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beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + UDP-GalNAc
?
-
-
-
-
?
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
-
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
-
tetramethylrhodamine labelled disaccharide
-
-
?
UDP-alpha-D-galactose + 8-methoxycarbonyloctyl beta-D-Galp-(1->4)-beta-D-Glcp
?
-
-
-
-
?
UDP-alpha-D-galactose + alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
UDP + alpha-D-Gal-(1->3)-[alpha-Fuc-(1->2)]-beta-D-Gal-(CH2)7CH3
UDP-alpha-D-galactose + alpha-L-Fuc-(1-2)-beta-D-Gal-octyl
?
-
-
-
-
?
UDP-alpha-D-galactose + alpha-L-Fuc-(1->2)-beta-D-Gal-octyl
?
-
-
-
-
?
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
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
UDP-D-galactose + 2'-fucosyllactose
UDP + D-galactosyl-(1-3)-2'-fucosyllactose
-
-
-
?
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
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
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
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)
-
-
-
-
?
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
-
-
-
-
?
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
-
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)
-
-
-
-
?
UDP-D-galactose + Fucalpha(1,2)Galbeta-1-benzyl
UDP + alpha-D-Gal(1,3)Fucalpha(1,2)Galbeta-1-benzyl
-
-
-
-
?
UDP-D-galactose + Fucalpha-1-(4-nitrophenol)
UDP + alpha-D-Gal(1,3)Fucalpha-1-(4-nitrophenol)
-
-
-
-
?
UDP-D-galactose + Fucalpha-1-benzyl
UDP + alpha-D-Gal(1,3)Fucalpha-1-benzyl
-
-
-
-
?
UDP-D-galactose + fucosylated Skp1 protein
UDP + alpha-D-galactosyl(1-3)-fucosyl-Skp1 protein
-
-
-
-
?
UDP-D-galactose + H type 3-Sp-biotin
UDP + ?
preferred substrates
-
-
?
UDP-D-galactose + H-disaccharide
UDP + alpha-D-galactosyl-1,3-H disaccharide
-
synthetic substrate
-
-
?
UDP-galactose + 2'-fucosyllactose
UDP + alpha-D-galactosyl-1,3-[2'-fucosyllactose]
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
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
-
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
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactosyl-R
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-R
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
UDP-galactose + blood group antigen
UDP + alpha-D-galactosyl-blood group antigen
-
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
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
UDP-galactose + H-active glycoprotein
UDP + B-active substance
-
-
-
?
UDP-galactose + L-2'-L-fucosyllactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactosyl-D-glucose
-
-
-
-
?
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
-
-
-
-
?
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
UDP-galactose + lacto-N-fucopentaose I
UDP + alpha-D-galactosyl-1,3-[lacto-N-fucopentaose I]
-
-
-
-
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-[N-acetyl-lactosamine]
-
-
-
-
?
UDP-galactose + O-alpha-L-fucosyl-1,2-galactose
UDP + alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactopyranoside
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
UDP-glucose + Fucalpha1-2Galbeta-O(CH2)7CH3
?
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
UDP-N-acetyl-D-galactosamine + 2'-fucosyllactose
UDP + N-acetyl-alpha-D-galactosaminyl-(1->3)-[alpha-L-fucosyl-(1->2)]-beta-D-galactosyl-(1->4)-beta-D-glucose
low A-type activity
-
-
?
UDP-N-acetyl-D-galactosamine + H type 3-Sp-biotin
UDP + ?
low A-type activity
-
-
?
UDP-N-acetylgalactosamine + 2'-fucosyllactose
UDP + N-acetyl-alpha-D-galactosyl-1,3-[2'-fucosyllactose]
-
-
-
-
?
UDP-N-acetylgalactosamine + L-2'-fucosyllactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-D-glucose
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
additional information
?
-
UDP-alpha-D-galactose + alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
UDP + alpha-D-Gal-(1->3)-[alpha-Fuc-(1->2)]-beta-D-Gal-(CH2)7CH3
-
-
-
?
UDP-alpha-D-galactose + alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
UDP + alpha-D-Gal-(1->3)-[alpha-Fuc-(1->2)]-beta-D-Gal-(CH2)7CH3
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
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 + 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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
UDP-galactose + 2'-fucosyllactose
UDP + alpha-D-galactosyl-1,3-[2'-fucosyllactose]
-
-
-
-
?
UDP-galactose + 2'-fucosyllactose
UDP + alpha-D-galactosyl-1,3-[2'-fucosyllactose]
-
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactose
-
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactose
-
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
-
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
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactosyl-R
substrate binding structure and residues involved, overview
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-R
-
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-R
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-R
-
importance of residue M214 for donor enzyme specificity
-
-
?
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
H-antigen disaccharide
-
-
?
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
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 H
UDP + alpha-D-galactosyl-blood group antigen H
-
-
-
-
?
UDP-galactose + blood group antigen H
UDP + alpha-D-galactosyl-blood group antigen H
-
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
-
the alpha1,3-galactosyl epitope is a major xenotransplant antigen
-
-
?
UDP-galactose + blood group antigen H
UDP + alpha-D-galactosyl-blood group antigen H
-
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
-
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
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
-
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
-
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
-
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
-
-
-
?
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
-
acts on blood group substance
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
tetramethylrhodamine labelled disaccharide
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
?
additional information
?
-
mouse ABO gene-encoded cis-AB transferase contains the GlyGlyAla tripeptide sequence, which is also found in the majority of GBGT1 genes encoding Forssman glycolipid synthase, EC 2.4.1.88. Mouse cis-AB transferase with the GlyGlyAla tripeptide sequence, but not the human cis-AB transferase with the LeuGlyAla, exhibits Forssman glycolipid synthase activity equivalent of mouse GBGT1 gene-encoded Forssman glycolipid synthase
-
-
-
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
-
-
?
