1.37 - fucosylgalactoside 3-alpha-galactosyltransferase

New: Word Map on EC 2.4.1.37
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.4.1.37
-
RECOMMENDED NAME
GeneOntology No.
fucosylgalactoside 3-alpha-galactosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl(1->2)]-D-galactosyl-R (where R can be OH, an oligosaccharide or a glycoconjugate)
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycosphingolipid biosynthesis - lacto and neolacto series
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:alpha-L-fucosyl-(1->2)-D-galactoside 3-alpha-D-galactosyltransferase
Acts on blood group substance, and can use a number of 2-fucosyl-galactosides as acceptors.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
blood-group substance B-dependent galactosyltransferase
-
-
-
-
glycoprotein-fucosylgalactoside alpha-galactosyltransferase
-
-
-
-
histo-blood group B transferase
-
-
-
-
histo-blood substance B-dependent galactosyltransferase
-
-
-
-
UDP-galactose:O-alpha-L-fucosyl(1-2)D-galactose alpha-D-galactosyltransferase
-
-
-
-
UDPgalactose:glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose 3-alpha-D-galactosyltransferase
-
-
-
-
[blood group substance] alpha-galactosyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37257-33-3
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Skp1B overexpressing strain HW302
-
-
Manually annotated by BRENDA team
blood group B donors
-
-
Manually annotated by BRENDA team
fragment; ABO gene
UniProt
Manually annotated by BRENDA team
genotype Wu4, P234A-mutant, heterozygot B/0; only four amino acids are responsible for B and A blood group enzymes R176G, G235S, L266M and G268A, the latter two amino acids are responsible for the difference in donor specificity and the first two have roles in acceptor binding and turnover
-
-
Manually annotated by BRENDA team
only four amino acids are responsible for B and A blood group enzymes R176G, G235S, L266M and G268A, the latter two amino acids are responsible for the difference in donor specificity and the first two have roles in acceptor binding and turnover
Uniprot
Manually annotated by BRENDA team
only four amino acids are responsible for B and A blood group enzymes R176G, G235S, L266M and G268A, the latter two amino acids are responsible for the difference in donor specificity and the first two have roles in acceptor binding and turnover
-
-
Manually annotated by BRENDA team
recombinantly expressed in Escherichia coli
Uniprot
Manually annotated by BRENDA team
recombinantly expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
white-handed gibbon
-
-
Manually annotated by BRENDA team
japanese monkey
-
-
Manually annotated by BRENDA team
strain BFM/2Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
Mus musculus brevirostris BFM/2Msf
strain BFM/2Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
strain CAST/Ei and HMI/Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
Mus musculus castaneus CAST/Ei
strain CAST/Ei and HMI/Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
strain BALB/c, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
Mus musculus domesticus BALB/c
strain BALB/c, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
strain ZBN, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
-
-
Manually annotated by BRENDA team
Mus spicilegus ZBN
strain ZBN, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
-
-
Manually annotated by BRENDA team
2 distinct alpha-3-D-galactosyltransferases: one which is more tightly membrane-bound, resembles the human B-gene-specific transferase in its acceptor specificity, and the second, which is a more soluble enzyme transfers D-galactose to the same positional linkage in unsubstituted beta-D-galactosyl residues
-
-
Manually annotated by BRENDA team
blood group B donors
-
-
Manually annotated by BRENDA team
B-type gene Abo2
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
human blood group B galactosyltransferase responsible for the biosynthesis of human blood group antigens
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-2-deoxygalactose + L-fucosyl-alpha-1,2-beta-galactosyl-OR
UDP + 2-deoxy-alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-OR
show the reaction diagram
-
tetramethylrhodamine labelled disaccharide
-
-
?
UDP-6-deoxygalactose + L-fucosyl-alpha-1,2-beta-galactosyl-OR
UDP + 6-deoxy-alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-OR
show the reaction diagram
-
tetramethylrhodamine labelled disaccharide
-
-
?
UDP-alpha-D-galactose + 8-methoxycarbonyloctyl beta-D-Galp-(1->4)-beta-D-Glcp
?
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-galactose + alpha-L-Fuc-(1-2)-beta-D-Gal-octyl
?
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-galactose + alpha-L-Fuc-(1->2)-beta-D-Gal-octal
?
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
show the reaction diagram
-
GTB, the blood group B enzyme is able to catalyze the synthesis of iGb3 in vitro, however, the rate observed is too low in order to account for iGb3 synthesis in vivo
-
-
?
UDP-D-galactose + 2'-fucosyllactose
UDP + D-galactosyl-(1-3)-2'-fucosyllactose
show the reaction diagram
Q8CFC4
-
-
-
?
UDP-D-galactose + alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-DGlcNAcp-O(CH2)7CH3
UDP + alpha-L-Fuc-(1,2)-[alpha-D-Galp-(1,3)-]-beta-D-Galp-(1,3)-beta-DGlcNAcp-O(CH2)7CH3
show the reaction diagram
-
69% of the activity with alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
-
-
?
UDP-D-galactose + alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
UDP + alpha-L-Fucp-(1,2)-[alpha-D-Galp-(1,3)-]-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
show the reaction diagram
-
90% of the activity with alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
-
-
?
UDP-D-galactose + alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
UDP + alpha-L-Fuc-(1,2)-[alpha-D-Galp-(1,3)-]-beta-D-Galp-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-(4-nitrophenol)
UDP + alpha-D-Gal-1,3-Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-(4-nitrophenol)
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-benzyl
UDP + alpha-D-Gal(1,3)Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-benzyl
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-Skp1 protein
UDP + alpha-D-Gal(1,3)Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-Skp1 protein
show the reaction diagram
-
best substrate, Skp1A1-(HW120)-myc and Skp1 from strain HL250
-
-
?
