Information on EC 2.4.1.37 - fucosylgalactoside 3-alpha-galactosyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
2.4.1.37
-
RECOMMENDED NAME
GeneOntology No.
fucosylgalactoside 3-alpha-galactosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl(1->2)]-D-galactosyl-R (where R can be OH, an oligosaccharide or a glycoconjugate)
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycosphingolipid biosynthesis - lacto and neolacto series
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:alpha-L-fucosyl-(1->2)-D-galactoside 3-alpha-D-galactosyltransferase
Acts on blood group substance, and can use a number of 2-fucosyl-galactosides as acceptors.
CAS REGISTRY NUMBER
COMMENTARY hide
37257-33-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Skp1B overexpressing strain HW302
-
-
Manually annotated by BRENDA team
white-handed gibbon
-
-
Manually annotated by BRENDA team
japanese monkey
-
-
Manually annotated by BRENDA team
strain BFM/2Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
strain BFM/2Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
strain CAST/Ei and HMI/Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
strain CAST/Ei and HMI/Msf, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
strain BALB/c, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
strain BALB/c, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
Uniprot
Manually annotated by BRENDA team
strain ZBN, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
-
-
Manually annotated by BRENDA team
strain ZBN, has a cis-AB gene that encodes an enzyme with both A and B transferase activities
-
-
Manually annotated by BRENDA team
2 distinct alpha-3-D-galactosyltransferases: one which is more tightly membrane-bound, resembles the human B-gene-specific transferase in its acceptor specificity, and the second, which is a more soluble enzyme transfers D-galactose to the same positional linkage in unsubstituted beta-D-galactosyl residues
-
-
Manually annotated by BRENDA team
blood group B donors
-
-
Manually annotated by BRENDA team
B-type gene Abo2
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
human blood group B galactosyltransferase responsible for the biosynthesis of human blood group antigens
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + UDP-GalNAc
?
show the reaction diagram
-
-
-
-
?
UDP-2-deoxygalactose + L-fucosyl-alpha-1,2-beta-galactosyl-OR
UDP + 2-deoxy-alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-OR
show the reaction diagram
-
tetramethylrhodamine labelled disaccharide
-
-
?
UDP-6-deoxygalactose + L-fucosyl-alpha-1,2-beta-galactosyl-OR
UDP + 6-deoxy-alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-OR
show the reaction diagram
-
tetramethylrhodamine labelled disaccharide
-
-
?
UDP-alpha-D-galactose + 8-methoxycarbonyloctyl beta-D-Galp-(1->4)-beta-D-Glcp
?
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-galactose + alpha-L-Fuc-(1-2)-beta-D-Gal-octyl
?
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-galactose + alpha-L-Fuc-(1->2)-beta-D-Gal-octyl
?
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
show the reaction diagram
UDP-D-galactose + 2'-fucosyllactose
UDP + D-galactosyl-(1-3)-2'-fucosyllactose
show the reaction diagram
-
-
-
?
UDP-D-galactose + alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-DGlcNAcp-O(CH2)7CH3
UDP + alpha-L-Fuc-(1,2)-[alpha-D-Galp-(1,3)-]-beta-D-Galp-(1,3)-beta-DGlcNAcp-O(CH2)7CH3
show the reaction diagram
-
69% of the activity with alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
-
-
?
UDP-D-galactose + alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
UDP + alpha-L-Fucp-(1,2)-[alpha-D-Galp-(1,3)-]-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
show the reaction diagram
-
90% of the activity with alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
-
-
?
UDP-D-galactose + alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
UDP + alpha-L-Fuc-(1,2)-[alpha-D-Galp-(1,3)-]-beta-D-Galp-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-(4-nitrophenol)
UDP + alpha-D-Gal-1,3-Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-(4-nitrophenol)
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-benzyl
UDP + alpha-D-Gal(1,3)Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-benzyl
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-Skp1 protein
UDP + alpha-D-Gal(1,3)Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-Skp1 protein
show the reaction diagram
-
best substrate, Skp1A1-(HW120)-myc and Skp1 from strain HL250
-
-
?