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0.08 - 0.5
2'-fucosyllactose
0.088 - 2.64
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
1.6
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-DGlcNAcp-O(CH2)7CH3
37°C, pH 7.0
0.184
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
37°C, pH 7.0
0.022
alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
37°C, pH 7.0
0.032 - 0.35
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
1.2
Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-(4-nitrophenol)
-
pH 7.4, 22°C
2.2
Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-benzyl
-
pH 7.4, 22°C
0.006
Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-Skp1 protein
-
pH 7.4, 22°C
0.82
Fucalpha(1,2)Galbeta-1-(4-nitrophenol)
-
pH 7.4, 22°C
0.84
Fucalpha(1,2)Galbeta1-benzyl
-
pH 7.4, 22°C
3.7
Fucalpha-1-(4-nitrophenol)
-
pH 7.4, 22°C
3.8
Fucalpha-1-benzyl
-
pH 7.4, 22°C
1.5 - 3.22
L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3
0.022 - 0.281
L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
0.027 - 0.116
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
2.5
lacto-N-fucopentaose I
-
-
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 - 0.78
UDP-alpha-D-galactose
0.0035
UDP-Gal
-
pH 7.4, 22°C
0.285 - 0.34
UDP-N-acetylgalactosamine
additional information
additional information
-
0.08
2'-fucosyllactose
-
-
0.5
2'-fucosyllactose
-
-
0.088
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
wild-type, pH 7.0, 37°C
0.1
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant D302E/D316E, pH 7.0, 37°C
0.101
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant R188K, pH 7.0, 37°C
0.117
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant D302A/D316A, pH 7.0, 37°C
0.19
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant E303C, pH 7.0, 37°C
0.332
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant D302C, pH 7.0, 37°C
0.98
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant E303A, pH 7.0, 37°C
2.64
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant E303D, pH 7.0, 37°C
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
0.3
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-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
1.5
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
-
0.106
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
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
-
-
0.023
UDP-alpha-D-galactose
-
mutant C80S/C196S, pH 7.0, temperature not specified in the publication
0.027
UDP-alpha-D-galactose
wild-type, pH 7.0, 37°C
0.036
UDP-alpha-D-galactose
mutant E303C, pH 7.0, 37°C
0.045
UDP-alpha-D-galactose
-
deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication
0.053
UDP-alpha-D-galactose
mutant D302C, pH 7.0, 37°C
0.074
UDP-alpha-D-galactose
mutant E303A, pH 7.0, 37°C
0.101
UDP-alpha-D-galactose
mutant R188K, pH 7.0, 37°C
0.112
UDP-alpha-D-galactose
mutant D302E/D316E, pH 7.0, 37°C
0.17
UDP-alpha-D-galactose
mutant D302A/D316A, pH 7.0, 37°C
0.211
UDP-alpha-D-galactose
mutant E303D, pH 7.0, 37°C
0.78
UDP-alpha-D-galactose
-
mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication
0.01
UDP-galactose
-
-
0.027
UDP-galactose
wild-type enzyme
0.033
UDP-galactose
37°C, pH 7.0, wild-type enzyme S185C
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
mutant D262N
0.05
UDP-galactose
-
in reaction with N-acetyllactosamine
0.052
UDP-galactose
mutant F216I
0.053
UDP-galactose
37°C, pH 7.0, wild-type enzyme
0.06
UDP-galactose
-
with L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3 as acceptor
0.166
UDP-galactose
37°C, pH 7.0, wild-type enzyme S185N
0.222
UDP-galactose
mutant A268T
4.5
UDP-galactose
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
37°C, pH 7.0, wild-type enzyme S185N
0.152
UDP-glucose
37°C, pH 7.0, wild-type enzyme S185C
0.188
UDP-glucose
37°C, pH 7.0, wild-type enzyme
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
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics, hyperbolic dependence on UDP-Gal concentration
-
additional information
additional information
-
kinetic mechanism and thermodynamic analysis of GTB using electrospray ionization mass spectrometry, comparison to GTA, EC 2.4.1.40
-
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AGTA_DICDI
648
0
75244
Swiss-Prot
other Location (Reliability: 1)
BGAT1_RAT
348
1
40375
Swiss-Prot
Secretory Pathway (Reliability: 1)
BGAT2_RAT
334
1
39079
Swiss-Prot
Secretory Pathway (Reliability: 1)
BGAT_HUMAN
354
1
40934
Swiss-Prot
Secretory Pathway (Reliability: 2)
BGAT_MOUSE
332
1
38777
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A061HUI4_CRIGR
330
0
38580
TrEMBL
other Location (Reliability: 1)
A0A2G8YCE7_TOXGO
576
0
62544
TrEMBL
other Location (Reliability: 1)
A0A2T6ITR4_TOXGO
577
0
62615
TrEMBL
other Location (Reliability: 1)
A0A086JG49_TOXGO
552
0
59768
TrEMBL
other Location (Reliability: 3)
A0A1J0M5B7_HUMAN
274
0
31871
TrEMBL
Secretory Pathway (Reliability: 3)
A0A139Y9K7_TOXGO
