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Information on EC 2.4.1.87 - N-acetyllactosaminide 3-alpha-galactosyltransferase
for references in articles please use BRENDA:EC2.4.1.87
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.87 N-acetyllactosaminide 3-alpha-galactosyltransferase
IUBMB Comments
Acts on β-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-α1-acid glycoprotein and N-acetyllactosamine (β-D-galactosyl-1,4-N-acetyl-β-D-glucosamine), but not on 2′-fucosylated-N-acetyllactosamine. The non-reducing terminal N-acetyllactosamine residues of glycoproteins can also act as acceptor. Now includes EC 2.4.1.124 and EC 2.4.1.151.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 2.4.1.87
- epitope
-
rejection
-
xenotransplantation
- porcine
-
hyperacute
- primates
-
anti-gal
- glycosyltransferases
-
gene-knockout
-
xenoantigens
-
xenogeneic
- baboon
-
pig-to-human
-
galalpha1,3gal
-
alphagal
-
galalpha1-3galbeta1-4glcnac-r
-
galt-ko
-
xenoreactive
-
alpha-galactosylated
-
pig-to-primate
-
non-gal
-
anti-alphagal
-
b4galnt2
-
forssman
-
xenoantibodies
-
decay-accelerating
- simplicifolia
-
anti-pig
-
alpha1,2-fucosyltransferase
-
pig-to-baboon
-
n-glycolylneuraminic
- neu5gc
- medicine
- diagnostics
- synthesis
Reaction Schemes
showSynonyms
ggta1, alpha1,3-galactosyltransferase, alpha1,3gt, alpha-1,3-galactosyltransferase, alpha-galactosyltransferase, alpha1,3galactosyltransferase, igb3s, alpha3gt, alpha1,3galt, igb3 synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha(1,3)GT
-
two independent genes encode glycosyltransferases that synthesize Galalpha(1,3)Gal by two separate glycosylation pathways, alpha(1,3)GT and iGb3 synthase
alpha-1,3-galactosyltransferase
alpha-galactosyltransferase
-
-
-
-
alpha1,3-galactosyltransferase
alpha1,3GT
alpha3-galactosyltransferase
alpha3GalT
alpha3GT
beta-D-galactosyl-N-acetylglucosaminylglycopeptide alpha-1,3-galactosyltransferase
-
-
-
-
EC 2.4.1.124
-
-
formerly
-
EC 2.4.1.151
-
-
formerly
-
galactosyltransferase, uridine diphosphogalactose-acetyllactosamine
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-acetyllactosamine alpha1-->3-
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-galactosylacetylglucosamine alpha-1,3-
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-galactosylacetylglucosaminylgalactosylglucosylceramide
-
-
-
-
GGTA1
glucosaminylglycopeptide alpha-1,3-galactosyltransferase
-
-
-
-
iGb3 synthase
-
two independent genes encode glycosyltransferases that synthesize Galalpha(1,3)Gal by two separate glycosylation pathways, alpha(1,3)GT and iGb3 synthase
N-acetyllactoseaminide 3-alpha-D-galactosyltransferase
-
-
-
-
one, three-galactosyltransferase
Otg1p
Otg2p
Otg3p
UDP-D-Gal(1,4)-D-GlcNAc alpha(1,3)-galactosyltransferase
-
-
-
-
UDP-Gal:N-acetyllactoseaminide alpha(1,3)-galactosyltransferase
-
-
-
-
UDP-galactose-acetyllactosamine alpha-D-galactosyltransferase
-
-
-
-
UDP-galactose-acetyllactoseamine alpha-D-galactosyltransferase
-
-
-
-
UDP-galactose:beta-D-galactosyl-beta-1,4-N-acetyl-D-glucosaminyl-glycopeptide alpha-1,3-D-galactosyltransferase
-
-
-
-
UDP-galactose:N-acetyllactoseaminide 3-alpha-D-galactosyltransferase
-
-
-
-
UDP-GalN-acetyllactoseaminide alpha-1,3-D-UDP-GalGalbeta1-->4GlcNAC-R alpha1-->3-galactosyltransferase
-
-
-
-
UDPgalactose:beta-D-galactosyl-beta-1,4-N-acetyl-D-glucosaminyl-glycopeptide alpha-1,3-D-galactosyltransferase
-
-
-
-
uridine diphosphogalactose-acetyllactosamine alpha1-->3-galactosyltransferase
-
-
-
-
uridine diphosphogalactose-galactosylacetylglucosaminylgalactosylglucosylceramide galactosyltransferase
-
-
-
-
wclR
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R (where R can be OH, an oligosaccharide or a glycoconjugate)
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R (where R can be OH, an oligosaccharide or a glycoconjugate)
structure-function relationship
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R (where R can be OH, an oligosaccharide or a glycoconjugate)
acts on beta-galactosyl-1,4-N-acetylglucosylaminyl termini on asialo-alpha1-acid glycoprotein and N-acetyllactosamine (beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine), but not on 2'-fucosylated-N-acetyllactosamine. The non-reducing terminal N-acetyllactosamine residues of glycoproteins can also act as acceptor
-
-
-
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R (where R can be OH, an oligosaccharide or a glycoconjugate)
where R can be OH, an oligosaccharide or a glycoconjugate
-
-
-
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R (where R can be OH, an oligosaccharide or a glycoconjugate)
E317 is not the catalytic nucleophile proposed in the double-displacement mechanism. Either a different amino acid may act as the catalytic nucleophile or the reaction must proceed by a different mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
terminal O-glycans residues modification (via type 2 precursor disaccharide)
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SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R 3-alpha-D-galactosyltransferase
Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on asialo-alpha1-acid glycoprotein and N-acetyllactosamine (beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosamine), but not on 2'-fucosylated-N-acetyllactosamine. The non-reducing terminal N-acetyllactosamine residues of glycoproteins can also act as acceptor. Now includes EC 2.4.1.124 and EC 2.4.1.151.