UDP-D-galactose + Fucalpha(1,2)Galbeta-1-(4-nitrophenol)
UDP + alpha-D-Gal(1,3)Fucalpha(1,2)Galbeta-1-(4-nitrophenol)
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha(1,2)Galbeta-1-benzyl
UDP + alpha-D-Gal(1,3)Fucalpha(1,2)Galbeta-1-benzyl
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha-1-(4-nitrophenol)
UDP + alpha-D-Gal(1,3)Fucalpha-1-(4-nitrophenol)
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + Fucalpha-1-benzyl
UDP + alpha-D-Gal(1,3)Fucalpha-1-benzyl
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + fucosylated Skp1 protein
UDP + alpha-D-galactosyl(1-3)-fucosyl-Skp1 protein
show the reaction diagram
-
-
-
-
?
UDP-D-galactose + H type 3-Sp-biotin
UDP + ?
show the reaction diagram
preferred substrates
-
-
?
UDP-D-galactose + H-disaccharide
UDP + alpha-D-galactosyl-1,3-H disaccharide
show the reaction diagram
-
synthetic substrate
-
-
?
UDP-galactose + 2'-fucosyllactose
UDP + alpha-D-galactosyl-1,3-[2'-fucosyllactose]
show the reaction diagram
UDP-galactose + alpha-L-Fuc-(1,2)-beta-D-Gal-O-octyl
UDP + alpha-L-Fuc(1,2)-[alpha-D-Galp-(1,3)-]-beta-D-Gal-O-octyl
show the reaction diagram
it is propose that, upon acceptor binding, GTB uses the Asp302 and Glu303 side chains as molecular tweezers to promote bound UDP-Gal but not UDP-Glc into a transition state that leads to product formation
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-beta-D-galactosyl-O-(CH2)7CH3
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-beta-D-galactosyl-O-(CH2)7CH3
show the reaction diagram
-
i.e. alpha-L-Fucp-(1,2)-beta-DGalp-O-(CH2)7CH3
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactose
show the reaction diagram
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactosyl-R
show the reaction diagram
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-R
show the reaction diagram
UDP-galactose + alpha-L-fucosyl-(1-2)-D-galactosyl-O-R
UDP + alpha-D-galactosyl-(1-3)-[alpha-L-fucosyl-(1-2)]-D-galactosyl-O-R
show the reaction diagram
UDP-galactose + blood group antigen
UDP + alpha-D-galactosyl-blood group antigen
show the reaction diagram
-
GTB catalyzes the transfer of galactose from UDP-Gal to the C3 position of the terminal galactose of H antigen acceptors
-
-
?
UDP-galactose + blood group antigen H
UDP + alpha-D-galactosyl-blood group antigen H
show the reaction diagram
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
UDP-galactose + H-active glycoprotein
UDP + B-active substance
show the reaction diagram
-
-
-
?
UDP-galactose + L-2'-L-fucosyllactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactosyl-D-glucose
show the reaction diagram
-
-
-
-
?
UDP-galactose + L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3
UDP + alpha-D-galactosyl-1,3[alpha-L-fucosyl-1,2]-alpha-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
UDP + alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
UDP-galactose + lacto-N-fucopentaose I
UDP + alpha-D-galactosyl-1,3-[lacto-N-fucopentaose I]
show the reaction diagram
-
-
-
-
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-[N-acetyl-lactosamine]
show the reaction diagram
-
-
-
-
?
UDP-galactose + O-alpha-L-fucosyl-1,2-galactose
UDP + alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactopyranoside
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl 3-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[3-O-methyl-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl 4-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[4-O-methyl-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl 6'-amino-6'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[6'-amino-6'-deoxy-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
UDP-galactose + octyl 6'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[6'-deoxy-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl 6'-fluoro-6'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[6'-fluoro-6'-deoxy-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-galactose + octyl 6'-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[6'-O-methyl-alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
UDP-galactose + octyl alpha-L-xylo-hexopyranosyl-(1-2)-beta-D-galactopyranoside
UDP + alpha-D-galactosyl-1,3-[alpha-L-xylo-hexopyranosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-glucose + Fucalpha1-2Galbeta-O(CH2)7CH3
?
show the reaction diagram
-
wild-type enzyme shows very low activity. Mutants, Ser185Asn and Ser185Cys, exhibit 4.3fold and 4.8fold elevation in kcat/Km for UDP-glucose relative to that of wild-type enzyme
-
-
?