UDP-D-galactose + Fucalpha(1,2)Galbeta-1-(4-nitrophenol)
UDP + alpha-D-Gal(1,3)Fucalpha(1,2)Galbeta-1-(4-nitrophenol)
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha(1,2)Galbeta-1-benzyl
UDP + alpha-D-Gal(1,3)Fucalpha(1,2)Galbeta-1-benzyl
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha-1-(4-nitrophenol)
UDP + alpha-D-Gal(1,3)Fucalpha-1-(4-nitrophenol)
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha-1-benzyl
UDP + alpha-D-Gal(1,3)Fucalpha-1-benzyl
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + fucosylated Skp1 protein
UDP + alpha-D-galactosyl(1-3)-fucosyl-Skp1 protein
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + H type 3-Sp-biotin
UDP + ?
show the reaction diagram
Q8CFC4
preferred substrates
-
-
?
UDP-D-galactose + H-disaccharide
UDP + alpha-D-galactosyl-1,3-H disaccharide
show the reaction diagram
-
synthetic substrate
-
-
?
UDP-galactose + 2'-fucosyllactose
UDP + alpha-D-galactosyl-1,3-[2'-fucosyllactose]
show the reaction diagram
-
-
-
-
?
UDP-galactose + 2'-fucosyllactose
UDP + alpha-D-galactosyl-1,3-[2'-fucosyllactose]
show the reaction diagram
-
-
-
-
?
UDP-galactose + alpha-L-Fuc-(1,2)-beta-D-Gal-O-octyl
UDP + alpha-L-Fuc(1,2)-[alpha-D-Galp-(1,3)-]-beta-D-Gal-O-octyl
show the reaction diagram
P16442
it is propose that, upon acceptor binding, GTB uses the Asp302 and Glu303 side chains as molecular tweezers to promote bound UDP-Gal but not UDP-Glc into a transition state that leads to product formation
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-O-(CH2)7CH3
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-beta-D-galactosyl-O-(CH2)7CH3
show the reaction diagram
-
i.e. alpha-L-Fucp-(1,2)-beta-DGalp-O-(CH2)7CH3
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactose
show the reaction diagram
-
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactose
show the reaction diagram
-
i.e. H disaccharide
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactose
show the reaction diagram
-
i.e. H disaccharide
in the absence of UDP and Mn2+, GTB recognizes its trisaccharide product with a low affinity of about 1 mM, while the presence of UDP and Mn2+ precludes B-trisaccharide binding
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-R
show the reaction diagram
-
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-R
show the reaction diagram
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-R
show the reaction diagram
-
importance of residue M214 for donor enzyme specificity
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactosyl-R
show the reaction diagram
-
substrate binding structure and residues involved, overview
-
-
?
UDP-galactose + alpha-L-fucosyl-(1-2)-D-galactosyl-O-R
UDP + alpha-D-galactosyl-(1-3)-[alpha-L-fucosyl-(1-2)]-D-galactosyl-O-R
show the reaction diagram
-
H-antigen disaccharide, H-antigen disaccharide, Met226 is responsible for substrate specificity for D-galactose as donor substrate, acceptor substrate binding pocket structure, overview
-
-
-
UDP-galactose + blood group antigen
UDP + alpha-D-galactosyl-blood group antigen
show the reaction diagram
-
GTB catalyzes the transfer of galactose from UDP-Gal to the C3 position of the terminal galactose of H antigen acceptors
-
-
?
UDP-galactose + blood group antigen H
UDP + alpha-D-galactosyl-blood group antigen H
show the reaction diagram
-
GTB catalyzes the transfer of galactose from UDP-Gal to the C3 position of the terminal galactose of H antigen acceptors
-
-
?
UDP-galactose + blood group antigen H
UDP + alpha-D-galactosyl-blood group antigen H
show the reaction diagram
-
the alpha1,3-galactosyl epitope is a major xenotransplant antigen
-
-
?
UDP-galactose + blood group antigen H
UDP + alpha-D-galactosyl-blood group antigen H
show the reaction diagram
-
alpha-L-fucosyl-(1,2)-D-galactosyl-antigen H
alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactosyl-antigen H
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
P16442
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
-
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
-
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
-
-
-
-
-
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
-
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
P38649
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
-
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
-
-
-
-
-
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
-
converts blood group 0 red blood cells to B-cells
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
-
enzyme transfers D-galactose in alpha-linkage to oligosaccharides, glycolipids and glycoproteins with terminal non-reducing H-active structures and confers blood group B activity on group 0 erythrocytes
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
-
acts on blood group substance
-
-
-
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
Mus spicilegus ZBN
-
-
-
-
?
UDP-galactose + H-active glycoprotein
UDP + B-active substance
show the reaction diagram
-
-
-
?
UDP-galactose + L-2'-L-fucosyllactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactosyl-D-glucose
show the reaction diagram
-
-
-
-
?
UDP-galactose + L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3
UDP + alpha-D-galactosyl-1,3[alpha-L-fucosyl-1,2]-alpha-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
UDP + alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
P16442
-
-
-
?
UDP-galactose + L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
UDP + alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
?
UDP-galactose + L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
UDP + alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
UDP + alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
tetramethylrhodamine labelled disaccharide
-
-
?
UDP-galactose + lacto-N-fucopentaose I
UDP + alpha-D-galactosyl-1,3-[lacto-N-fucopentaose I]
show the reaction diagram
-
-
-
-
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-[N-acetyl-lactosamine]
show the reaction diagram
-
-
-
-
?