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CAS REGISTRY NUMBER
COMMENTARY
128449-51-4
-
306996-46-3
EC 2.4.1.87, formerly
78642-28-1
EC 2.4.1.124, EC 2.4.1.151, formerly
96477-57-5
EC 2.4.1.151, formerly
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4 UDP-alpha-D-galactose + Galbeta(1-4)GlcNAcbeta(1-3)(Galbeta(1-4)GlcNAcbeta(1-6))Galbeta(1-4)GlcNAcbeta(1-3)[Galbeta(1-4)GlcNAcbeta(1-3)(Galbeta(1-4)GlcNAc(1-6)Galbeta(1-4)GlcNAcbeta(1-6))]Galbeta(1-4)GlcNAc
4 UDP + Galalpha(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(Galalpha(1-3)Galbeta(1-4)GlcNAcbeta(1-6))Galbeta(1-4)GlcNAcbeta(1-3)[Galalpha(1-3)Galbeta(1-4)GlcNAcbeta(1-3)(Galalpha(1-3)Galbeta(1-4)GlcNAc(1-6))Galbeta(1-4)GlcNAcbeta(1-6)]Galbeta(1-4)GlcNAc
-
Substrates: -
Products: -
Products: -
?
UDP-2-acetonyl-2-deoxy-galactose + asialofetuin
UDP + ?
Substrates: mutant enzymes SGG and AGG, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
Products: -
Products: -
?
UDP-2-acetonyl-2-deoxy-galactose + N-acetyllactosaminyl-chitotriose
UDP + ?
Substrates: mutant enzymes SGG, AGG, and TGG, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
UDP-alpha-D-galactose + Galbeta(1-4)GlcNAcbeta(1-2)Man(1-3)Manbeta(1-4)GlcNAc
UDP + alpha-D-galactosyl-1,3-Galbeta(1-4)GlcNAcbeta(1-2)Man(1-3)Manbeta(1-4)GlcNAc
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + Glcalpha-diphospho-O(CH2)10CH3
UDP + Galalpha(1->3)Glcalpha-diphospho-O(CH2)10CH3
-
Substrates: wciN encodes an alpha-1,3-galactosyltransferase catalyzing the transfer of galactosyl from UDP-Gal onto the Glcalpha-diphosphate-lipid acceptor to form Galalpha(1->3)Glcalpha-diphosphate-lipid
Products: -
Products: -
?
UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosamine-diphospho-O-(CH2)9CH3
UDP + alpha-D-galactosyl-(1->3)-N-acetyl-alpha-D-glucosamine-diphospho-O-(CH2)9CH3
UDP-Gal + Gal-beta-1,4-GlcNAc-(CH2)8CO2CH3
UDP + ?
Substrates: -
Products: -
Products: -
?
UDP-galactose + alpha-L-Fucp-1,2-beta-D-Galp-O(CH2)7CH3
UDP + ?
-
Substrates: The presence of UDP and Mn2+ has a marked influence on the thermodynamic parameters enthalpy and entropy of association, they decrease, binding to substrate is independent of UDP at physiological temperatures, but cooperatively is observed at lower temperatures
Products: -
Products: -
?
UDP-galactose + asialo-alpha1-acid glycoprotein
UDP + alpha-D-galactosyl-asialo-alpha1-acid glycoprotein
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + asialofetuin
UDP + alpha-D-galactosylasialofetuin
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-Gal(1-3)beta-D-GlcNAc(1-3)beta-D-Gal(1-4)-D-Glc
UDP + alpha-D-Gal(1-3)beta-D-Gal(1-3)beta-D-GlcNAc(1-3)beta-D-Gal(1-4)-D-Glc
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-Gal(1-4)-D-GlcNAc(1-2)-[beta-D-Gal(1-4)beta-D-GlcNAc(1-6)]-D-Man
?
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-Gal(1-4)beta-D-GlcNAc(1-2)-D-Man
UDP + alpha-D-Gal(1-3)beta-D-Gal(1-4)beta-D-GlcNAc(1-2)-D-Man
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-Gal(1-4)beta-D-GlcNAc(1-6)-D-Man
UDP + alpha-D-Gal(1-3)beta-D-Gal(1-4)beta-D-GlcNAc(1-6)-D-Man
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-Gal(1-4)GlcNAcbeta(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
UDP + alpha-D-Gal(1-3)beta-D-Gal(1-4)GlcNAcbeta(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-D-glucose
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-D-glucose
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP-galactose + D-galactose
UDP + alpha-D-galactosyl-1,3-D-galactoside
Substrates: -
Products: -
Products: -
?
UDP-galactose + galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide
UDP + O-alpha-galactosyl-1,3-galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide
-
Substrates: biosynthesis of blood group B specific pentaglycosylceramide
Products: -
Products: -
?
UDP-galactose + galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide
UDP + O-alpha-galactosyl-1,3-galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide + O-alpha-galactosyl-1,4-galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide
-
Substrates: specific for UDP-galactose as donor substrate
Products: -
Products: -
?