UDP-glucose + L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
UDP + alpha-D-glucosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
UDP-N-acetyl-D-galactose + 2'-fucosyllactose
UDP + N-acetyl-D-galactosyl-(1-3)-2'-fucosyllactose
show the reaction diagram
low A-type activity
-
-
?
UDP-N-acetyl-D-galactose + H type 3-Sp-biotin
UDP + ?
show the reaction diagram
low A-type activity
-
-
?
UDP-N-acetylgalactosamine + 2'-fucosyllactose
UDP + N-acetyl-alpha-D-galactosyl-1,3-[2'-fucosyllactose]
show the reaction diagram
-
-
-
-
?
UDP-N-acetylgalactosamine + L-2'-fucosyllactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-D-glucose
show the reaction diagram
-
-
-
-
?
UDP-N-acetylgalactosamine + L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3
UDP + N-acetyl-alpha-D-galactosyl-1,3[alpha-L-fucosyl-1,2]-alpha-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
UDP-N-acetylgalactosamine + L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
UDP + N-acetyl-alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-beta-D-galactosyl-O(CH2)7CH3
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-D-galactose + fucosylated Skp1 protein
UDP + alpha-D-galactosyl(1-3)-fucosyl-Skp1 protein
show the reaction diagram
-
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactose
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactose
show the reaction diagram
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl(1,2)]-D-galactosyl-R
show the reaction diagram
-
-
-
-
?
UDP-galactose + alpha-L-fucosyl-(1,2)-D-galactosyl-R
UDP + alpha-D-galactosyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactosyl-R
show the reaction diagram
UDP-galactose + alpha-L-fucosyl-(1-2)-D-galactosyl-O-R
UDP + alpha-D-galactosyl-(1-3)-[alpha-L-fucosyl-(1-2)]-D-galactosyl-O-R
show the reaction diagram
-
H-antigen disaccharide
-
-
-
UDP-galactose + blood group antigen
UDP + alpha-D-galactosyl-blood group antigen
show the reaction diagram
-
GTB catalyzes the transfer of galactose from UDP-Gal to the C3 position of the terminal galactose of H antigen acceptors
-
-
?
UDP-galactose + blood group antigen H
UDP + alpha-D-galactosyl-blood group antigen H
show the reaction diagram
UDP-galactose + glycoprotein alpha-L-fucosyl-1,2-D-galactose
UDP + glycoprotein alpha-D-galactosyl-1,3-[alpha-L-fucosyl-1,2]-D-galactose
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
0.1 mM, significant increase in activity, more significant acceleration at 10 mM
Co2+
-
slight activation
Hg
-
structures of the mercury derivative of GTB and GTB C209A, mercury does not affect the conformation of active-site residues, the structure of GTB C209A demonstrates that the mercury coordinated by Cys209 is partially responsible for the disorder of the 16-amino-acid internal loop observed in the heavy-atom structure of GTB
KCl
-
lower activity compared to NaCl, best at 50 mM
NaCl
-
preferred salt, best at 50 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(1-benzothiophen-3-yl)methanamine
-
-
1-(2-chloro-6-fluorobenzyl)piperazine
-
-
1-(3-methoxyphenyl)piperazine
-
-
1-(3-phenyl-1,2,4-thiadiazol-5-yl)-1,4-diazepane
-
-
1-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine
-
-
1-methyl-1H-benzotriazole-5-carboxylic acid
-
-
2,3-dimethylquinoxaline-6-carboxylic acid
-
-
7-aminothieno[2,3-b]pyrazine-6-carboxylic acid
-
-
9-(D-1-deoxy-arabinit-1-yl)-1,3,7-trihydropurine-2,6,8-trione
-
-
9-D-ribityl-1,3,7-trihydropurine-2,6,8-trione
-
-
alpha-L-fucosyl-(1-2)-beta-D-(3-amino)-galactosyl-O-R
-
complex mode inhibitor, binding structure, Met226 is involved by interacting with the C3-position group
alpha-L-fucosyl-(1-2)-beta-D-(3-deoxy)-galactosyl-O-R
-
competitive inhibitor, binding structure, Met226 is involved by interacting with the C3-position group
EDTA
-
complete inhibition
Fucalpha(1,2)Galbeta1-benzyl
-
competitive, 37% and 61% inhibition at 1 mM and 4 mM, respectively
N-methyl-1-[3-(pyridin-3-yl)phenyl]methanamine