UDP-galactose + O-alpha-L-fucosyl-1,2-galactose
UDP + alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactopyranoside
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl 3-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[3-O-methyl-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl 4-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[4-O-methyl-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl 6'-amino-6'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[6'-amino-6'-deoxy-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
-
UDP-galactose + octyl 6'-amino-6'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[6'-amino-6'-deoxy-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl 6'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[6'-deoxy-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl 6'-fluoro-6'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[6'-fluoro-6'-deoxy-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl 6'-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[6'-O-methyl-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
-
UDP-galactose + octyl 6'-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[6'-O-methyl-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl alpha-L-xylo-hexopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[alpha-L-xylo-hexopyranosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-glucose + Fucalpha1-2Galbeta-O(CH2)7CH3
?
show the reaction diagram
-
wild-type enzyme shows very low activity. Mutants, Ser185Asn and Ser185Cys, exhibit 4.3fold and 4.8fold elevation in kcat/Km for UDP-glucose relative to that of wild-type enzyme
-
-
?
UDP-glucose + L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
UDP + alpha-D-glucosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
?
UDP-glucose + L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
UDP + alpha-D-glucosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactose + 2'-fucosyllactose
UDP + N-acetyl-D-galactosyl-(1-3)-2'-fucosyllactose
show the reaction diagram
Q8CFC4
low A-type activity
-
-
?
UDP-N-acetyl-D-galactose + H type 3-Sp-biotin
UDP + ?
show the reaction diagram
Q8CFC4
low A-type activity
-
-
?
UDP-N-acetylgalactosamine + 2'-fucosyllactose
UDP + N-acetyl-alpha-D-galactosyl-1,3-[2'-fucosyllactose]
show the reaction diagram
-
-
-
-
?
UDP-N-acetylgalactosamine + L-2'-fucosyllactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-D-glucose
show the reaction diagram
-
-
-
-
?
UDP-N-acetylgalactosamine + L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3
UDP + N-acetyl-alpha-D-galactosyl-1,3[alpha-L-fucosyl-1,2]-alpha-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-N-acetylgalactosamine + L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
UDP + N-acetyl-alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + UDP-GalNAc
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
2 distinct alpha-3-D-galactosyltransferases: one which is more tightly membrane-bound, resembles the human B-gene-specific transferase in its acceptor specificity, and the second, which is a more soluble enzyme transfers D-galactose to the same positional linkage in unsubstituted beta-D-galactosyl residues
-
-
-
additional information
?
-
-
substrate specificity, enzyme forms Galalpha1,3Fuc-linkages, specific for L-fucose residues
-
-
-
additional information
?
-
-
fragment-based screening of the donor substrate specificity. Enzyme binds several UDP-activated sugars, including UDP-Glc, UDP-GlcNAc, and UDP-GalNAc. In all cases, UDP is the dominant binding epitope. The binding of donor substrate to GTB is essentially controlled by the base as a molecular anchor. Uracil represents the smallest fragment that is recognized. CDP, AMP, and GDP do not exhibit any significant binding affinity for the enzyme. The ribose and beta-phosphate moieties increase the affinity of the ligands. The pyranose sugar weakens the binding, although this part of the molecule controls the specificity of the enzyme. UDP represents the best binder. The binding affinities of UDP-Gal, UDP-Glc, and UMP are about the same, but lower than that of UDP. beta-D-Galactose and alpha-D-galactose bind weakly to GTB. Whereas beta-D-galactose binds to the acceptor and donor sites, it is suggested that alpha-D-galactose occupies a third hitherto unknown binding pocket
-
-
-
additional information
?
-
-
development and evaluation of a general screening assay method for glycosyltransferase activities, overview
-
-
-
additional information
?
-
-
histo-blood group B transferase transfers alpha-D-galatose to the antigen,H, while the B type enzyme transfers N-acetylgalactosamine, overview
-
-
-
additional information
?
-
-
the enzyme shows weakened activity with B antigen variants resulting from ABO polymophisms, phenotyping and genotyping of ABO antigens, overview
-
-
-
additional information
?
-
-
enzyme-substrate interaction analysis by electrospray ionization mass spectrometry, binding of substrate and product analogues, overview
-
-
-
additional information
?
-
-
galactose is used as an acceptor analogue and UDP as a donor analogue in all soaking trials
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-D-galactose + fucosylated Skp1 protein
UDP + alpha-D-galactosyl(1-3)-fucosyl-Skp1 protein
show the reaction diagram
-
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactose
show the reaction diagram
-
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactose
show the reaction diagram
-
i.e. H disaccharide
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-R
show the reaction diagram
-
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-R
show the reaction diagram
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactosyl-R
show the reaction diagram
-
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1-2)-D-galactosyl-O-R
UDP + alpha-D-galactosyl-(1-3)-[alpha-L-fucosyl-(1-2)]-D-galactosyl-O-R
show the reaction diagram
-
H-antigen disaccharide
-
-
-
UDP-galactose + blood group antigen
UDP + alpha-D-galactosyl-blood group antigen
show the reaction diagram
-
GTB catalyzes the transfer of galactose from UDP-Gal to the C3 position of the terminal galactose of H antigen acceptors
-
-
?
UDP-galactose + blood group antigen H
UDP + alpha-D-galactosyl-blood group antigen H
show the reaction diagram
-
-
-
-
?
UDP-galactose + blood group antigen H
UDP + alpha-D-galactosyl-blood group antigen H
show the reaction diagram
-
the alpha1,3-galactosyl epitope is a major xenotransplant antigen
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
-
acts on blood group substance
-
-
-
additional information
?
