Any feedback?
Information on EC 2.4.1.37 - fucosylgalactoside 3-alpha-galactosyltransferase and Organism(s) Homo sapiens and UniProt Accession P16442
for references in articles please use BRENDA:EC2.4.1.37Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.4.1.37 fucosylgalactoside 3-alpha-galactosyltransferaseIUBMB Comments
Acts on blood group substance, and can use a number of 2-fucosyl-galactosides as acceptors.
Specify your search results
Word Map
- 2.4.1.37
-
serological
- udp-galnac
- trisaccharide
-
abo-incompatible
-
galalpha1-3galbeta1-4glcnac-r
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
b transferase, b glycosyltransferase, blood group b galactosyltransferase, alpha(1-3)galactosyltransferase, blood group b glycosyltransferase, histo-blood group abo system transferase, blood group b alpha-(1,3)-galactosyltransferase, abo(h) blood group b glycosyltransferase, blood group b glycosyltransferase gtb, glycosyltransferases b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GTB
-
blood group B glycosyltransferase
blood-group substance B-dependent galactosyltransferase
-
-
-
-
glycoprotein-fucosylgalactoside alpha-galactosyltransferase
-
-
-
-
GTB
-
-
histo-blood group B transferase
histo-blood substance B-dependent galactosyltransferase
-
-
-
-
UDP-galactose:O-alpha-L-fucosyl(1-2)D-galactose alpha-D-galactosyltransferase
-
-
-
-
UDPgalactose:glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose 3-alpha-D-galactosyltransferase
-
-
-
-
[blood group substance] alpha-galactosyltransferase
-
-
-
-
additional information
the enzyme belongs to the ABO glycosyltransferases
blood group B glycosyltransferase
-
histo-blood group B transferase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY
37257-33-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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-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)-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 + 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-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-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
-
-
?
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-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 + 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-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 + 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 + 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 + 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 + 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-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-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 + 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-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-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 + 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
-
-
-
?
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 + 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
-
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 + 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
?
-
the enzyme shows weakened activity with B antigen variants resulting from ABO polymophisms, phenotyping and genotyping of ABO antigens, overview
-
-
?
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
?
-
-
enzyme-substrate interaction analysis by electrospray ionization mass spectrometry, binding of substrate and product analogues, overview
-
-
?
additional information
?
-
-
galactose is used as an acceptor analogue and UDP as a donor analogue in all soaking trials
-
-
?
NATURAL SUBSTRATE
NATURAL 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
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-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-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-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 + 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
-
acts on blood group substance
-
-
?
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
-
-
-
?
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
-
-
?
additional information
?
-
the enzyme shows weakened activity with B antigen variants resulting from ABO polymophisms, phenotyping and genotyping of ABO antigens, 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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Mn2+
Ca2+
-
0.1 mM, significant increase in activity, more significant acceleration at 10 mM
Mg2+
Mn2+
Mn2+
the enzyme has a characteristic 211DVD213 motif that coordinates to a Mn2+ ion shown to be critical in donor binding and catalysis
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+
-
activates 9fold at 24°C, GTB requires divalent metal ions for full activity
Mn2+
-
required, in the absence of divalent metal ion, GTB does not exhibit any appreciable affinity for its native donor UDP-Gal
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
9-(5-O-alpha-D-galactopyranosyl)-D-arabinityl-1,3,7-trihydropurine-2,6,8-trione
-
extremely specific inhibitor
additional information
-
not inhibited by ethanolamine, 2-amino-2-deoxy glucosamine, and 2-amino-2-deoxy-mannosamine
-
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
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
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
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
-
-
0.1
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant D302E/D316E, pH 7.0, 37°C
0.117
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant D302A/D316A, pH 7.0, 37°C
0.032
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
0.054
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
0.035
UDP-galactose
-
with L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3 as acceptor
0.06
UDP-galactose
-
with L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3 as acceptor
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 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
-
kinetic mechanism and thermodynamic analysis of GTB using electrospray ionization mass spectrometry, comparison to GTA, EC 2.4.1.40
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-D-GlcNAcp-O(CH2)7CH3
37°C, pH 7.0
1.2
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O(CH2)8CO2CH3
37°C, pH 7.0
0.002
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant D302A/D316A, pH 7.0, 37°C
2.4
alpha-Fuc-(1->2)-beta-D-Gal-(CH2)7CH3
mutant D302E/D316E, pH 7.0, 37°C
0.15
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc
0.41
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc
0.7
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
mutant C80S/C196S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-GalNAc
5.6
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
mutant C80S/C196S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose
7.3
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
deletion construct with amino acids 68-354, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose
8
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
-
mutant C89S/C196S/C209S, pH 7.0, temperature not specified in the publication, co-substrate: donor UDP-alpha-D-galactose
5.1
UDP-galactose
wild-type enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
1-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine
pH not specified in the publication, temperature not specified in the publication
0.271
1-[3-(naphthalen-1-yl)-1,2,4-thiadiazol-5-yl]piperazine
pH not specified in the publication, temperature not specified in the publication
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
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
489115, 659283, 674703, 676942, 690230, 693025, 706852, 735391, 736196, 736489, 736492, 756450, 756456, 756474, 756482, 756888, 756889, 757247, 758454, 758457
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
Uniprot
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
human blood group B galactosyltransferase responsible for the biosynthesis of human blood group antigens
physiological function
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