UDP-galactose + galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide
UDP + O-alpha-galactosyl-1,4-galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide
-
Substrates: biosynthesis of blood group B specific pentaglycosylceramide
Products: -
Products: -
?
UDP-galactose + lactose
UDP + alpha-D-galactosyl-(1-3)-beta-D-galactosyl-(1-4)-beta-D-glucose
UDP-galactose + lactose
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
UDP-galactose + Manalpha(1->2)Manalpha(1->2)Man-pyridylamine
UDP + Galalpha(1->3)Manalpha(1->2)Manalpha(1->2)Man-pyridylamine
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
UDP-galactose + p-nitrophenyl-alpha-D-galactoside
UDP + ?
Substrates: -
Products: -
Products: -
?
UDP-galactose + p-nitrophenyl-beta-D-galactoside
UDP + ?
Substrates: -
Products: -
Products: -
?
UDP-galactose + saccharides containing Galalpha(1-3)Gal epitope
?
AF415202
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-azido-galactosamine + N-acetyllactosaminyl-chitotriose
UDP + ?
Substrates: mutant enzymes SGG, AGG, and TGG, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
Products: -
Products: -
?
UDP-N-acetylgalactosamine + N-acetyllactosamine
UDP + ?
Substrates: no reaction of wild-type, only of AGGL mutant
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosamine-diphospho-O-(CH2)9CH3
UDP + alpha-D-galactosyl-(1->3)-N-acetyl-alpha-D-glucosamine-diphospho-O-(CH2)9CH3
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + N-acetyl-alpha-D-glucosamine-diphospho-O-(CH2)9CH3
UDP + alpha-D-galactosyl-(1->3)-N-acetyl-alpha-D-glucosamine-diphospho-O-(CH2)9CH3
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + N-acetyllactosamine
UDP + ?
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: enzyme introduces galactosyl residues in alpha anomeric configuration to the Galbeta(1-4)GlcNAc units on the acceptor substrate
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: highly active with glycoproteins, oligosaccharides and glycolipids having a terminal Galbeta(1-4)GlcNAcbeta(1-2)Manalpha(1-3)Manbeta(1-4)GlcNAc and paragloboside
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: not: alpha-L-Fuc(1-2)beta-D-Gal(1-4)-D-GlcNAc
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
Substrates: R = glycoprotein or glycolipid
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: beta-D-Gal(1-4)-[alpha-L-Fuc(1-3)]-D-GlcNAc
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: very poor acceptor: lactose, beta-D-Gal(1-3)-D-GlcNAc
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: acts preferentially on the alpha-D-Man(1,6) arm, this branch is preferred 2.5times in bi-, 5.5-8.5times in tri-, and 12.7times in tetraantennary structures over the alpha-D-Man(1-3) arm, within the alpha-D-Man(1-6) branch there is a 1.3-1.9fold consistently higher frequency of galactosylation of the beta-D-GlcNAc(1-2) as compared to the beta-D-GlcNAc(1-6) antenna
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: the most active acceptors have the structure beta-D-Gal(1-4)beta-D-GlcNAc(1-) at their nonreducing termini
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
Substrates: gene expression is regulated developmentally
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: alpha(1,3)GT is able to synthesize Galalpha(1,3)Gal on glycoproteins destined for the cell surface. Igb3S shows no activity with glycoproteins but is capable of synthesizing Galalpha(1,3)Gal on glycolipids
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
Substrates: -
Products: -
Products: -
?
UDP-galactose + glycoprotein
UDP + alpha-D-galactosylglycoprotein
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + glycoprotein
UDP + alpha-D-galactosylglycoprotein
-
Substrates: the nonreducing terminal N-acetyllactosamine residue of glycoproteins can act as acceptor
Products: -
Products: -
?
UDP-galactose + glycoprotein
UDP + alpha-D-galactosylglycoprotein
-
Substrates: the nonreducing terminal N-acetyllactosamine residue of glycoproteins can act as acceptor
Products: -
Products: -
?
UDP-galactose + lactose
UDP + ?
Substrates: wild-type enzyme, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
Products: -
Products: -
?
UDP-galactose + lactose
UDP + ?
Substrates: wild-type enzyme, and mutant enzymes AAA, GAG, AGG, SGG, TGG, LGG, VGG, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
Products: -
Products: -
?
UDP-galactose + lactose
UDP + alpha-D-galactosyl-(1-3)-beta-D-galactosyl-(1-4)-beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + lactose
UDP + alpha-D-galactosyl-(1-3)-beta-D-galactosyl-(1-4)-beta-D-glucose
Substrates: -
Products: -
Products: -
?
UDP-galactose + lactose
UDP + alpha-D-galactosyl-(1-3)-beta-D-galactosyl-(1-4)-beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + lactose
UDP + alpha-D-galactosyl-(1-3)-beta-D-galactosyl-(1-4)-beta-D-glucose
-
Substrates: very poor acceptor
Products: -
Products: -
?
UDP-galactose + lactose
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
Substrates: -
Products: -
Products: -
?
UDP-galactose + lactose
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-D-glucose
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + Manalpha(1->2)Manalpha(1->2)Man-pyridylamine
UDP + Galalpha(1->3)Manalpha(1->2)Manalpha(1->2)Man-pyridylamine
-
Substrates: substrate for isoform Otg2p
Products: -
Products: -
?