-
-
N-methyl-1-[3-(pyridin-4-yl)phenyl]methanamine
-
-
octyl 3'-amino-3'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
octyl 3'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
octyl alpha-L-fucopyranosyl-(1-2)-beta-D-gulopyranoside
UDP
-
competitive with respect to UDP-galactose
UDP-N-acetylgalactosamine
-
weak, competitive with respect to UDP-galactose
additional information
-
not affected by Tween 20 at 0.1-1.0%
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha-L-Fuc-(1,2)-beta-D-3-deoxy-Gal-O-octyl
-
i.e. 3DD, an acceptor substrate analogue, accelerates enzymatic hydrolysis of UDP-Gal
DTT
-
required, best at 2 mM
additional information
-
not affected by Tween 20 at 0.1-1.0%
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08 - 0.5
2'-fucosyllactose
1.6
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-DGlcNAcp-O(CH2)7CH3
-
37C, pH 7.0
0.184
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
-
37C, pH 7.0
0.022
alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
-
37C, pH 7.0
0.032 - 0.35
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
1.2
Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-(4-nitrophenol)
-
pH 7.4, 22C
2.2
Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-benzyl
-
pH 7.4, 22C
0.006
Fucalpha(1,2)Galbeta(1,3)GlcNAcalpha-1-Skp1 protein
-
pH 7.4, 22C
0.82
Fucalpha(1,2)Galbeta-1-(4-nitrophenol)
-
pH 7.4, 22C
0.84
Fucalpha(1,2)Galbeta1-benzyl
-
pH 7.4, 22C
3.7
Fucalpha-1-(4-nitrophenol)
-
pH 7.4, 22C
3.8
Fucalpha-1-benzyl
-
pH 7.4, 22C
1.5 - 3.22
L-fucosyl-alpha-1,2-alpha-D-galactosyl-O(CH2)7CH3
0.022 - 0.281
L-fucosyl-alpha-1,2-beta-D-galactosyl-O(CH2)7CH3
0.027 - 0.116
L-fucosyl-alpha-1,2-beta-galactosyl-O(CH2)7CH3
2.5
lacto-N-fucopentaose I
-
-
0.8
N-acetyllactosamine
-
-
2.2
O-alpha-L-fucosyl-1,2-galactose
-
-
0.2
octyl 3-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
4
octyl 4-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.565
octyl 6'-amino-6'-deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.538
octyl 6'-O-methyl-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.4
octyl alpha-L-xylo-hexopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.055
UDP-6-deoxygalactose
-
-
0.023 - 0.78
UDP-alpha-D-galactose
0.0035
UDP-Gal
-
pH 7.4, 22C
0.01 - 4.5
UDP-galactose
0.023 - 0.78
UDP-GalNAc
0.12 - 0.238
UDP-glucose
0.285 - 0.34
UDP-N-acetylgalactosamine
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-D-GlcNAcp-O(CH2)7CH3
Homo sapiens
-
37C, pH 7.0
1.2
alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O(CH2)8CO2CH3
Homo sapiens
-
37C, pH 7.0
3.5
alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3
Homo sapiens
-
37C, pH 7.0
0.15 - 8
beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
0.000004 - 5.1
UDP-D-galactose
0.37 - 0.74
UDP-Gal
0.004 - 5.4
UDP-galactose
4 - 5.1
UDP-GalNAc
0.0000167 - 0.002
UDP-glucose
0.00016 - 1.6
UDP-N-acetylgalactosamine
additional information
additional information
Homo sapiens
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.571
9-(D-1-deoxy-arabinit-1-yl)-1,3,7-trihydropurine-2,6,8-trione
-
pH 7.0, 37C
0.361
9-D-ribityl-1,3,7-trihydropurine-2,6,8-trione
-
pH 7.0, 37C
0.005
octyl 3'-amino-3'deoxy-alpha-L-fucopyranosyl-(1-2)-beta-D-galactopyranoside
-
-
0.0078 - 0.026
octyl alpha-L-fucopyranosyl-(1-2)-beta-D-gulopyranoside
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.11
1-(1-benzothiophen-3-yl)methanamine
Homo sapiens
-
pH 6.7, 37C
2.72
1-(2-chloro-6-fluorobenzyl)piperazine
Homo sapiens
-
pH 6.7, 37C
1.28
1-(3-methoxyphenyl)piperazine
Homo sapiens
-
pH 6.7, 37C
1.04
1-(3-phenyl-1,2,4-thiadiazol-5-yl)-1,4-diazepane
Homo sapiens
-
pH 6.7, 37C
0.79
1-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazine
Homo sapiens
-
pH 6.7, 37C
2.16
1-methyl-1H-benzotriazole-5-carboxylic acid
Homo sapiens
-
pH 6.7, 37C
1.56
2,3-dimethylquinoxaline-6-carboxylic acid
Homo sapiens
-
pH 6.7, 37C
0.97
7-aminothieno[2,3-b]pyrazine-6-carboxylic acid