-
-
histo-blood group B transferase transfers alpha-D-galatose to the antigen,H, while the B type enzyme transfers N-acetylgalactosamine, overview
-
-
-
additional information
?
-
-
the enzyme shows weakened activity with B antigen variants resulting from ABO polymophisms, phenotyping and genotyping of ABO antigens, overview
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
0.1 mM, significant increase in activity, more significant acceleration at 10 mM
Co2+
-
slight activation
Hg
-
structures of the mercury derivative of GTB and GTB C209A, mercury does not affect the conformation of active-site residues, the structure of GTB C209A demonstrates that the mercury coordinated by Cys209 is partially responsible for the disorder of the 16-amino-acid internal loop observed in the heavy-atom structure of GTB
KCl
-
lower activity compared to NaCl, best at 50 mM
Mg2+
-
4fold lower activity compared to Mn2+
Mg2+
-
0.1 mM, significant increase in activity, more significant acceleration at 10 mM
Mg2+
-
activates, GTB requires divalent metal ions for full activity
Mg2+
-
activity depends on a bivalent cation
Mn2+
-
divalent cation required, Mn2+ most effective, optimum concentration 20 mM
Mn2+
-
required, maximal activity at 15-30 mM
Mn2+
-
divalent cation required, Mn2+ most effective, optimum concentration 20 mM
Mn2+
-
required, best at 2mM
Mn2+
-
0.1 mM, significant increase in activity
Mn2+
-
the enzyme has a characteristic 211DVD213 motif that coordinates to a Mn2+ ion shown to be critical in donor binding and catalysis
Mn2+
-
required, in the absence of divalent metal ion, GTB does not exhibit any appreciable affinity for its native donor UDP-Gal
Mn2+
-
activates 9fold at 24C, GTB requires divalent metal ions for full activity
Mn2+
-
cofactor
Mn2+
-
activity depends on a bivalent cation
NaCl
-
preferred salt, best at 50 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(1-benzothiophen-3-yl)methanamine
-
-
1-(2-chloro-6-fluorobenzyl)piperazine
-
-
1-(3-methoxyphenyl)piperazine
-
-
1-(3-phenyl-1,2,4-thiadiazol-5-yl)-1,4-diazepane
-
-
1-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine
-
-
1-methyl-1H-benzotriazole-5-carboxylic acid
-
-
2,3-dimethylquinoxaline-6-carboxylic acid
-
-
7-aminothieno[2,3-b]pyrazine-6-carboxylic acid
-
-
9-(D-1-deoxy-arabinit-1-yl)-1,3,7-trihydropurine-2,6,8-trione
-
-
-
9-D-ribityl-1,3,7-trihydropurine-2,6,8-trione
-
-
-
alpha-L-fucosyl-(1-2)-beta-D-(3-amino)-galactosyl-O-R
-
complex mode inhibitor, binding structure, Met226 is involved by interacting with the C3-position group
alpha-L-fucosyl-(1-2)-beta-D-(3-deoxy)-galactosyl-O-R
-
competitive inhibitor, binding structure, Met226 is involved by interacting with the C3-position group
EDTA
-
complete inhibition
N-methyl-1-[3-(pyridin-3-yl)phenyl]methanamine
-
-
N-methyl-1-[3-(pyridin-4-yl)phenyl]methanamine
-
-
octyl 3'-amino-3'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
octyl 3'-amino-3'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
93% inhibition at 0.025 mM
octyl 3'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
octyl alpha-L-fucopyranosyl-(1-2)-beta-D-gulopyranoside
-
-
octyl alpha-L-fucopyranosyl-(1-2)-beta-D-gulopyranoside
-
88% inhibition at 0.025 mM, competitive
UDP
-
competitive with respect to UDP-galactose
UDP-N-acetylgalactosamine
-
weak, competitive with respect to UDP-galactose
Fucalpha(1,2)Galbeta1-benzyl
-
competitive, 37% and 61% inhibition at 1 mM and 4 mM, respectively
additional information
-
not affected by Tween 20 at 0.1-1.0%
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-L-Fuc-(1,2)-beta-D-3-deoxy-Gal-O-octyl
-
i.e. 3DD, an acceptor substrate analogue, accelerates enzymatic hydrolysis of UDP-Gal
DTT
-
required, best at 2 mM
additional information
-
not affected by Tween 20 at 0.1-1.0%
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
2'-fucosyllactose
-
-
0.5
2'-fucosyllactose
-
-
1.6
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-DGlcNAcp-O(CH2)7CH3
-
37C, pH 7.0
0.184
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
-
37C, pH 7.0
0.022
alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
-
37C, pH 7.0
0.032
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
mutant C80S/C196S, pH 7.0, temperature not specified in the publication, donor UDP-alpha-D-galactose
0.055
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, donor UDP-alpha-D-galactose
0.2
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, donor UDP-GalNAc
0.3
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, donor UDP-GalNAc; mutant C80S/C196S, pH 7.0, temperature not specified in the publication, donor UDP-GalNAc
0.35
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, donor UDP-alpha-D-galactose
1.2
Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-(4-nitrophenol)
-
pH 7.4, 22C
2.2
Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-benzyl
-
pH 7.4, 22C
0.006
Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-Skp1 protein
-
pH 7.4, 22C
0.82
Fucalpha(1,2)Galbeta-1-(4-nitrophenol)
-
pH 7.4, 22C
0.84
Fucalpha(1,2)Galbeta1-benzyl
-
pH 7.4, 22C
3.7
Fucalpha-1-(4-nitrophenol)
-
pH 7.4, 22C
3.8
Fucalpha-1-benzyl
-
pH 7.4, 22C
1.5
L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3
-
with UDP-galactose as donor
3.22
L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3
-
with UDP-N-acetylgalactosamine as donor
0.022
L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
-
-
0.054
L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
-
with UDP-galactose as donor
0.061
L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
-
with UDP-galactose as donor
0.099
L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
-
-
0.25