576
0
62558
TrEMBL
other Location (Reliability: 1)
G0QTB3_ICHMG
Ichthyophthirius multifiliis (strain G5)
313
0
37061
TrEMBL
other Location (Reliability: 1)
G0QNL9_ICHMG
Ichthyophthirius multifiliis (strain G5)
290
0
32640
TrEMBL
other Location (Reliability: 1)
Q8WXZ0_HUMAN
229
0
26724
TrEMBL
other Location (Reliability: 4)
Q8WXY8_HUMAN
229
0
26768
TrEMBL
other Location (Reliability: 4)
A0A139XK15_TOXGO
31
0
3490
TrEMBL
other Location (Reliability: 1)
G0QK94_ICHMG
Ichthyophthirius multifiliis (strain G5)
1268
0
150971
TrEMBL
other Location (Reliability: 1)
G0R157_ICHMG
Ichthyophthirius multifiliis (strain G5)
368
0
42644
TrEMBL
other Location (Reliability: 1)
O15512_HUMAN
274
0
31959
TrEMBL
Secretory Pathway (Reliability: 4)
A0A086M7D5_TOXGO
577
0
62615
TrEMBL
other Location (Reliability: 1)
S8G8T4_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
576
0
62558
TrEMBL
other Location (Reliability: 1)
Q8WXZ1_HUMAN
229
0
26773
TrEMBL
other Location (Reliability: 4)
A0A139XJZ9_TOXGO
64
0
7009
TrEMBL
other Location (Reliability: 4)
G0QUW6_ICHMG
Ichthyophthirius multifiliis (strain G5)
634
0
71166
TrEMBL
other Location (Reliability: 2)
A0A086KSU0_TOXGO
577
0
62615
TrEMBL
other Location (Reliability: 1)
G0QZ79_ICHMG
Ichthyophthirius multifiliis (strain G5)
482
0
55785
TrEMBL
other Location (Reliability: 1)
A0A086QFR3_TOXGO
532
0
58039
TrEMBL
other Location (Reliability: 3)
Q4LAQ2_HUMAN
229
0
26711
TrEMBL
other Location (Reliability: 4)
A0A086KHD7_TOXGO
532
0
58029
TrEMBL
other Location (Reliability: 3)
A0A2G9HIN2_9LAMI
316
0
36040
TrEMBL
other Location (Reliability: 3)
G8IIL0_HUMAN
354
1
40926
TrEMBL
Secretory Pathway (Reliability: 2)
Q8WXY5_HUMAN
229
0
26715
TrEMBL
other Location (Reliability: 4)
G0QL52_ICHMG
Ichthyophthirius multifiliis (strain G5)
643
0
74711
TrEMBL
other Location (Reliability: 1)
G0R5P1_ICHMG
Ichthyophthirius multifiliis (strain G5)
332
0
37866
TrEMBL
other Location (Reliability: 1)
G0QNN4_ICHMG
Ichthyophthirius multifiliis (strain G5)
740
8
85405
TrEMBL
Secretory Pathway (Reliability: 4)
A0A086PUG8_TOXGO
460
0
49692
TrEMBL
other Location (Reliability: 3)
A0A2G8XR10_TOXGO
31
0
3490
TrEMBL
other Location (Reliability: 1)
A0A425HZL8_TOXGO
577
0
62615
TrEMBL
other Location (Reliability: 1)
G0R5J5_ICHMG
Ichthyophthirius multifiliis (strain G5)
314
0
35779
TrEMBL
other Location (Reliability: 3)
G0QVE1_ICHMG
Ichthyophthirius multifiliis (strain G5)
477
0
55609
TrEMBL
other Location (Reliability: 1)
A0A086L281_TOXGO
577
0
62615
TrEMBL
other Location (Reliability: 1)
A0A125YRU9_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
690
0
75759
TrEMBL
Mitochondrion (Reliability: 2)
Q8WXY9_HUMAN
229
0
26685
TrEMBL
other Location (Reliability: 5)
A0A0K2FRI0_HUMAN
229
0
26643
TrEMBL
other Location (Reliability: 4)
G0QPS8_ICHMG
Ichthyophthirius multifiliis (strain G5)
359
0
41077
TrEMBL
other Location (Reliability: 2)
G0R198_ICHMG
Ichthyophthirius multifiliis (strain G5)
630
0
73099
TrEMBL
other Location (Reliability: 3)
Q8WXY7_HUMAN
229
0
26757
TrEMBL
other Location (Reliability: 4)
G0QY00_ICHMG
Ichthyophthirius multifiliis (strain G5)
156
0
17286
TrEMBL
other Location (Reliability: 1)
A0A061HXH8_CRIGR
285
0
33071
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2G8XR13_TOXGO
594
0
65209
TrEMBL
Mitochondrion (Reliability: 2)
A0A086KGZ2_TOXGO
552
0
59768
TrEMBL
other Location (Reliability: 3)
G0QTH9_ICHMG
Ichthyophthirius multifiliis (strain G5)
330
0
37120
TrEMBL
other Location (Reliability: 2)
F8KUR1_PARAV
Parachlamydia acanthamoebae (strain UV7)
249
1
28348
TrEMBL
-
A0A2P6R146_ROSCH
869
1
97803
TrEMBL
Mitochondrion (Reliability: 4)
A0A7S9GFL1_HUMAN
274
0
31864
TrEMBL
Secretory Pathway (Reliability: 3)
G3IBD3_CRIGR
354
1
41396
TrEMBL
Secretory Pathway (Reliability: 2)
S7UK59_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
690
0
75759
TrEMBL
Mitochondrion (Reliability: 2)
A0A125YVG4_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
577
0
62615
TrEMBL
other Location (Reliability: 1)
A0A425HNT3_TOXGO
450
0
48665
TrEMBL
Mitochondrion (Reliability: 2)
A0A3R8BP50_TOXGO
128
0
14481
TrEMBL
other Location (Reliability: 3)
A0A0C1BYL5_9BACT
256
1
29143
TrEMBL
-
G0QXV3_ICHMG
Ichthyophthirius multifiliis (strain G5)
1513
0
177347
TrEMBL
other Location (Reliability: 1)
G0QXW3_ICHMG
Ichthyophthirius multifiliis (strain G5)
1348
0
157736
TrEMBL
other Location (Reliability: 3)
S7WHI6_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
577
0
62615
TrEMBL
other Location (Reliability: 1)
Q8WXY6_HUMAN
229
0
26744
TrEMBL
other Location (Reliability: 4)
A0A139XJZ6_TOXGO
594
0
65239
TrEMBL
Mitochondrion (Reliability: 2)
G0QY61_ICHMG
Ichthyophthirius multifiliis (strain G5)
1108
0
128714
TrEMBL
other Location (Reliability: 2)
A0A086PXX0_TOXGO
576
0
62538
TrEMBL
other Location (Reliability: 1)
A0A2T6IT03_TOXGO
460
0
49692
TrEMBL
other Location (Reliability: 3)
A0A086K0P7_TOXGO
577
0
62615
TrEMBL
other Location (Reliability: 1)
G0QJ01_ICHMG
Ichthyophthirius multifiliis (strain G5)