UDP-galactose + Manalpha(1->2)Manalpha(1->2)Man-pyridylamine
UDP + Galalpha(1->3)Manalpha(1->2)Manalpha(1->2)Man-pyridylamine
-
Substrates: substrate for isoform Otg2p
Products: -
Products: -
?
UDP-galactose + N-acetyllactosamine
UDP + ?
Substrates: -
Products: -
Products: -
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
Substrates: i.e. beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
Products: -
Products: -
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
Substrates: i.e. beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
Products: -
Products: -
ir
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
Substrates: i.e. beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
Products: -
Products: -
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
Substrates: oligosaccharides, glycoproteins and glycosaminoglycans containing the terminal nonreducing N-acetyllactosamine unit all serve as acceptors
Products: -
Products: -
?
UDP-galactose + substituted LacNAc-saccharides containing Galalpha(1-3)Gal epitope
?
-
Substrates: acceptor substrate substrate specificity, overview
Products: -
Products: -
?
UDP-galactose + substituted LacNAc-saccharides containing Galalpha(1-3)Gal epitope
?
-
Substrates: strictly specific for UDP-galactose
Products: -
Products: -
?
UDP-N-acetylgalactosamine + lactose
UDP + ?
Substrates: no reaction of wild-type, only of AGGL mutant
Products: -
Products: -
?
UDP-N-acetylgalactosamine + lactose
UDP + ?
Substrates: mutant enzymes AAA, GAG, AGG, SGG, TGG, LGG, VGG, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
Products: -
Products: -
?
additional information
?
-
-
Substrates: acceptor substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: acceptor substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: product analysis with H-NMR spectroscopy
Products: -
Products: -
?
additional information
?
-
-
Substrates: functions in the biosynthesis of calf thymocyte cell-surface glycoconjugates including glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: functions in biosynthesis of calf thymocyte cell-surface glycoconjugates including glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: structural basis of UDP-galactose binding at the catalytic domain of alpha3GT, overview
Products: -
Products: -
?
additional information
?
-
Substrates: structural basis of UDP-galactose binding at the catalytic domain of alpha3GT, overview
Products: -
Products: -
?
additional information
?
-
Substrates: no donors: UDP-Glc, UDP-GlcNAc, UDPGalNAc, CMP-Neu and GDP-Man
Products: -
Products: -
?
additional information
?
-
Substrates: no donors: UDP-Glc, UDP-GlcNAc, UDPGalNAc, CMP-Neu and GDP-Man
Products: -
Products: -
?
additional information
?
-
-
Substrates: acceptor substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: acceptor substrate specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: specificity, most active acceptors have the structure beta-D-Gal-(1-4)-beta-D-GlcNAc(1-4) at their nonreducing termini
Products: -
Products: -
?
additional information
?
-
-
Substrates: synthesis of Ehrlich ascites tumor cell glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the biosynthesis of alpha-D-galactosyl-terminated poly-N-acetyllactosamine glycans that occur on the surface of Ehrlich ascites tumor cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: iGb3S is an additional enzyme capable of synthesizing the xenoreactive Galalpha(1,3)Gal epitope. Galalpha(1,3)Gal synthesized by iGb3S, in contrast to alpha1,3GT, is resistant to downregulation by competition with alpha1,2fucosyltransferase. Galalpha(1,3)Gal synthesized by iGb3S is immunogenic and elicits antibodies in GGTA1-/- mice. Galalpha(1,3)Gal synthesized by iGb3S may affect survival of pig transplants in humans
Products: -
Products: -
?
additional information
?
-
-
Substrates: functions in the biosynthesis of cell surface polylactosaminoglycans on Novikoff cells, attachs a galactose to the N-acetylglucosaminyl residue introduced by EC 2.4.1.149
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform Otg1p is inactive towards Man9GlcNAc2-pyridylamine and Manalpha(1->2)Manalpha(1->2)Man-pyridylamine. Isoforms Otg1p, Otg2p and Otg3p are inactive toward Man-pyridylamine, Manalpha(1->2)Man-pyridylamine, and Galalpha(1->2)Man-pyridylamine as acceptor substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: isoform Otg1p is inactive towards Man9GlcNAc2-pyridylamine and Manalpha(1->2)Manalpha(1->2)Man-pyridylamine. Isoforms Otg1p, Otg2p and Otg3p are inactive toward Man-pyridylamine, Manalpha(1->2)Man-pyridylamine, and Galalpha(1->2)Man-pyridylamine as acceptor substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity towards GlcNAcalpha-diphospho-O-(CH2)10CH3, UDP-D-glucose, Glcalpha-monophosphate, 4-nitrophenyl alpha-D-glucopyranoside, Glcalpha(1->2)Glc, Glcalpha-OMe, and Glcbeta-OMe
Products: -
Products: -
?
additional information
?
-
AF415202
Substrates: the alphaGal(1-3)Gal epitope is the major xenoantigen responsible for the hyperacute vascular rejection occurring in pig-to-primate organ transplantation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the alphaGal(1-3)Gal epitope is the major xenoantigen responsible for the hyperacute vascular rejection occurring in pig-to-primate organ transplantation
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
UDP-galactose + alpha-L-Fucp-1,2-beta-D-Galp-O(CH2)7CH3
UDP + ?
-
Substrates: The presence of UDP and Mn2+ has a marked influence on the thermodynamic parameters enthalpy and entropy of association, they decrease, binding to substrate is independent of UDP at physiological temperatures, but cooperatively is observed at lower temperatures
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP-galactose + galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide
UDP + O-alpha-galactosyl-1,3-galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide
-
Substrates: biosynthesis of blood group B specific pentaglycosylceramide
Products: -
Products: -
?