L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
-
with UDP-N-acetylgalactosamine as donor
0.281
L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
-
with UDP-N-acetylgalactosamine as donor
0.027
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
P16442
-
0.106
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
P16442
P234S mutant
0.11
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
-
-
0.116
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
-
-
0.8
N-acetyllactosamine
-
-
2.2
O-alpha-L-fucosyl-1,2-galactose
-
-
0.2
octyl 3-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
4
octyl 4-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.565
octyl 6'-amino-6'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.538
octyl 6'-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.4
octyl alpha-L-xylo-hexopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.055
UDP-6-deoxygalactose
-
-
0.023
UDP-alpha-D-galactose
-
mutant C80S/C196S, pH 7.0, temperature not specified in the publication
0.045
UDP-alpha-D-galactose
-
deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication
0.78
UDP-alpha-D-galactose
-
mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication
0.0035
UDP-Gal
-
pH 7.4, 22C
0.01
UDP-galactose
-
-
0.027
UDP-galactose
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme
0.033
UDP-galactose
-
37C, pH 7.0, wild-type enzyme S185C
0.034
UDP-galactose
-
-
0.035
UDP-galactose
-
with L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3 as acceptor
0.036
UDP-galactose
-
in reaction with 2'-fucosyllactose
0.042
UDP-galactose
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
mutant D262N; mutant D262N; mutant D262N; mutant D262N; mutant D262N; mutant D262N
0.05
UDP-galactose
-
in reaction with N-acetyllactosamine
0.052
UDP-galactose
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
mutant F216I; mutant F216I; mutant F216I; mutant F216I; mutant F216I; mutant F216I
0.053
UDP-galactose
-
37C, pH 7.0, wild-type enzyme
0.06
UDP-galactose
-
with L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3 as acceptor
0.06
UDP-galactose
-
-
0.088
UDP-galactose
P16442
-
0.095
UDP-galactose
-
-
0.166
UDP-galactose
-
37C, pH 7.0, wild-type enzyme S185N
0.222
UDP-galactose
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
mutant A268T; mutant A268T; mutant A268T; mutant A268T; mutant A268T; mutant A268T
4.5
UDP-galactose
P16442
P234S mutant
0.023
UDP-GalNAc
-
mutant C80S/C196S, pH 7.0, temperature not specified in the publication
0.045
UDP-GalNAc
-
deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication
0.78
UDP-GalNAc
-
mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication
0.12
UDP-glucose
-
37C, pH 7.0, wild-type enzyme S185N
0.152
UDP-glucose
-
37C, pH 7.0, wild-type enzyme S185C
0.188
UDP-glucose
-
37C, pH 7.0, wild-type enzyme
0.238
UDP-glucose
-
-
0.285
UDP-N-acetylgalactosamine
-
-
0.3
UDP-N-acetylgalactosamine
-
with L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3 as acceptor
0.34
UDP-N-acetylgalactosamine
-
with L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3 as acceptor
2.5
lacto-N-fucopentaose I
-
-
additional information
additional information
-
kinetics, hyperbolic dependence on UDP-Gal concentration
-
additional information
additional information
-
kinetics
-
additional information
additional information
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
kinetics of wild-type and mutant enzymes; kinetics of wild-type and mutant enzymes; kinetics of wild-type and mutant enzymes; kinetics of wild-type and mutant enzymes; kinetics of wild-type and mutant enzymes; kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetic mechanism and thermodynamic analysis of GTB using electrospray ionization mass spectrometry, comparison to GTA, EC 2.4.1.40
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-D-GlcNAcp-O(CH2)7CH3
-
37C, pH 7.0
1.2
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O(CH2)8CO2CH3
-
37C, pH 7.0
3.5
alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
-
37C, pH 7.0
0.15
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc
0.41
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc
0.7
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
mutant C80S/C196S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc
5.6
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
mutant C80S/C196S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose
7.3
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose
0.000004
UDP-D-galactose
-
mutant R188S enzyme
0.15
UDP-D-galactose
-
mutant M186V enzyme
5.1
UDP-D-galactose
-
wild-type enzyme
0.37
UDP-Gal
-
pH 7.0, 37C, recombinant wild-type enzyme
0.7
UDP-Gal
-
pH 7.0, 37C, recombinant mutant M214S
0.74
UDP-Gal
-
pH 7.0, 37C, recombinant mutant M214G
0.004
UDP-galactose
P16442
P234S mutant
0.0042
UDP-galactose
-
mutant enzyme M214R
0.039
UDP-galactose
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
mutant A268T; mutant A268T; mutant A268T; mutant A268T; mutant A268T; mutant A268T
0.085
UDP-galactose
P16442
-
0.092
UDP-galactose
-
37C, pH 7.0, wild-type enzyme S185C
0.108
UDP-galactose
-
-
0.52
UDP-galactose
-
37C, pH 7.0, wild-type enzyme S185N
1.3
UDP-galactose
-
mutant ezyme M214V
2
UDP-galactose
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
mutant F216I; mutant F216I; mutant F216I; mutant F216I; mutant F216I; mutant F216I
2.5
UDP-galactose
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
mutant D262N; mutant D262N; mutant D262N; mutant D262N; mutant D262N; mutant D262N
5.1
UDP-galactose
-
wild-type enzyme
5.1
UDP-galactose
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme
5.2
UDP-galactose
-
37C, pH 7.0, wild-type enzyme