1246
0
146603
TrEMBL
other Location (Reliability: 3)
G0R0G7_ICHMG
Ichthyophthirius multifiliis (strain G5)
249
0
28492
TrEMBL
other Location (Reliability: 2)
V4Z2X0_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
552
0
59768
TrEMBL
other Location (Reliability: 3)
G0QPJ8_ICHMG
Ichthyophthirius multifiliis (strain G5)
385
0
43045
TrEMBL
other Location (Reliability: 2)
A0A2G8XR08_TOXGO
64
0
7009
TrEMBL
other Location (Reliability: 4)
A0A396GS67_MEDTR
657
1
75175
TrEMBL
Secretory Pathway (Reliability: 1)
A0A086LPX1_TOXGO
460
0
49692
TrEMBL
other Location (Reliability: 3)
G0QK35_ICHMG
Ichthyophthirius multifiliis (strain G5)
1211
0
141766
TrEMBL
other Location (Reliability: 1)
G0QW46_ICHMG
Ichthyophthirius multifiliis (strain G5)
494
0
56746
TrEMBL
other Location (Reliability: 1)
A0A086QT94_TOXGO
576
0
62542
TrEMBL
other Location (Reliability: 1)
A5X6H3_HUMAN
229
0
26775
TrEMBL
-
A5X6H4_HUMAN
229
0
26711
TrEMBL
-
A5X6H5_HUMAN
229
0
26731
TrEMBL
-
A5X6H7_HUMAN
229
0
26742
TrEMBL
-
A5X6H8_HUMAN
229
0
26773
TrEMBL
-
EPCAM_HUMAN
314
0
34932
Swiss-Prot
-
Q6L638_HUMAN
229
0
26727
TrEMBL
-
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assignment of all methyl resonance signals in Ala, Ile, Leu, Met and Val labeled samples of GTA and GTB by lanthanide-induced pseudocontact shifts and methyl-methyl NOESY. The fully closed state is not adopted in the presence of lanthanide ions
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 adopts an open conformation in the absence of substrates. Binding of the donor substrate UDP-Gal or of UDP induces a semiclosed conformation. In the presence of both donor and acceptor substrates, the enzymes shift towards a closed conformation with ordering of an internal loop and the C-terminal residues, which then completely cover the donor-binding pocket. The enzyme shows substantial plasticity and conformational flexibility. Residues Ile123 at the bottom of the UDP binding pocket, and Ile192 as part of the internal loop are significantly disturbed upon stepwise addition of UDP and H-disaccharide-O-CH3
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
in complex with UDP and galactose, using 1% (w/v) PEG 4000, 4.5-5% (w/v) 2-methyl-2,4-pentanediol, 100 mM ammonium sulfate, 70 mM sodium chloride, 50 mM N-[2-acetamido]-2-iminodiacetic acid buffer pH 7.5, 30 mM sodium acetate buffer pH 4.6 and 5 mM MnCl2
Methyl-TROSY-based titration experiments in combination with zz-exchange experiments show dramatic changes of binding kinetics associated with allosteric interactions between donor-type and acceptor-type ligands. Binding of the acceptor substrates H-disaccharide, H-type II trisaccharide, and H-type VI trisaccharide affects the chemical shifts of the 13C-methyl groups of Met 266, Val 299, Leu 324, and Leu 329, which belong to the acceptor substrate binding pocket
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 4-6°C 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
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
-
structures of isoforms GTA and GTB in complex with their respective trisaccharide products. A conflict exists between the transferred sugar monosaccharide and the beta-phosphate of the UDP donor. The mechanism of product release shows monosaccharide transfer to the H-antigen acceptor induces active site disorder and ejection of the UDP leaving group prior to trisaccharide egress
structures of wild-type and mutants D302A, D302C, D302L, R188K. Conserved active site residues Arg188 and Asp302 are critical for catalysis, and disruption of their hydrogen bond network through mutation can dramatically decrease enzymatic activity
study of substrate-induced conformational transitions of GTB. Acceptor binding is fast on the chemical-shift timescale with rather small chemical-shift perturbations in the range of less than approximately 20 Hz. Donor or acceptor binding to GTB saturated with acceptor or donor substrate, respectively, is slow (below 10 Hz). Substrate binding drives the enzyme into the closed state required for catalysis
using 1% (w/v) polyethylene glycol 4000, 4.5-5% (w/v) 2-methyl-2,4-pentanediol, 100 mM ammonium sulfate, 70 mM sodium chloride, 50 mM N-[2-acetamido]-2-iminodiacetic acid buffer, pH 7.5, 30 mM sodium acetate buffer, pH 4.6, and 5 mM MnCl2
wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling
wild-type and mutants E303A, E303C, E303D, E303Q
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
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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
D302A
almost complete loss of activity
D302A/D316A
strong decrease in kcat value
D302C
kcat value is 9% that of wild-type GTB
D302E
kcat value is 47% that of wild-type GTB
D302E/D316E
50% decrease in kcat value
D302L
almost complete loss of activity
DELTA68-354
-
construct in which the N-terminal transmembrane domain is deleted. Deletion results in a more crystallizable protein
E303A