Homo sapiens
-
pH 6.7, 37C
1.9
9-(D-1-deoxy-arabinit-1-yl)-1,3,7-trihydropurine-2,6,8-trione
Homo sapiens
-
pH 7.0, 37C
1.2
9-D-ribityl-1,3,7-trihydropurine-2,6,8-trione
Homo sapiens
-
pH 7.0, 37C
2.61
N-methyl-1-[3-(pyridin-3-yl)phenyl]methanamine
Homo sapiens
-
pH 6.7, 37C
1.61
N-methyl-1-[3-(pyridin-4-yl)phenyl]methanamine
Homo sapiens
-
pH 6.7, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
-
wild-type enzyme, with cosubstrate UDP-GalNAc
0.11
-
mutant M214G, with cosubstrate UDP-GalNAc
0.14
-
mutant M214S, with cosubstrate UDP-GalNAc
1.36
-
-
1.9
-
mutant M214S, with cosubstrate UDP-Gal
1.92
-
-
3.3
-
wild-type enzyme, with cosubstrate UDP-Gal
4.4
-
mutant M214G, with cosubstrate UDP-Gal
72
-
purified native enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4 - 7.4
-
dependent on the buffer system
6.4 - 6.8
-
in reaction with N-acetyllactosamine
6.7
-
assay at
6.8
-
in reaction with 2'-fucosyllactose
7 - 7.3
-
assay at
7 - 7.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
B-type enzyme expression in the surface epithelium
Manually annotated by BRENDA team
B-type enzyme expression
Manually annotated by BRENDA team
B-type enzyme expression in the surface epithelium
Manually annotated by BRENDA team
B-type enzyme expression
Manually annotated by BRENDA team
additional information
no B-type enzyme expression in small intestine, striated muscle, heart, liver, lung, skin, uterus, testis, lymph node, or brain
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme catalyzing the transfer of galactose to 2'-fucosyllactose is much more tightly attached to membrane than the transferase which utilizes N-acetyllactosamine
Manually annotated by BRENDA team
additional information
-
no activity in microsomes
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80000
-
gel filtration, 0.2 M NaCl added to the buffer
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 34483, recombinant truncated enzyme mutant, mass spectrometry
dimer
-
2 * 40000, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytic domain with and without H-antigen and UDP, at 1.32 and 1.65 A resolution
-
crystals of purified native enzyme are soaked with various combinations of UDP-GalNAc, UDP-Gal, UDP, and acceptor analogues alpha-L-fucosyl-1,2-beta-D-(3-deoxy)-galactosyl-O-R or alpha-L-fucosyl-1,2-beta-D-(3-amino)-galactosyl-O-R, ligands are solved in 7.5% PEG 4000, 15% glycerol, 75 mM N-[2-acetamido]-2-iminodiacetic acid, pH 7.5, 10 mM MnCl2, and 10 mM inhibitor, 3-4 days, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
enzyme soaked with acceptor analogs: galactose, lactose, N-acetyllactosamine, beta-D-Galp-O(CH2)8CO2CH3, alpha-L-Fucp-(1,2)-beta-D-Galp-O(CH2)7CH3, beta-D-Galp-(1,4)-beta-D-Glcp-OCH3, alpha-L-Fucp-(1,2)-beta-D-Galp-(1,3)-beta-D-GlcNAcp-O(CH2)7CH3, alpha-L-Fucp-(1,2)-beta-D-Galp-(1,4)-beta-D-GlcNAcp-O-(CH2)8CO2CH3
-
mutant GTB C209A is crystallized in both the presence and the absence of mercury, 0.01 ml drops containing 6-8 mg/ml GTB, 70 mM N-(2-acetamido)-2-iminodiacetic acid, pH 7.5, 50 mM sodium acetate, pH 4.6, 40 mM NaCl, 5-8 mM MnCl2, 2.5% v/v 2-methyl-2,4-pentanediol, 5% v/v glycerol, 2% w/v PEG 4000 and 0.3-0.5 mM 3-chloromercuri-2-methoxypropylurea is suspended over 1 ml reservoir solution containing 50 mM N-(2-acetamido)-2-iminodiacetic acid, pH 7.5, 10 mM, MnCl2, 100 mM ammonium sulfate, 5% v/v MPD, 10% v/v glycerol and 8-10% w/v PEG 4000. Growing crystals of native GTB in the absence of mercury using protein concentrations of 6-8 mg /ml are unsuccessful, therefore crystals of the C209A mutant are grown from protein concentrations of over 30 mg/ml with the lowest observed concentration that yielded diffraction-quality crystals being 15 mg/ml 5-8 ml drops containing 1% PEG 4000, 4.5% MPD, 0.1 M ammonium sulfate, 0.07 M NaCl, 0.05 M N-(2-acetamido)-2-iminodiacetic acid, pH 7.5, and 5 mM CoCl2 are stored at 4-6C for 3-5 days over a reservoir of 2.7% PEG 4000, 7% MPD, 0.32 M ammonium sulfate, 0.25 M NaCl and 0.2 M N-(2-acetamido)-2-iminodiacetic acid. Both sets of crystals are washed with mother liquor containing 6-7% PEG 4000, 70 mM N-(2-acetamido)-2-iminodiacetic acid, pH 7.5, 30 mM sodium acetate, pH 4.6, 40 mM ammonium sulfate, 29-30% glycerol and 9-10 mM MnCl2 or 5 mM CoCl2 for the heavy-metal derivative or native protein, respectively. X-ray diffraction structure determination and analysis at 1.8-2.4 A resolution