physiological function
the deletion of exon 3 or 4, but not of exon 2 or 5, of human GTA transcripts bestows moderate Forssman glycolipid synthase activity. Strong Forssman glycolipid synthase activity is attained, in addition to GTA and GTB activities, by cointroducing one of those deletions and the replacement of the LeuGlyGly tripeptide sequence at codons 266 to 268 by GlyGlyAla substitution, i.e. to the residues of Forssman glycolipid synthase
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BGAT_HUMAN
354
1
40934
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
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
additional information
three-dimensional structure molecular modeling of wild-type and mutant enzymes
additional information
three-dimensional structure molecular modeling of wild-type and mutant enzymes
additional information
three-dimensional structure molecular modeling of wild-type and mutant enzymes
additional information
three-dimensional structure molecular modeling of wild-type and mutant enzymes
additional information
three-dimensional structure molecular modeling of wild-type and mutant enzymes
additional information
-
three-dimensional structure molecular modeling of wild-type and mutant enzymes
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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 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
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 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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
R188K
site-directed mutagenesis, the mutant shows affected substrate binding
R188S
site-directed mutagenesis, the mutant shows affected substrate binding
S185C
mutant enzyme exhibits 4.8fold elevations in kcat/Km for UDP-glucose relative to that of wild-type enzyme
S185N
mutant enzyme exhibits 4.3fold elevations in kcat/Km for UDP-glucose relative to that of wild-type enzyme
A268T
C80S/C196S
-
both the double and triple mutants show differing levels of disorder depending on their liganded state, with the level of disorder increasing when substrates are bound.The double mutant shows disorder over residues 177-180 in the unliganded and H-antigen bound forms, with disorder increasing to residues 176-185 for the UDP-, UDP + H-, and UDP-alpha-D-galactose + 3-deoxy-Gal inactive acceptor analog-bound structures. The double mutant has a reduction in Km for both donor and acceptor substrates. Mutation shows little effect over kcat
C80S/C196S/C209S
-
both the double and triple mutants show differing levels of disorder depending on their liganded state, with the level of disorder increasing when substrates are bound.The unliganded triple mutant shows a nearly complete internal loop, with residues 176-181 disordered for the H-antigen-bound structure and 177-179 disordered for the UDP-bound structure. The UDP + H- and UDPGal + 3-deoxy-Gal inactive acceptor analog-bound structures of the triple mutant show an internal loop completely disordered over residues 176-184. The triple Cys-to-Ser mutant has an acceptor Km elevated approximately 5times over wild type, while the donor Km has doubled. Mutation shows little effect over kcat
D262N
DELTA68-354
-
construct in which the N-terminal transmembrane domain is deleted. Deletion results in a more crystallizable protein
F216I
I192T
M186V
-
site-directed mutagenesis, mutation is a naturally occuring polymorphism, amino-acid substitution in the disordered loop of the enzyme causes a weak B phenotype of erythrocytes, mutant enzyme shows reduced activity compared to the wild-type enzyme
M189V
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
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
additional information
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
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
ABO glycosyltransferase polymorphisms leading to reduced activity and substrate recognition, phenotyping and genotyping, overview
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
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
-
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)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
one-step procedure involving absorption onto group 0 erythrocyte membranes followed by elution with the low molecular weight H-active trisaccharide 2'-fucosyllactose
-
purified by successive ion exchange chromatography with SP sepharose FF and affinity chromatography with UDP-hexanolamine sepharose
-
recombinant enzyme from Escherichia coli by cation exchange chromatograophy, UDP-hexanolamine affinity chromatography, and dialysis
-
recombinant wild-type and mutant M186V enzymes from Escherichia coli by ion exchange and UDP-hexanolamine affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ABO glycosyltransferase polymorphisms, phenotyping and genotyping, overview
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strain BL21
-
expressed in Escherichia coli TG-1, the membrane-anchoring domain is replaced with an ompA bacterial secretory signal
-
gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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)
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
-
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
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
1-21
2000
Homo sapiens
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
Glycoconj. J.
16
599-606
2000
Homo sapiens
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
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
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
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
323-328
1995
Homo sapiens
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
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
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
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
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
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
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
J. Biol. Chem.
278
49191-49195
2003
Homo sapiens (P16442)
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
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
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
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)
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
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)
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
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
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)
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
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
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
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)
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
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
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
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
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
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
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)
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
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)
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)
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)
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
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)
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
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)
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
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)
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)
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)
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)
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)
EXTERNAL LINKS (specific for EC-Number 2.4.1.37)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