5.4
UDP-galactose
-
mutant enzyme M214T
4
UDP-GalNAc
-
pH 7.0, 37C, recombinant mutant M214G
5
UDP-GalNAc
-
pH 7.0, 37C, recombinant mutant M214S
5.1
UDP-GalNAc
-
pH 7.0, 37C, recombinant wild-type enzyme
0.0000167
UDP-glucose
-
-
0.00053
UDP-glucose
-
37C, pH 7.0, wild-type enzyme
0.0014
UDP-glucose
-
37C, pH 7.0, wild-type enzyme S185N
0.002
UDP-glucose
-
37C, pH 7.0, wild-type enzyme S185C
0.00016
UDP-N-acetylgalactosamine
-
mutant enzyme M214R
0.005
UDP-N-acetylgalactosamine
-
-
0.37
UDP-N-acetylgalactosamine
-
mutant enzyme M214V
0.42
UDP-N-acetylgalactosamine
-
wild-type enzyme
1.6
UDP-N-acetylgalactosamine
-
mutant enzyme M214T
8
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.571
9-(D-1-deoxy-arabinit-1-yl)-1,3,7-trihydropurine-2,6,8-trione
-
pH 7.0, 37C
-
0.361
9-D-ribityl-1,3,7-trihydropurine-2,6,8-trione
-
pH 7.0, 37C
-
0.005
octyl 3'-amino-3'deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.0078
octyl alpha-L-fucopyranosyl-(1-2)-beta-D-gulopyranoside
-
native enzyme
0.026
octyl alpha-L-fucopyranosyl-(1-2)-beta-D-gulopyranoside
-
recombinant enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.11
1-(1-benzothiophen-3-yl)methanamine
-
pH 6.7, 37C
2.72
1-(2-chloro-6-fluorobenzyl)piperazine
-
pH 6.7, 37C
1.28
1-(3-methoxyphenyl)piperazine
-
pH 6.7, 37C
1.04
1-(3-phenyl-1,2,4-thiadiazol-5-yl)-1,4-diazepane
-
pH 6.7, 37C
0.79
1-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine
-
pH 6.7, 37C
2.16
1-methyl-1H-benzotriazole-5-carboxylic acid
-
pH 6.7, 37C
1.56
2,3-dimethylquinoxaline-6-carboxylic acid
-
pH 6.7, 37C
0.97
7-aminothieno[2,3-b]pyrazine-6-carboxylic acid
-
pH 6.7, 37C
1.9
9-(D-1-deoxy-arabinit-1-yl)-1,3,7-trihydropurine-2,6,8-trione
-
pH 7.0, 37C
-
1.2
9-D-ribityl-1,3,7-trihydropurine-2,6,8-trione
-
pH 7.0, 37C
-
2.61
N-methyl-1-[3-(pyridin-3-yl)phenyl]methanamine
-
pH 6.7, 37C
1.61
N-methyl-1-[3-(pyridin-4-yl)phenyl]methanamine
-
pH 6.7, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.05
-
wild-type enzyme, with cosubstrate UDP-GalNAc
0.11
-
mutant M214G, with cosubstrate UDP-GalNAc
0.14
-
mutant M214S, with cosubstrate UDP-GalNAc
1.36
-
-
1.9
-
mutant M214S, with cosubstrate UDP-Gal
1.92
-
-
3.3
-
wild-type enzyme, with cosubstrate UDP-Gal
4.4
-
mutant M214G, with cosubstrate UDP-Gal
72
-
purified native enzyme
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3
-
blood group B
6.4 - 6.8
-
in reaction with N-acetyllactosamine
6.4 - 7.4
-
dependent on the buffer system
6.5
-
blood group B
6.7
-
assay at
6.8
-
in reaction with 2'-fucosyllactose
7 - 7.3
-
assay at
7 - 7.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24
-
assay at
37
P16442
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q8CFC4
B-type enzyme expression in the surface epithelium
Manually annotated by BRENDA team
Q8CFC4
B-type enzyme expression
Manually annotated by BRENDA team
Q8CFC4
B-type enzyme expression
Manually annotated by BRENDA team
Q8CFC4
B-type enzyme expression
Manually annotated by BRENDA team
Mus spicilegus ZBN
-
-
-
Manually annotated by BRENDA team
Q8CFC4
B-type enzyme expression in the surface epithelium
Manually annotated by BRENDA team
additional information
Q8CFC4
no B-type enzyme expression in small intestine, striated muscle, heart, liver, lung, skin, uterus, testis, lymph node, or brain
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme catalyzing the transfer of galactose to 2'-fucosyllactose is much more tightly attached to membrane than the transferase which utilizes N-acetyllactosamine
Manually annotated by BRENDA team
additional information
-
no activity in microsomes
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
-
gel filtration, 0.2 M NaCl added to the buffer
489129
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 34483, recombinant truncated enzyme mutant, mass spectrometry
dimer
-
2 * 40000, SDS-PAGE
additional information
-
high resolution structures for GTB and GTA/GTB chimeric enzyme mutants GTB/G176R and GTB/G176R/G235S bound to a panel of donor and acceptor analogue substrates, showing open, semi-closed, and closed conformations as the enzymes go from the unliganded to the liganded states, the active site in the unliganded or H antigen-bound enzymes is composed of two alpha-helices spanning Arg180-Met186 and Arg188-Asp194, respectively, loop ordering, overview
additional information
-
three-dimensional structure molecular modeling of wild-type and mutant enzymes
additional information
-
topology of ABO glycosyltransferase
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic domain with and without H-antigen and UDP, at 1.32 and 1.65 A resolution
-
crystals of purified native enzyme are soaked with various combinations of UDP-GalNAc, UDP-Gal, UDP, and acceptor analogues alpha-L-fucosyl-1,2-beta-D-(3-deoxy)-galactosyl-O-R or alpha-L-fucosyl-1,2-beta-D-(3-amino)-galactosyl-O-R, ligands are solved in 7.5% PEG 4000, 15% glycerol, 75 mM N-[2-acetamido]-2-iminodiacetic acid, pH 7.5, 10 mM MnCl2, and 10 mM inhibitor, 3-4 days, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
enzyme soaked with acceptor analogs: galactose, lactose, N-acetyllactosamine, beta-D-Galp-O(CH2)8CO2CH3, alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3, beta-D-Galp-(1,4)-beta-D-Glcp-OCH3, alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-D-GlcNAcp-O(CH2)7CH3, alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
-