residue E303 plays a critical role in maintaining the stability of a strained double-turn in the active site through several hydrogen bonds
E303C
residue E303 plays a critical role in maintaining the stability of a strained double-turn in the active site through several hydrogen bonds. Mutant retains significant activity despite disrupted active site architecture
E303D
residue E303 plays a critical role in maintaining the stability of a strained double-turn in the active site through several hydrogen bonds. Mutant retains significant activity despite disrupted active site architecture
E303Q
residue E303 plays a critical role in maintaining the stability of a strained double-turn in the active site through several hydrogen bonds. Mutant maintains active site architecture but exhibits zero activity
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
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
M214V
mutation is adjacent to the 211DVD213 motif. Individuals with M214T mutation give rise to AweakB phenotype
P234S
dramatic and complete reversal of donor specificity, it preferentially utilizes UDP-GalNac for transfer
R188H
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
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
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
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
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
R188K
almost complete loss of activity
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
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 occruing polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occruing polymorphisms in the ABO gene, phenotypes, 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
identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occurring 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)
additional information
amino acids at codons 266 and 268 of human isoforms GTA, EC 2.4.1.40, and GTB, EC 2.4.1.37, are crucial to their distinct sugar specificities. In vitro mutagenized GTAs/GTBs having any of 20 possible amino acids at those codons show that those codons determine the transferase activity and sugar specificity
additional information
the enzymes GTA, EC 2.4.1.40, and GTB have nearly identical sequences, while the corresponding mutants of GTA/GTB have up to a 13fold difference in their residual activities relative to wild type.The mutated Cys, Asp and Gln functional groups are no more than 0.8 A further from the anomeric carbon of donor substrate compared to wild type
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Marcus, S.L.; Polakowski, R.; Seto, N.O.L.; Leinala, E.; Borisova, S.; Blancher, A.; Roubinet, F.; Evans, S.V.; Palcic, M.M.
A single point mutation reverses the donor specificity of human blood group B-synthesizing galactosyltransferase
J. Biol. Chem.
278
12403-12405
2003
Homo sapiens (P16442)
brenda
Patenaude, S.I.; Seto, N.O.L.; Borisova, S.N.; Szpacenko, A.; Marcus, S.L.; Palcic, M.M.; Evans, S.V.
The structural basis for specificity in human ABO(H) blood group biosynthesis
Nat. Struct. Biol.
9
685-690
2002
Homo sapiens (P16442)
brenda
Yamamoto, M.; Lin, X.H.; Kominato, Y.; Hata, Y.; Noda, R.; Saitou, N.; Yamamoto, F.
Murine equivalent of the human histo-blood group ABO gene is a cis-AB gene and encodes a glycosyltransferase with both A and B transferase activity
J. Biol. Chem.
276
13701-13708
2001
Mus spicilegus, Mus musculus brevirostris (P38649), Mus musculus castaneus (P38649), Mus musculus domesticus (P38649), Mus musculus brevirostris BFM/2Msf (P38649), Mus spicilegus ZBN, Mus musculus domesticus BALB/c (P38649), Mus musculus castaneus CAST/Ei (P38649)
brenda
Sujino, K.; Uchiyama, T.; Hindsgaul, O.; Seto, N.O.L.; Wakarchuk, W.W.; Palcic, M.M.
Enzymatic synthesis of oligosaccharide analogues: evaluation of UDP-Gal analogues as donors for three retaining alpha-galactosyltransferases
J. Am. Chem. Soc.
122
1261-1269
2000
Homo sapiens
-
brenda
Seto, N.O.L.; Compston, C.A.; Szpacenko, A.; Palcic, M.M.
Enzymatic synthesis of blood group A and B trisaccharide analogues
Carbohydr. Res.
324
161-169
2000
Homo sapiens
brenda
Mukherjee, A.; Palcic, M.M.; Hindsgaul, O.
Synthesis and enzymatic evaluation of modified acceptors of recombinant blood group A and B glycosyltransferases
Carbohydr. Res.
326
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2000
Homo sapiens
brenda
Kamath, V.P.; Seto, N.O.L.; Compston, C.A.; Hindsgaul, O.; Palcic, M.M.
Synthesis of the acceptor analog alpha-Fuc(1-2)-alpha-Gal-O(CH2)7CH3: a probe for the kinetic mechanism of recombinant human blood group B glycosyltransferase
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16
599-606
2000
Homo sapiens
brenda
Seto, N.O.; Compston, C.A.; Evans, S.V.; Bundle, D.R.; Narang, S.A.; Palcic, M.M.
Donor substrate specificity of recombinant human blood group A, B and hybrid A/B glycosyltransferases expressed in Escherichia coli
Eur. J. Biochem.