UDP-galactose + galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide
UDP + O-alpha-galactosyl-1,4-galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide
-
Substrates: biosynthesis of blood group B specific pentaglycosylceramide
Products: -
Products: -
?
UDP-galactose + lactose
UDP + ?
Substrates: wild-type enzyme, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-alpha-D-galactose + N-acetyllactosamine
UDP + ?
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: -
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
Substrates: gene expression is regulated developmentally
Products: -
Products: -
?
UDP-galactose + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R
-
Substrates: alpha(1,3)GT is able to synthesize Galalpha(1,3)Gal on glycoproteins destined for the cell surface. Igb3S shows no activity with glycoproteins but is capable of synthesizing Galalpha(1,3)Gal on glycolipids
Products: -
Products: -
?
additional information
?
-
-
Substrates: functions in the biosynthesis of calf thymocyte cell-surface glycoconjugates including glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: functions in biosynthesis of calf thymocyte cell-surface glycoconjugates including glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: synthesis of Ehrlich ascites tumor cell glycoproteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the biosynthesis of alpha-D-galactosyl-terminated poly-N-acetyllactosamine glycans that occur on the surface of Ehrlich ascites tumor cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: iGb3S is an additional enzyme capable of synthesizing the xenoreactive Galalpha(1,3)Gal epitope. Galalpha(1,3)Gal synthesized by iGb3S, in contrast to alpha1,3GT, is resistant to downregulation by competition with alpha1,2fucosyltransferase. Galalpha(1,3)Gal synthesized by iGb3S is immunogenic and elicits antibodies in GGTA1-/- mice. Galalpha(1,3)Gal synthesized by iGb3S may affect survival of pig transplants in humans
Products: -
Products: -
?
additional information
?
-
-
Substrates: functions in the biosynthesis of cell surface polylactosaminoglycans on Novikoff cells, attachs a galactose to the N-acetylglucosaminyl residue introduced by EC 2.4.1.149
Products: -
Products: -
?
additional information
?
-
AF415202
Substrates: the alphaGal(1-3)Gal epitope is the major xenoantigen responsible for the hyperacute vascular rejection occurring in pig-to-primate organ transplantation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the alphaGal(1-3)Gal epitope is the major xenoantigen responsible for the hyperacute vascular rejection occurring in pig-to-primate organ transplantation
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
MnCl2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
octyl 3-amino-3-deoxy-3-N-(2-diazo-3,3,3-trifluoropropionyl-beta-D-galactopyranosyl-(1,4)-2-acetamido-2-deoxy-beta-D-glucopyranoside)
-
i.e. DTFP-LacNAc-C8
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Designing a HER2/neu promoter to drive alpha1,3galactosyltransferase expression for targeted anti-alphaGal antibody-mediated tumor cell killing.
Carcinogenesis
Enzymatic basis for changes in fucoganglioside during chemical carcinogenesis. Induction of a specific alpha-fucosyltransferase and status of an alpha-galactosyltransferase in precancerous rat liver and hepatoma.
Carcinoma, Ehrlich Tumor
An alpha-D-galactosyltransferase activity in Ehrlich ascites tumor cells. Biosynthesis and characterization of a trisaccharide (alpha-D-galactose-(1 goes to 3)-N-acetyllactosamine).
Carcinoma, Embryonal
Transcriptional regulation of alpha1,3-galactosyltransferase in embryonal carcinoma cells by retinoic acid. Masking of Lewis X antigens by alpha-galactosylation.
Carcinoma, Hepatocellular
Enzymatic basis for changes in fucoganglioside during chemical carcinogenesis. Induction of a specific alpha-fucosyltransferase and status of an alpha-galactosyltransferase in precancerous rat liver and hepatoma.
Lymphoma
Anti-Gal-mediated targeting of human B lymphoma cells to antigen-presenting cells: a potential method for immunotherapy using autologous tumor cells.
Lymphoma
Enzymatic and organizational difference in expression of a Burkitt lymphoma-associated antigen (globotriaosylceramide) in Burkitt lymphoma and lymphoblastoid cell lines.
Melanoma
Eliciting hyperacute xenograft response to treat human cancer: alpha(1,3) galactosyltransferase gene therapy.
Melanoma
In vivo targeting of vaccinating tumor cells to antigen-presenting cells by a gene therapy method with adenovirus containing the alpha1,3galactosyltransferase gene.
Melanoma
Increased immunogenicity of tumor vaccines complexed with anti-Gal: studies in knockout mice for alpha1,3galactosyltransferase.
Melanoma
Increased immunogenicity of tumor-associated antigen, mucin 1, engineered to express alpha-gal epitopes: a novel approach to immunotherapy in pancreatic cancer.
Melanoma
Reduction of metastatic properties of BL6 melanoma cells expressing terminal fucose(alpha)1-2-galactose after alpha1,2-fucosyltransferase cDNA transfection.
Melanoma, Experimental
Intratumoral injection of alpha-gal glycolipids induces xenograft-like destruction and conversion of lesions into endogenous vaccines.
Neoplasms
An alpha-D-galactosyltransferase activity in Ehrlich ascites tumor cells. Biosynthesis and characterization of a trisaccharide (alpha-D-galactose-(1 goes to 3)-N-acetyllactosamine).
Neoplasms
Autologous tumor vaccines processed to express alpha-gal epitopes: a practical approach to immunotherapy in cancer.