mutant GTB C209A is crystallized in both the presence and the absence of mercury, 0.01 ml drops containing 6-8 mg/ml GTB, 70 mM N-(2-acetamido)-2-iminodiacetic acid, pH 7.5, 50 mM sodium acetate, pH 4.6, 40 mM NaCl, 5-8 mM MnCl2, 2.5% v/v 2-methyl-2,4-pentanediol, 5% v/v glycerol, 2% w/v PEG 4000 and 0.3-0.5 mM 3-chloromercuri-2-methoxypropylurea is suspended over 1 ml reservoir solution containing 50 mM N-(2-acetamido)-2-iminodiacetic acid, pH 7.5, 10 mM, MnCl2, 100 mM ammonium sulfate, 5% v/v MPD, 10% v/v glycerol and 8-10% w/v PEG 4000. Growing crystals of native GTB in the absence of mercury using protein concentrations of 6-8 mg /ml are unsuccessful, therefore crystals of the C209A mutant are grown from protein concentrations of over 30 mg/ml with the lowest observed concentration that yielded diffraction-quality crystals being 15 mg/ml 5-8 ml drops containing 1% PEG 4000, 4.5% MPD, 0.1 M ammonium sulfate, 0.07 M NaCl, 0.05 M N-(2-acetamido)-2-iminodiacetic acid, pH 7.5, and 5 mM CoCl2 are stored at 4-6C for 3-5 days over a reservoir of 2.7% PEG 4000, 7% MPD, 0.32 M ammonium sulfate, 0.25 M NaCl and 0.2 M N-(2-acetamido)-2-iminodiacetic acid. Both sets of crystals are washed with mother liquor containing 6-7% PEG 4000, 70 mM N-(2-acetamido)-2-iminodiacetic acid, pH 7.5, 30 mM sodium acetate, pH 4.6, 40 mM ammonium sulfate, 29-30% glycerol and 9-10 mM MnCl2 or 5 mM CoCl2 for the heavy-metal derivative or native protein, respectively. X-ray diffraction structure determination and analysis at 1.8-2.4 A resolution
-
P234S-mutant, 1.55 and 1.65 A resolution, with and without H-antigen
P16442
structures of GTA, GTB and several chimeras determined by single-crystal X-ray diffraction demonstrate a range of susceptibility to the choice of cryoprotectant, in which the mobile polypeptide loops can be induced by glycerol to form the ordered closed conformation associated with substrate recognition and by MPD (hexylene glycol, 2-methyl-2,4-pentanediol) to hinder binding of substrate in the active site owing to chelation of the Mn2+ cofactor and thereby adopt the disordered open state
-
wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling; wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling; wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling; wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling; wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling; wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
wild-type enzyme and GTA/GTB chimeric enzyme mutants GTB/G176R and GTB/G176R/G235S bound to a panel of donor and acceptor analogue substrates, hanging drop vapour diffusion method, method variantions, overview, X-ray diffraction structure determination and analysis at 1.43-1.75 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
5 min, 20% loss of activity, 20 min, 60% loss of activity
489130
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1 mM EDTA and 5% v/v glycerol stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, crude extract, 25% loss of activity after 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 2400fold by 2 steps ion exchange chromatography, HI chromatography, and gel filtration to homogeneity
-
one-step procedure involving absorption onto group 0 erythrocyte membranes followed by elution with the low molecular weight H-active trisaccharide 2'-fucosyllactose
-
purified by successive ion exchange chromatography with SP sepharose FF and affinity chromatography with UDP-hexanolamine sepharose
-
recombinant enzyme from Escherichia coli by cation exchange chromatograophy, UDP-hexanolamine affinity chromatography, and dialysis
-
recombinant wild-type and mutant enzymes from Escherichia coli
-
recombinant wild-type and mutant M186V enzymes from Escherichia coli by ion exchange and UDP-hexanolamine affinity chromatography
-
using Ni-NTA chromatography
-
via ELISA
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ABO glycosyltransferase polymorphisms, phenotyping and genotyping, overview
-
catalytic domain expressed in Escherichia coli
-
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strain BL21
-
expressed in Escherichia coli
-
expressed in Escherichia coli TG-1
-
expressed in Escherichia coli TG-1, the membrane-anchoring domain is replaced with an ompA bacterial secretory signal
-
expression of wild-type and chimeric mutant enzyme in HeLa cells
-
expression of wild-type and mutant enzymes in Escherichia coli
-
gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping; gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping; gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping; gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping; gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping; gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
overexpressed in Escherichia coli BL21 cells
-
overexpression in Escherichia coli strain BL21
-
overexpression of truncated GTB in Escherichia coli strain BL21
-
P234S-mutant expressed in Escherichia coli BL21
P16442
recombinantly expressed as a His-tagged fusion protein
-
transfected into HeLa cells derived from human adenocarcinoma of uterus
P38649
transfected into HeLa cells derived from human adenocarcinoma of uterus
-
monomorphic B-type gene Abo2, DNA and amino acid sequence determination and analysis, located on chromosome 3q11-q12, functional expression in CHO cells expressing the H precursor
Q8CFC4
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A268T
-
naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
A268T
-
naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
C209A
-
site-directed mutagenesis, mutant structure determination
C80S/C196S
-
both the double and triple mutants show differing levels of disorder depending on their liganded state, with the level of disorder increasing when substrates are bound.The double mutant shows disorder over residues 177-180 in the unliganded and H-antigen bound forms, with disorder increasing to residues 176-185 for the UDP-, UDP + H-, and UDP-alpha-D-galactose + 3-deoxy-Gal inactive acceptor analog-bound structures. The double mutant has a reduction in Km for both donor and acceptor substrates. Mutation shows little effect over kcat