259
770-775
1999
Homo sapiens
brenda
Yu, L.C.; Lee, H.L.; Chan, Y.S.; Lin, M.
The molecular basis for the B(A) allele: an amino acid alteration in the human histoblood group B alpha-(1,3)-galactosyltransferase increases its intrinsic alpha-(1,3)-N-acetylgalactosaminyltransferase activity
Biochem. Biophys. Res. Commun.
262
487-493
1999
Homo sapiens
brenda
Seto, N.O.L.; Palcic, M.M.; Compston, C.A.; Li, H.; Bundle, D.R.; Narang, S.A.
Sequential interchange of four amino acids from blood group B to blood group A glycosyltransferase boosts catalytic activity and progressively modifies substrate recognition in human recombinant enzymes
J. Biol. Chem.
272
14133-14138
1997
Homo sapiens
brenda
Seto, N.O.L.; Palcic, M.M.; Hindsgaul, O.; Bundle, D.R.; Narang, S.A.
Expression of a recombinant human glycosyltransferase from a synthetic gene and its utilization for synthesis of the human blood group B trisaccharide
Eur. J. Biochem.
234
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1995
Homo sapiens
brenda
Lowary, T.L.; Hindsgaul, O.
Recognition of synthetic O-methyl, epimeric, and amino analogues of the acceptor alpha-L-Fuc p-(1-2)-beta-D-Gal p-OR by the blood-group A and B gene-specified glycosyltransferases
Carbohydr. Res.
251
33-67
1994
Homo sapiens
brenda
Nakajima, T.; Furukawa, K.; Takenaka, O.
Blood group A and B glycosyltransferase in nonhuman primate plasma
Exp. Clin. Immunogenet.
10
21-30
1993
Homo sapiens, Hylobates lar entelloides, Macaca fuscata
brenda
Yazawa, S.; Nakajima, T.; Kameyama, N.; Saga, K.I.; Tachikawa, T.
An enzyme-linked immunosorbent assay for blood-group A and B enzymes
Carbohydr. Res.
239
329-335
1993
Homo sapiens
brenda
Betteridge, A.; Watkins, W.M.
Two alpha-3-D-galactosyltransferases in rabbit stomach mucosa with different acceptor substrate specificities
Eur. J. Biochem.
132
29-35
1983
Oryctolagus cuniculus
brenda
Nagai, M.; Dave, V.; Muensch, H.; Yoshida, A.
Human blood group glycosyltransferase. II. Purification of galactosyltransferase
J. Biol. Chem.
253
380-381
1978
Homo sapiens
brenda
Carne, L.R.; Watkins, W.M.
Human blood group B gene-specified alpha-3-galactosyltransferase: purification of the enzyme in serum by biospecific adsorption onto blood group O erythrocyte membranes
Biochem. Biophys. Res. Commun.
77
700-707
1977
Homo sapiens
brenda
Race, C.; Zideman, D.; Watkins, W.M.
An alpha-D-galactosyltransferase associated with the blood-group B character
Biochem. J.
107
733-735
1968
Papio sp., Homo sapiens
brenda
Turcot, A.L.; Blancher, A.; Le Moullac-Vaidye, B.; Despiau, S.; Rocher, J.; Roubinet, F.; Szpirer, C.; Le Pendu, J.
Cloning of a rat gene encoding the histo-blood group B enzyme: rats have more than one Abo gene
Glycobiology
13
919-928
2003
Rattus norvegicus (Q8CFC4)
brenda
Nguyen, H.P.; Seto, N.O.L.; Cai, Y.; Leinala, E.K.; Borisova, S.N.; Palcic, M.M.; Evans, S.V.
The influence of an intramolecular hydrogen bond in differential recognition of inhibitory acceptor analogs by human ABO(H) blood group A and B glycosyltransferases
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278
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2003
Homo sapiens (P16442)
brenda
Ketcham, C.; Wang, F.; Fisher, S.Z.; Ercan, A.; van der Wel, H.; Locke, R.D.; Sirajud-Doulah, k.; Matta, K.L.; West, C.M.
Specificity of a soluble UDP-galactose:fucoside alpha1,3-galactosyltransferase that modifies the cytoplasmic glycoprotein Skp1 in Dictyostelium
J. Biol. Chem.
279
29050-29059
2004
Dictyostelium discoideum
brenda
Yazer, M.H.; Denomme, G.A.; Rose, N.L.; Palcic, M.M.
Amino-acid substitution in the disordered loop of blood group B-glycosyltransferase enzyme causes weak B phenotype
Transfusion
45
1178-1182
2005
Homo sapiens
brenda
Angulo, J.; Langpap, B.; Blume, A.; Biet, T.; Meyer, B.; Krishna, N.R.; Peters, H.; Palcic, M.M.; Peters, T.
Blood group B galactosyltransferase: insights into substrate binding from NMR experiments
J. Am. Chem. Soc.
128
13529-13538
2006
Homo sapiens (P16442), Homo sapiens
brenda
Blume, A.; Angulo, J.; Biet, T.; Peters, H.; Benie, A.J.; Palcic, M.; Peters, T.
Fragment-based screening of the donor substrate specificity of human blood group B galactosyltransferase using saturation transfer difference NMR
J. Biol. Chem.
281
32728-32740
2006
Homo sapiens
brenda
Letts, J.A.; Rose, N.L.; Fang, Y.R.; Barry, C.H.; Borisova, S.N.; Seto, N.O.; Palcic, M.M.; Evans, S.V.
Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases
J. Biol. Chem.
281
3625-3632
2006
Homo sapiens (P16442)
brenda
Persson, M.; Letts, J.A.; Hosseini-Maaf, B.; Borisova, S.N.; Palcic, M.M.; Evans, S.V.; Olsson, M.L.
Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif
J. Biol. Chem.
282
9564-9570
2007
Homo sapiens (P16442), Homo sapiens
brenda
Nakahara, T.; Hindsgaul, O.; Palcic, M.M.; Nishimura, S.
Computational design and experimental evaluation of glycosyltransferase mutants: engineering of a blood type B galactosyltransferase with enhanced glucosyltransferase activity
Protein Eng. Des. Sel.
19
571-578
2006
Homo sapiens (P16442)
brenda
Letts, J.A.; Persson, M.; Schuman, B.; Borisova, S.N.; Palcic, M.M.; Evans, S.V.
The effect of heavy atoms on the conformation of the active-site polypeptide loop in human ABO(H) blood-group glycosyltransferase B
Acta Crystallogr. Sect. D
63
860-865
2007
Homo sapiens (P16442), Homo sapiens
brenda
Persson, M.; Palcic, M.M.
A high-throughput pH indicator assay for screening glycosyltransferase saturation mutagenesis libraries
Anal. Biochem.
378
1-7
2008
Homo sapiens
brenda
Alfaro, J.A.; Zheng, R.B.; Persson, M.; Letts, J.A.; Polakowski, R.; Bai, Y.; Borisova, S.N.; Seto, N.O.; Lowary, T.L.; Palcic, M.M.; Evans, S.V.
ABO(H) blood group A and B glycosyltransferases recognize substrate via specific conformational changes
J. Biol. Chem.
283
10097-10108
2008
Homo sapiens (P16442)
brenda
Hosseini-Maaf, B.; Letts, J.A.; Persson, M.; Smart, E.; LePennec, P.; Hustinx, H.; Zhao, Z.; Palcic, M.M.; Evans, S.V.; Chester, M.A.; Olsson, M.L.
Structural basis for red cell phenotypic changes in newly identified, naturally occurring subgroup mutants of the human blood group B glycosyltransferase
Transfusion
47
864-875
2007
Homo sapiens (A5X6H3), Homo sapiens (A5X6H4), Homo sapiens (A5X6H5), Homo sapiens (A5X6H7), Homo sapiens (A5X6H8), Homo sapiens (Q6L638), Homo sapiens
brenda
Soya, N.; Shoemaker, G.K.; Palcic, M.M.; Klassen, J.S.
Comparative study of substrate and product binding to the human ABO(H) blood group glycosyltransferases
Glycobiology
19
1224-1234
2009
Homo sapiens
brenda
Sindhuwinata, N.; Munoz, E.; Munoz, F.J.; Palcic, M.M.; Peters, H.; Peters, T.
Binding of an acceptor substrate analog enhances the enzymatic activity of human blood group B galactosyltransferase
Glycobiology
20
718-723
2010
Homo sapiens
brenda
Seltsam, A.; Grueger, D.; Just, B.; Figueiredo, C.; Gupta, C.D.; Deluca, D.S.; Blasczyk, R.
Aberrant intracellular trafficking of a variant B glycosyltransferase
Transfusion
48
1898-1905
2008
Homo sapiens (P16442)
brenda
Yamamoto, F.; Yamamoto, M.; Blancher, A.
Generation of histo-blood group B transferase by replacing the N-acetyl-D-galactosamine recognition domain of human A transferase with the galactose-recognition domain of evolutionarily related murine alpha1,3-galactosyltransferase
Transfusion
50
622-630
2009
Homo sapiens
brenda
Johal, A.; Schuman, B.; Alfaro, J.; Borisova, S.; Seto, N.; Evans, S.
Sequence-dependent effects of cryoprotectants on the active sites of the human ABO(H) blood group A and B glycosyltransferases
Acta Crystallogr. Sect. D
68
268-276
2012
Homo sapiens
brenda
Adlercreutz, D.; Weadge, J.T.; Petersen, B.O.; Duus, J.; Dovichi, N.J.; Palcic, M.M.
Enzymatic synthesis of Gb3 and iGb3 ceramides
Carbohydr. Res.
345
1384-1388
2010
Homo sapiens
brenda
Schaefer, K.; Albers, J.; Sindhuwinata, N.; Peters, T.; Meyer, B.
A new concept for glycosyltransferase inhibitors: nonionic mimics of the nucleotide donor of the human blood group B galactosyltransferase
ChemBioChem
13
443-450
2012
Homo sapiens
brenda
Rademacher, C.; Landstroem, J.; Sindhuwinata, N.; Palcic, M.M.; Widmalm, G.; Peters, T.
NMR-based exploration of the acceptor binding site of human blood group B galactosyltransferase with molecular fragments
Glycoconj. J.
27
349-358
2010
Homo sapiens
brenda
Schuman, B.; Persson, M.; Landry, R.C.; Polakowski, R.; Weadge, J.T.; Seto, N.O.; Borisova, S.N.; Palcic, M.M.; Evans, S.V.
Cysteine-to-serine mutants dramatically reorder the active site of human ABO(H) blood group B glycosyltransferase without affecting activity: structural insights into cooperative substrate binding
J. Mol. Biol.
402
399-411
2010
Homo sapiens
brenda
Jorgensen, R.; Batot, G.; Mannerstedt, K.; Imberty, A.; Breton, C.; Hindsgaul, O.; Royant, A.; Palcic, M.M.
Structures of a human blood group glycosyltransferase in complex with a photo-activatable UDP-Gal derivative reveal two different binding conformations
Acta Crystallogr. Sect. F
70
1015-1021
2014
Homo sapiens (P16442)
brenda
Sindhuwinata, N.; Grimm, L.L.; Weissbach, S.; Zinn, S.; Munoz, E.; Palcic, M.M.; Peters, T.