Neoplasms
Designing a HER2/neu promoter to drive alpha1,3galactosyltransferase expression for targeted anti-alphaGal antibody-mediated tumor cell killing.
Neoplasms
Eliciting hyperacute xenograft response to treat human cancer: alpha(1,3) galactosyltransferase gene therapy.
Neoplasms
Human TNF-related apoptosis-inducing ligand-expressing dendritic cells from transgenic pigs attenuate human xenogeneic T cell responses.
Neoplasms
In vivo targeting of vaccinating tumor cells to antigen-presenting cells by a gene therapy method with adenovirus containing the alpha1,3galactosyltransferase gene.
Neoplasms
Increased immunogenicity of tumor vaccines complexed with anti-Gal: studies in knockout mice for alpha1,3galactosyltransferase.
Neoplasms
Intratumoral injection of alpha-gal glycolipids induces xenograft-like destruction and conversion of lesions into endogenous vaccines.
Neoplasms
Regulation of alpha1,3galactosyltransferase expression in pig endothelial cells. Implications for xenotransplantation.
Neoplasms
Synthesis of alpha-gal epitopes (Galalpha1-3Galbeta1-4GlcNAc-R) on human tumor cells by recombinant alpha1,3galactosyltransferase produced in Pichia pastoris.
Neoplasms
The alpha-gal epitope and the anti-Gal antibody in xenotransplantation and in cancer immunotherapy.
Pancreatic Neoplasms
Decrease of human pancreatic cancer cell tumorigenicity by alpha1,3galactosyltransferase gene transfer.
Pancreatic Neoplasms
Relationship between alphaGal epitope expression and decrease of tumorigenicity in pancreatic adenocarcinoma model.
Pheochromocytoma
UDP-galactose:globotriaosylceramide alpha-galactosyltransferase activity in rat pheochromocytoma (PC12h) cells.
Sepsis
Loss of ?-gal during primate evolution enhanced antibody-effector function and resistance to bacterial sepsis.
Teratocarcinoma
Transcriptional regulation of alpha1,3-galactosyltransferase in embryonal carcinoma cells by retinoic acid. Masking of Lewis X antigens by alpha-galactosylation.
Thrombotic Microangiopathies
Potential of aspirin to inhibit thrombotic microangiopathy in alpha1,3-galactosyltransferase gene-knockout pig hearts after transplantation in baboons.
Thrombotic Microangiopathies
The innate immune response and activation of coagulation in alpha1,3-galactosyltransferase gene-knockout xenograft recipients.
Thrombotic Microangiopathies
Thrombotic microangiopathy associated with humoral rejection of cardiac xenografts from alpha1,3-galactosyltransferase gene-knockout pigs in baboons.
Trypanosomiasis, African
Specific inhibition of an alpha-galactosyltransferase from Trypanosoma brucei by synthetic substrate analogues.
Venous Thromboembolism
ABO blood group, glycosyltransferase activity and risk of venous thromboembolism.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.67
galactosyl-1,3-N-acetylglucosaminyl-1,3-galactosyl-1,4-glucosyl-1,1-ceramide
-
-
4.5
lactose
wild-type kb, UDP-galactose as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
180
lactose
mutant SGG kb, UDP-galactose as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
258
lactose
mutant AGG kb, UDP-N-acetylgalactosamine as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
330
lactose
mutant SGG kb, UDP-N-acetylgalactosamine as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.004
UDP-galactose
mutant AGG kia, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.014
UDP-galactose
mutant SGG kia, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.042
UDP-galactose
mutant AGG ka, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.07
UDP-galactose
mutant SGG ka, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.13
UDP-galactose
37°C, mutant enzyme E317Q, galactosyltransferase reaction
0.13
UDP-galactose
wild-type kia, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.66
UDP-galactose
37°C, mutant enzyme Q247E, galactosyltransferase reaction
0.72
UDP-galactose
37°C, mutant enzyme R365K, galactosyltransferase reaction
0.74
UDP-galactose
wild-type kib, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.79
UDP-galactose
wild-type ka, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
1.02
UDP-galactose
37°C, mutant enzyme H280Q, galactosyltransferase reaction
25.7
UDP-galactose
mutant AGG kib, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
36
UDP-galactose
mutant SGG kib, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
270
UDP-galactose
mutant AGG kb, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.068
UDP-N-acetylgalactosamine
mutant AGG kia, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.101
UDP-N-acetylgalactosamine
mutant SGG kia, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.5
UDP-N-acetylgalactosamine
mutant AGG ka, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.64
UDP-N-acetylgalactosamine
AGGL mutant, N-acetyllactosamine, pH 6, 30°C
0.74
UDP-N-acetylgalactosamine
mutant SGG ka, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
36.1
UDP-N-acetylgalactosamine
mutant AGG kib, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
45.8
UDP-N-acetylgalactosamine
mutant SGG kib, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
additional information
-
Km-values for substituted LacNAc-saccharides containing Galalpha(1-3)Gal epitope
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
UDP-galactose
mutant AGG, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.1
UDP-galactose
mutant SGG, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.14
UDP-galactose
37°C, mutant enzyme Q247E, galactosyltransferase reaction
0.17
UDP-galactose
37°C, mutant enzyme R365K, galactosyltransferase reaction
0.77
UDP-galactose
37°C, mutant enzyme H280Q, galactosyltransferase reaction
3.4
UDP-galactose
wild-type, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.045
UDP-N-acetylgalactosamine
AGGL mutant, N-acetyllactosamine, pH 6, 30°C
0.3
UDP-N-acetylgalactosamine
mutant AGG, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.4
UDP-N-acetylgalactosamine