-
P234S-mutant, 1.55 and 1.65 A resolution, with and without H-antigen
structures of GTA, GTB and several chimeras determined by single-crystal X-ray diffraction demonstrate a range of susceptibility to the choice of cryoprotectant, in which the mobile polypeptide loops can be induced by glycerol to form the ordered closed conformation associated with substrate recognition and by MPD (hexylene glycol, 2-methyl-2,4-pentanediol) to hinder binding of substrate in the active site owing to chelation of the Mn2+ cofactor and thereby adopt the disordered open state
-
wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling; wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling; wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling; wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling; wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling; wild-type and mutant enzymes, X-ray diffraction structure determination and analysis at 1.99 A resolution, modelling
wild-type enzyme and GTA/GTB chimeric enzyme mutants GTB/G176R and GTB/G176R/G235S bound to a panel of donor and acceptor analogue substrates, hanging drop vapour diffusion method, method variantions, overview, X-ray diffraction structure determination and analysis at 1.43-1.75 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
5 min, 20% loss of activity, 20 min, 60% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1 mM EDTA and 5% v/v glycerol stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, crude extract, 25% loss of activity after 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 2400fold by 2 steps ion exchange chromatography, HI chromatography, and gel filtration to homogeneity
-
one-step procedure involving absorption onto group 0 erythrocyte membranes followed by elution with the low molecular weight H-active trisaccharide 2'-fucosyllactose
-
purified by successive ion exchange chromatography with SP sepharose FF and affinity chromatography with UDP-hexanolamine sepharose
-
recombinant enzyme from Escherichia coli by cation exchange chromatograophy, UDP-hexanolamine affinity chromatography, and dialysis
-
recombinant wild-type and mutant enzymes from Escherichia coli
-
recombinant wild-type and mutant M186V enzymes from Escherichia coli by ion exchange and UDP-hexanolamine affinity chromatography
-
using Ni-NTA chromatography
-
via ELISA
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ABO glycosyltransferase polymorphisms, phenotyping and genotyping, overview
-
catalytic domain expressed in Escherichia coli
-
DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strain BL21
-
expressed in Escherichia coli
-
expressed in Escherichia coli TG-1
-
expressed in Escherichia coli TG-1, the membrane-anchoring domain is replaced with an ompA bacterial secretory signal
-
expression of wild-type and chimeric mutant enzyme in HeLa cells
-
expression of wild-type and mutant enzymes in Escherichia coli
-
gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping; gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping; gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping; gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping; gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping; gene ABO, DNA and amino acid sequence determination and analysis of different allelic variants, blood group genotyping
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
overexpressed in Escherichia coli BL21 cells
