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Enzyme Nomenclature
Information on EC 2.4.1.37 - fucosylgalactoside 3-alpha-galactosyltransferase
Word Map on EC 2.4.1.37
- 2.4.1.37
- udp-galnac
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trisaccharide
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cis-ab
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galalpha1-3galbeta1-4glcnac-r
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anti-b
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.4.1.37
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RECOMMENDED NAME
GeneOntology No.
fucosylgalactoside 3-alpha-galactosyltransferase
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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)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37257-33-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain BFM/2Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
strain BFM/2Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
strain CAST/Ei and HMI/Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
strain CAST/Ei and HMI/Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
strain BALB/c, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
strain BALB/c, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
strain ZBN, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
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strain ZBN, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
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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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Uniprot
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489117, 489118, 489119, 489120, 489123, 489124, 489125, 489127, 660551, 690409, 703890, 703919, 706853, 718480, 719219, 719291, 719571, 720246, 735779, 736611
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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
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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
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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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human blood group B galactosyltransferase responsible for the biosynthesis of human blood group antigens
physiological function
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the enzyme catalyzes the final step in ABO(H) blood group B antigen synthesis through sugar transfer from activated donor to the H antigen acceptor
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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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
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tetramethylrhodamine labelled disaccharide
-
-
?
UDP-alpha-D-galactose + 8-methoxycarbonyloctyl beta-D-Galp-(1->4)-beta-D-Glcp
?
-
-
-
-
?
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
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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
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90% of the activity with alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
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-
?
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)
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-
-
-
?
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
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-
-
-
?
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
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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)
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-
-
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?
UDP-D-galactose + Fucalpha(1,2)Galbeta-1-benzyl
UDP + alpha-D-Gal(1,3)Fucalpha(1,2)Galbeta-1-benzyl
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-
-
-
?
UDP-D-galactose + Fucalpha-1-(4-nitrophenol)
UDP + alpha-D-Gal(1,3)Fucalpha-1-(4-nitrophenol)
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-
-
-
?
UDP-D-galactose + Fucalpha-1-benzyl
UDP + alpha-D-Gal(1,3)Fucalpha-1-benzyl
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-
-
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?
UDP-D-galactose + fucosylated Skp1 protein
UDP + alpha-D-galactosyl(1-3)-fucosyl-Skp1 protein
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-
-
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?
UDP-D-galactose + H type 3-Sp-biotin
UDP + ?
preferred substrates
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-
?
UDP-D-galactose + H-disaccharide
UDP + alpha-D-galactosyl-1,3-H disaccharide
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synthetic substrate
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-
?
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
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-
?
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
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i.e. alpha-L-Fucp-(1,2)-beta-DGalp-O-(CH2)7CH3
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-
?
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
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GTB catalyzes the transfer of galactose from UDP-Gal to the C3 position of the terminal galactose of H antigen acceptors
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-
?
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 + 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
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-
-
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?
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]
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-
-
-
?
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-galactose + 2'-fucosyllactose
UDP + N-acetyl-D-galactosyl-(1-3)-2'-fucosyllactose
low A-type activity
-
-
?
UDP-N-acetyl-D-galactose + 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
-
-
-
-
?
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-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
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-
?
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
-
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-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'-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'-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 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-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
?
-
-
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-D-galactose + fucosylated Skp1 protein
UDP + alpha-D-galactosyl(1-3)-fucosyl-Skp1 protein
-
-
-
-
?
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
-
H-antigen disaccharide
-
-
-
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 + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein 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
-
-
-
-
?
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-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
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
-
-
-
?