mutant SGG, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000074
lactose
mutant AGG kcat/kb, UDP-galactose as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.00055
lactose
mutant SGG kcat/kb, UDP-galactose as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.0007
lactose
mutant SGG kcat/kb, UDP-N-acetylgalactosamine as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.0011
lactose
mutant AGG kcat/kb, UDP-N-acetylgalactosamine as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.75
lactose
wild-type kcat/kb, UDP-galactose as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.5
UDP-galactose
mutant AGG kcat/ka, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
1.4
UDP-galactose
mutant SGG kcat/ka, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
4.3
UDP-galactose
wild-type kcat/ka, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.5
UDP-N-acetylgalactosamine
mutant SGG kcat/ka, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
0.6
UDP-N-acetylgalactosamine
mutant AGG kcat/ka, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
octyl 3-amino-3-deoxy-3-N-(2-diazo-3,3,3-trifluoropropionyl-beta-D-galactopyranosyl-(1,4)-2-acetamido-2-deoxy-beta-D-glucopyranoside)
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.1
wild-type, UDP-galactose as donor, lactose as acceptor, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
additional information
relative activity: 100% wild-type, 0.1% mutant E317A, 0.4% mutant E317D, 0.8% mutant E317C, 0.1% mutant E317H
additional information
-
relative activity: 100% wild-type, 0.1% mutant E317A, 0.4% mutant E317D, 0.8% mutant E317C, 0.1% mutant E317H
additional information
mutant AAA, 20 or 200 mM lactose as acceptor, 14 and 41% galactosyltransferase activity (UDP-galactose as donor), 4 and 6% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
-
mutant AAA, 20 or 200 mM lactose as acceptor, 14 and 41% galactosyltransferase activity (UDP-galactose as donor), 4 and 6% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
mutant GAG, 20 or 200 mM lactose as acceptor, 5 and 27% galactosyltransferase activity (UDP-galactose as donor), 4 and 6% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
-
mutant GAG, 20 or 200 mM lactose as acceptor, 5 and 27% galactosyltransferase activity (UDP-galactose as donor), 4 and 6% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
mutant AGG, 20 or 200 mM lactose as acceptor, 0.4 and 1% galactosyltransferase activity (UDP-galactose as donor), 0.3 and 2% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
-
mutant AGG, 20 or 200 mM lactose as acceptor, 0.4 and 1% galactosyltransferase activity (UDP-galactose as donor), 0.3 and 2% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
mutant SGG, 20 or 200 mM lactose as acceptor, 5 and 5% galactosyltransferase activity (UDP-galactose as donor), 2 and 11% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
-
mutant SGG, 20 or 200 mM lactose as acceptor, 5 and 5% galactosyltransferase activity (UDP-galactose as donor), 2 and 11% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
mutant TGG, 20 or 200 mM lactose as acceptor, 3 and 15% galactosyltransferase activity (UDP-galactose as donor), 1 and 6% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
-
mutant TGG, 20 or 200 mM lactose as acceptor, 3 and 15% galactosyltransferase activity (UDP-galactose as donor), 1 and 6% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
mutant LGG, 20 or 200 mM lactose as acceptor, 2 and 1% galactosyltransferase activity (UDP-galactose as donor), 3 and 2% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
-
mutant LGG, 20 or 200 mM lactose as acceptor, 2 and 1% galactosyltransferase activity (UDP-galactose as donor), 3 and 2% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
mutant VGG, 20 or 200 mM lactose as acceptor, 4 and 16% galactosyltransferase activity (UDP-galactose as donor), 0.5 and 3% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
additional information
-
mutant VGG, 20 or 200 mM lactose as acceptor, 4 and 16% galactosyltransferase activity (UDP-galactose as donor), 0.5 and 3% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3 - 7
-
pH 5.3: about 45% of activity maximum, pH 7.0: about 30% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
old world monkeys evolved into large populations of diverse species only during the late Miocene and subsequent periods, gene GGTA1 encoding an inactivated enzyme
-
-
brenda
new world monkey, gene GGTA1 encoding an active enzyme
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
absence of galactose-alpha-1,3-galactose residue in the GalT-KO pig cells results in a higher level of overall fucosylated N-glycans in GalT-KO pig fibroblasts compared to wild-type pig fibroblasts, the relative quantity of the N-glycolylneuraminic acid antigen is also slightly higher in the GalT-KO pigs, mutant phenotype, overview
metabolism
physiological function
-
the wciN gene encodes a galactosyltransferase involved in the repeating unit assembly of Pneumococcus type 6B capsular polysaccharide
additional information
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope
evolution
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope. Phylogenetic analysis
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope. Phylogenetic analysis
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope. Phylogenetic analysis
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope. Phylogenetic analysis
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope. Phylogenetic analysis
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope. Phylogenetic analysis
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope. Phylogenetic analysis
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope. Phylogenetic analysis
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope. Phylogenetic analysis
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope. Phylogenetic analysis
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope. Phylogenetic analysis