C80S/C196S/C209S
-
both the double and triple mutants show differing levels of disorder depending on their liganded state, with the level of disorder increasing when substrates are bound.The unliganded triple mutant shows a nearly complete internal loop, with residues 176-181 disordered for the H-antigen-bound structure and 177-179 disordered for the UDP-bound structure. The UDP + H- and UDPGal + 3-deoxy-Gal inactive acceptor analog-bound structures of the triple mutant show an internal loop completely disordered over residues 176-184. The triple Cys-to-Ser mutant has an acceptor Km elevated approximately 5times over wild type, while the donor Km has doubled. Mutation shows little effect over kcat
D262N
-
naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
D262N
-
naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
DELTA68-354
-
construct in which the N-terminal transmembrane domain is deleted. Deletion results in a more crystallizable protein
F216I
-
naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
F216I
-
naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
I192T
-
naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
I192T
-
naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
M186V
-
site-directed mutagenesis, mutation is a naturally occuring polymorphism, amino-acid substitution in the disordered loop of the enzyme causes a weak B phenotype of erythrocytes, mutant enzyme shows reduced activity compared to the wild-type enzyme
M189V
-
naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
M189V
-
naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
M214G
-
saturation mutagenesis of GTB enzyme at M214 leads to a two-fold higher kcat for UDP-GalNAc and specific activity of the mutant compared to the wild-type GTB
M214R
-
mutation is adjacent to the 211DVD213 motif. 1200fold decrease in kcat compared with wild type enzyme. The crystal structure of M214R shows that DVD motif coordination to Mn2+ is disrupted by Arg214 causing displacement of the metal by a water molecule. Individuals with the M214R mutation show the Bel variant expressing very low levels of B antigens
M214S
-
saturation mutagenesis of GTB enzyme at M214 leads to a two-fold higher kcat for UDP-GalNAc and specific activity of the mutant compared to the wild-type GTB
M214T
-
mutation is adjacent to the 211DVD213 motif. The crystal structure of the M214T mutant shows no change in DVD motif coordination to Mn2+. Instead a critical residue, Met266, which is responsible for determining donor specificity, has adopted alternate conformations. The conformation with the highest occupancy opens up the active site to accommodate the larger A-specific donor, UDP-GalNAc, accounting for the dual specificity. Individuals with M214T mutation give rise to AweakB phenotype
P234S
P16442
dramatic and complete reversal of donor specificity, it preferentially utilizes UDP-GalNac for transfer
R188H
-
site-directed mutagenesis, the mutant shows affected substrate binding
R188K
-
site-directed mutagenesis, the mutant shows affected substrate binding
R188S
-
site-directed mutagenesis, nearly inactive mutant
R188S
-
site-directed mutagenesis, the mutant shows affected substrate binding
S185C
-
mutant enzyme exhibits 4.8fold elevations in kcat/Km for UDP-glucose relative to that of wild-type enzyme
S185D
-
activity with UDP-galactose is 0.09% of wild-type activity
S185E
-
activity with UDP-galactose is 0.04% of wild-type activity
S185N
-
mutant enzyme exhibits 4.3fold elevations in kcat/Km for UDP-glucose relative to that of wild-type enzyme
M214V
-
mutation is adjacent to the 211DVD213 motif. Individuals with M214T mutation give rise to AweakB phenotype
additional information
-
construction of GTA/GTB chimeric enzyme mutants GTB/G176R and GTB/G176R/G235S, structures of the mutants bound to a panel of donor and acceptor analogue substrates, showing open, semi-closed, and closed conformations as the enzymes go from the unliganded to the liganded states, overview
additional information
-
identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview
additional information
-
identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview
additional information
-
screening of a saturation mutagenesis library for mutant determination with altered cosubstrate specificity
additional information
-
ABO glycosyltransferase polymorphisms leading to reduced activity and substrate recognition, phenotyping and genotyping, overview
additional information
-
construction of truncated GTB monomers composed of the full C-terminal and catalytic domain as well as a truncated N-terminal domain
additional information
-
generation of a structural chemira of histo-blood group B transferase, a B type transferase, by replacing the N-acetyl-D-galactosamine recognition domain of human type A transferase with the galactose-recognition domain of evolutionarily related murine alpha1,3-galactosyltransferase, leading to functional conversion from human A to B transferase activity, overview. When the glycine 268 of the A transferase is substituted by the alanine of the B transferase, the construct expresses an enzyme with weak B transferase activity, but when the alanine 268 of B transferase is substituted by the glycine of A transferase, the construct expresses an enzyme with strong A and B transferase activity
additional information
-
chimeric GTA and GTB enzymes are generated (AABB, ABBA and ABBB)