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
-
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
-
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
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
0.1 mM, significant increase in activity, more significant acceleration at 10 mM
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
Mg2+
Mn2+
Mg2+
-
0.1 mM, significant increase in activity, more significant acceleration at 10 mM
Mn2+
-
divalent cation required, Mn2+ most effective, optimum concentration 20 mM
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 24°C, GTB requires divalent metal ions for full activity
Mn2+
-
divalent cation required, Mn2+ most effective, optimum concentration 20 mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9-(5-O-alpha-D-galactopyranosyl)-D-arabinityl-1,3,7-trihydropurine-2,6,8-trione
-
extremely specific inhibitor
-
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
Fucalpha(1,2)Galbeta1-benzyl
-
competitive, 37% and 61% inhibition at 1 mM and 4 mM, respectively
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 alpha-L-fucopyranosyl-(1-2)-beta-D-gulopyranoside
-
88% inhibition at 0.025 mM, competitive
additional information
-
not inhibited by ethanolamine, 2-amino-2-deoxy glucosamine, and 2-amino-2-deoxy-mannosamine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
1.2
Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-(4-nitrophenol)
-
pH 7.4, 22°C
0.006
Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-Skp1 protein
-
pH 7.4, 22°C
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
-
-
0.032
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
1.5
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
0.054
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
0.25
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
0.023
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
0.027
UDP-galactose
wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme
0.035
UDP-galactose
-
with L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3 as acceptor
0.042
UDP-galactose
mutant D262N; mutant D262N; mutant D262N; mutant D262N; mutant D262N; mutant D262N
0.052
UDP-galactose
mutant F216I; mutant F216I; mutant F216I; mutant F216I; mutant F216I; mutant F216I
0.06
UDP-galactose
-
with L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3 as acceptor
0.222
UDP-galactose
mutant A268T; mutant A268T; mutant A268T; mutant A268T; mutant A268T; mutant A268T
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
0.3
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, hyperbolic dependence on UDP-Gal concentration
-
additional information
additional information
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
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
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
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
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
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
-
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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
Homo sapiens
-
37°C, pH 7.0
1.2
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O(CH2)8CO2CH3
Homo sapiens
-
37°C, pH 7.0
0.15
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
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
Homo sapiens
-
deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose
8
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
Homo sapiens
-
mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose
0.039
UDP-galactose
Homo sapiens
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
mutant A268T; mutant A268T; mutant A268T; mutant A268T; mutant A268T; mutant A268T
2
UDP-galactose
Homo sapiens
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
mutant F216I; mutant F216I; mutant F216I; mutant F216I; mutant F216I; mutant F216I
2.5
UDP-galactose
Homo sapiens
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
mutant D262N; mutant D262N; mutant D262N; mutant D262N; mutant D262N; mutant D262N
5.1
UDP-galactose
Homo sapiens
A5X6H3, A5X6H4, A5X6H5, A5X6H7, A5X6H8, Q6L638
wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme; wild-type enzyme
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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, 37°C
0.005
octyl 3'-amino-3'deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.026
octyl alpha-L-fucopyranosyl-(1-2)-beta-D-gulopyranoside
-
recombinant enzyme
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.9
9-(D-1-deoxy-arabinit-1-yl)-1,3,7-trihydropurine-2,6,8-trione
Homo sapiens
-
pH 7.0, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3
6.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
no B-type enzyme expression in small intestine, striated muscle, heart, liver, lung, skin, uterus, testis, lymph node, or brain
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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
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes
additional information
three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes
additional information
three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes
additional information
three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes
additional information
three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes
additional information
three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes; three-dimensional structure molecular modeling of wild-type and mutant enzymes
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic domain with and without H-antigen and UDP, at 1.32 and 1.65 A resolution
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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
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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
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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
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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
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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
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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
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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
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 2400fold by 2 steps ion exchange chromatography, HI chromatography, and gel filtration to homogeneity
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one-step procedure involving absorption onto group 0 erythrocyte membranes followed by elution with the low molecular weight H-active trisaccharide 2'-fucosyllactose
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purified by successive ion exchange chromatography with SP sepharose FF and affinity chromatography with UDP-hexanolamine sepharose
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recombinant enzyme from Escherichia coli by cation exchange chromatograophy, UDP-hexanolamine affinity chromatography, and dialysis
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recombinant wild-type and mutant M186V enzymes from Escherichia coli by ion exchange and UDP-hexanolamine affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strain BL21
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expressed in Escherichia coli TG-1, the membrane-anchoring domain is replaced with an ompA bacterial secretory signal
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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
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
transfected into HeLa cells derived from human adenocarcinoma of uterus
transfected into HeLa cells derived from human adenocarcinoma of uterus
transfected into HeLa cells derived from human adenocarcinoma of uterus
transfected into HeLa cells derived from human adenocarcinoma of uterus
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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; naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
C80S/C196S
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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
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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; naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
DELTA68-354
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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; naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; 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; naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
M186V
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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; naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; naturally occurring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview
M214G
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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
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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
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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
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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
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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
R188S
S185C
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mutant enzyme exhibits 4.8fold elevations in kcat/Km for UDP-glucose relative to that of wild-type enzyme
S185N
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mutant enzyme exhibits 4.3fold elevations in kcat/Km for UDP-glucose relative to that of wild-type enzyme
additional information
additional information
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screening of a saturation mutagenesis library for mutant determination with altered cosubstrate specificity
additional information
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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; identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview
additional information
identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occruing polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview; identification of naturally occurring polymorphisms in the ABO gene, phenotypes, overview
additional information
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construction of truncated GTB monomers composed of the full C-terminal and catalytic domain as well as a truncated N-terminal domain
additional information
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ABO glycosyltransferase polymorphisms leading to reduced activity and substrate recognition, phenotyping and genotyping, overview
additional information
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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
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chimeric GTA and GTB enzymes are generated (AABB, ABBA and ABBB)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.37)
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