Thermodynamic signature of substrates and substrate analogs binding to human blood group B galactosyltransferase from isothermal titration calorimetry experiments
Biopolymers
99
784-795
2013
Homo sapiens
brenda
Johal, A.R.; Blackler, R.J.; Alfaro, J.A.; Schuman, B.; Borisova, S.; Evans, S.V.
pH-induced conformational changes in human ABO(H) blood group glycosyltransferases confirm the importance of electrostatic interactions in the formation of the semi-closed state
Glycobiology
24
237-246
2014
Homo sapiens (P16442)
brenda
Gagnon, S.M.; Meloncelli, P.J.; Zheng, R.B.; Haji-Ghassemi, O.; Johal, A.R.; Borisova, S.N.; Lowary, T.L.; Evans, S.V.
High resolution structures of the human ABO(H) blood group enzymes in complex with donor analogs reveal that the enzymes utilize multiple donor conformations to bind substrates in a stepwise manner
J. Biol. Chem.
290
27040-27052
2015
Homo sapiens (P16442)
brenda
Wagner, G.K.; Pesnot, T.; Palcic, M.M.; Jorgensen, R.
Novel UDP-GalNAc Derivative structures provide insight into the donor specificity of human blood group glycosyltransferase
J. Biol. Chem.
290
31162-31172
2015
Homo sapiens (P16442)
brenda
Schaefer, K.; Sindhuwinata, N.; Hackl, T.; Koetzler, M.P.; Niemeyer, F.C.; Palcic, M.M.; Peters, T.; Meyer, B.
A nonionic inhibitor with high specificity for the UDP-Gal donor binding site of human blood group B galactosyltransferase: design, synthesis, and characterization
J. Med. Chem.
56
2150-2154
2013
Homo sapiens
brenda
Grimm, L.; Weissbach, S.; Fluegge, F.; Begemann, N.; Palcic, M.; Peters, T.
Protein NMR studies of substrate binding to human blood group A and B glycosyltransferases
ChemBioChem
18
1260-1269
2017
Homo sapiens (P16442)
brenda
Weissbach, S.; Fluegge, F.; Peters, T.
Substrate binding drives active-site closing of human blood group B balactosyltransferase as revealed by hot-spot labeling and NMR spectroscopy experiments
ChemBioChem
19
970-978
2018
Homo sapiens (P16442), Homo sapiens
brenda
Fluegge, F.; Peters, T.
Insights into allosteric control of human blood group A and B glycosyltransferases from dynamic NMR
ChemistryOpen
8
760-769
2019
Homo sapiens (P16442)
brenda
Strecker, C.; Peters, H.; Hackl, T.; Peters, T.; Meyer, B.
Fragment growing to design optimized inhibitors for human blood group B galactosyltransferase (GTB)
ChemMedChem
14
1336-1342
2019
Homo sapiens (P16442), Homo sapiens
brenda
Blackler, R.J.; Gagnon, S.M.; Polakowski, R.; Rose, N.L.; Zheng, R.B.; Letts, J.A.; Johal, A.R.; Schuman, B.; Borisova, S.N.; Palcic, M.M.; Evans, S.V.
Glycosyltransfer in mutants of putative catalytic residue Glu303 of the human ABO(H) A and B blood group glycosyltransferases GTA and GTB proceeds through a labile active site
Glycobiology
27
370-380
2017
Homo sapiens (P16442)
brenda
Gagnon, S.M.L.; Legg, M.S.G.; Sindhuwinata, N.; Letts, J.A.; Johal, A.R.; Schuman, B.; Borisova, S.N.; Palcic, M.M.; Peters, T.; Evans, S.V.
High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release
Glycobiology
27
966-977
2017
Homo sapiens (P16442)
brenda
Gagnon, S.; Legg, M.; Polakowski, R.; Letts, J.; Persson, M.; Lin, S.; Zheng, R.; Rempel, B.; Schuman, B.; Haji-Ghassemi, O.; Borisova, S.; Palcic, M.; Evans, S.
Conserved residues Arg188 and Asp302 are critical for active site organization and catalysis in human ABO(H) blood group A and B glycosyltransferases
Glycobiology
28
624-636
2018
Homo sapiens (P16422)
brenda
Fluegge, F.; Peters, T.
Complete assignment of Ala, Ile, Leu, Met and Val methyl groups of human blood group A and B glycosyltransferases using lanthanide-induced pseudocontact shifts and methyl-methyl NOESY
J. Biomol. NMR
70
245-259
2018
Homo sapiens (P16442)
brenda
Yamamoto, M.; Cid, E.; Yamamoto, F.
Crosstalk between ABO and Forssman (FORS) blood group systems FORS1 antigen synthesis by ABO gene-encoded glycosyltransferases
Sci. Rep.
7
41632
2017
Mus musculus (P38649)
brenda
Cid , E.; Yamamoto, M.; Yamamoto, F.
Amino acid substitutions at sugar-recognizing codons confer ABO blood group system-related alpha1,3 Gal(NAc) transferases with differential enzymatic activity
Sci. Rep.
9
846
2019
Homo sapiens (P16442)
brenda
Yamamoto, M.; Tarasco, M.C.; Cid, E.; Kobayashi, H.; Yamamoto, F.
ABO blood group A transferase and its codon 69 substitution enzymes synthesize FORS1 antigen of FORS blood group system
Sci. Rep.
9
9717
2019
Homo sapiens (P16442)
brenda