-
overexpression in Escherichia coli strain BL21
-
overexpression of truncated GTB in Escherichia coli strain BL21
-
P234S-mutant expressed in Escherichia coli BL21
recombinantly expressed as a His-tagged fusion protein
-
transfected into HeLa cells derived from human adenocarcinoma of uterus
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
C209A
-
site-directed mutagenesis, mutant structure determination
C80S/C196S
-
both the double and triple mutants show differing levels of disorder depending on their liganded state, with the level of disorder increasing when substrates are bound.The double mutant shows disorder over residues 177-180 in the unliganded and H-antigen bound forms, with disorder increasing to residues 176-185 for the UDP-, UDP + H-, and UDP-alpha-D-galactose + 3-deoxy-Gal inactive acceptor analog-bound structures. The double mutant has a reduction in Km for both donor and acceptor substrates. Mutation shows little effect over kcat
C80S/C196S/C209S
-
both the double and triple mutants show differing levels of disorder depending on their liganded state, with the level of disorder increasing when substrates are bound.The unliganded triple mutant shows a nearly complete internal loop, with residues 176-181 disordered for the H-antigen-bound structure and 177-179 disordered for the UDP-bound structure. The UDP + H- and UDPGal + 3-deoxy-Gal inactive acceptor analog-bound structures of the triple mutant show an internal loop completely disordered over residues 176-184. The triple Cys-to-Ser mutant has an acceptor Km elevated approximately 5times over wild type, while the donor Km has doubled. Mutation shows little effect over kcat
D262N
naturally occuring mutant from individuals with weak B phenotype showing serologically weak B antigen on their red cells, overview; 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
-
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
-
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
-
saturation mutagenesis of GTB enzyme at M214 leads to a two-fold higher kcat for UDP-GalNAc and specific activity of the mutant compared to the wild-type GTB
M214R
-
mutation is adjacent to the 211DVD213 motif. 1200fold decrease in kcat compared with wild type enzyme. The crystal structure of M214R shows that DVD motif coordination to Mn2+ is disrupted by Arg214 causing displacement of the metal by a water molecule. Individuals with the M214R mutation show the Bel variant expressing very low levels of B antigens
M214S
-
saturation mutagenesis of GTB enzyme at M214 leads to a two-fold higher kcat for UDP-GalNAc and specific activity of the mutant compared to the wild-type GTB
M214T
-
mutation is adjacent to the 211DVD213 motif. The crystal structure of the M214T mutant shows no change in DVD motif coordination to Mn2+. Instead a critical residue, Met266, which is responsible for determining donor specificity, has adopted alternate conformations. The conformation with the highest occupancy opens up the active site to accommodate the larger A-specific donor, UDP-GalNAc, accounting for the dual specificity. Individuals with M214T mutation give rise to AweakB phenotype
M214V
-
mutation is adjacent to the 211DVD213 motif. Individuals with M214T mutation give rise to AweakB phenotype
P234S
dramatic and complete reversal of donor specificity, it preferentially utilizes UDP-GalNac for transfer
R188H
-
site-directed mutagenesis, the mutant shows affected substrate binding
R188K
-
site-directed mutagenesis, the mutant shows affected substrate binding
S185C
-
mutant enzyme exhibits 4.8fold elevations in kcat/Km for UDP-glucose relative to that of wild-type enzyme
S185D
-
activity with UDP-galactose is 0.09% of wild-type activity
S185E
-
activity with UDP-galactose is 0.04% of wild-type activity
S185N
-
mutant enzyme exhibits 4.3fold elevations in kcat/Km for UDP-glucose relative to that of wild-type enzyme
additional information