evolution
-
the enzyme is a family 6 glycosyltransferase, family members have a nucleophilic residue (Glu317) situated close to the anomeric carbon
evolution
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope
evolution
-
alpha1,3-galactosyltransferase gene displays unique evolutionary characteristics. This gene appeared early in mammalian evolution and is absent in other vertebrates. The alpha1,3GT gene is active in marsupials, nonprimate placental mammals, lemurs (prosimians) and New World monkeys, encoding the alpha1,3GT enzyme that synthesizes a carbohydrate antigen called alpha-gal epitope. The alpha-gal epitope is present in large numbers on cell membrane glycolipids and glycoproteins. The alpha1,3GT gene is inactivated in ancestral Old World monkeys and apes by frameshift single-base deletions forming premature stop codons. Because of this gene inactivation, humans, apes, and Old World monkeys lack alpha-gal epitopes and naturally produce an antibody called the anti-Gal antibody which binds specifically to alpha-gal epitopes and which is the most abundant antibody in humans. The evolutionary event that resulted in the inactivation of the alpha1,3GT gene in ancestral Old World primates might have been mediated by a pathogen endemic to Eurasia-Africa landmass that exerted pressure for selection of primate populations lacking the alpha-gal epitope. Once the alpha-gal epitope was eliminated, primates could produce the anti-Gal antibody, possibly as means of defense against pathogens expressing this epitope
metabolism
-
Otg proteins are involved in alpha1,3-galactosylation of O- and N-linked glycans
metabolism
-
Otg proteins are involved in alpha1,3-galactosylation of O- and N-linked glycans
-
additional information
the N-terminal loop is folded when the acceptor substrate is bound in the active site, substrate binding structure and analysis using ab initio quantum mechanics/molecular mechanics dynamic simulations, overview
additional information
-
identification and quantification of 47 N-glycans from wild-type and enzyme kockout pig fibroblasts using MALDI-TOF mass spectrometry, overview
additional information
-
the N-terminal loop is folded when the acceptor substrate is bound in the active site, substrate binding structure and analysis using ab initio quantum mechanics/molecular mechanics dynamic simulations, overview
additional information
-
reaction mechanism: substrate-assisted mechanism for retaining glycosyltransferases consisting of the stabilization of the developing negative charge on the beta-phosphate by the hydrogen of the attacking hydroxyl group of the acceptor molecule. This interaction is impaired in the alpha1,3-GalT reactants, which explains why Glu317 is required to nucleophilically assist initial catalysis by pushing leaving-group departure. The presence of Glu317 opens the door to the possibility of a double-displacement mechanism in GT6 family. In alpha1,3-GalT the substrate-assisted catalysis might be necessary in both mechanisms, because the nucleophilic strength of Glu317 is reduced by the interactions it makes to ensure proper acceptor binding. The same effect might be found in the absence of the acceptor when Glu317 interacts with water molecules, quantum mechanics/molecular mechanics dynamic simulations analysis, overview
Show AA Sequence and Transmembrane Helices (451 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
secondary structure and fold recognition prediction from amino acid sequence and analysis
additional information
-
secondary structure and fold recognition prediction from amino acid sequence and analysis
additional information
molecular modeling and HCA alignment of C-terminal domain
additional information
-
molecular modeling and HCA alignment of C-terminal domain
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
5% PEG 6000, 0.1 M Tris-HCl, pH 8.0, 10 mM MnCl2, 10 mM UDP, in complex with substrate p-nitrophenyl-beta-galactoside, 25% glycerol as cryoprotectant
AGGL-mutant in complex with UDP-N-acetylgalactosamine with 20 mM MES-NaOH buffer, pH 6, 10% glycerol, 10 mM MnCl2, 10 mM UDP-N-acetylgalactosamine and reservoir solution (10-15% PEG 6000, 0.1 M Tris-HCl, pH 8, 15-25% MPD), and RAAI-mutant with 0.1 M Tris-HCl, pH 8, 10-50% PEG 4000, 0.2 M sodium acetate, 10 mM MnCl2, 10 mM UDP-galactose with the same reservoir solution, vapor diffusion hanging drop method
apo crystals of alpha3GT are grown by the vapour-diffusion, hanging-drop method. Structure of a complex containing an inhibitory analogue of UDP-galactose, UDP-2F-galactose, in a complex with the Arg365Lys mutant of alpha3GT. The binding of a donor substrate analogue induces conformational changes in both the ligand and the enzyme. Two loops of alpha3GT are stabilized in the complex of which the C-terminal region, in particular, is highly flexible. Structural transitions in this region are connected with donor substrate binding and distortion (ground state destabilization), cleavage of the UDP to galactose bond, formation of a binding site for acceptor substrate and UDP release
crystal structure of the Glu317Gln mutant in complex with UDP-Gal is reported
purified recombinant enzyme mutants with bound UDP-Gal and Mn2+, hanging drop vapour diffusion at 16°C, mixing of 0.001 ml protein solution containing 5 mg/ml mutant E317Q in 20 mM MES-NaOH buffer, pH 6.0, and 10% glycerol, containing 10 mM MnCl2 and 10 mM UDP-Gal with 0.001 ml of reservoir solution containing 10% PEG 6000, 0.1 M Tris-HCl, pH 8.0, and 8% MPD, for mutant D316N and D316E, 0.001 ml of 5 mg/ml protein in in 20 mM MES-NaOH buffer, pH 6.0, with 10% glycerol, 10 mM UDP-Gal, 10 mM MnCl2, and 10 mM N-acetyllactosamine, are mixed with 0.001 ml of a reservoir solution containing 5-10% PEG 6000, 0.1 M Tris-HCl, pH 8.0, and 5-14% MPD, X-ray diffraction structure determination and analysis at 1.77-2.2 A resolution
structure analysis of the enzyme in ternary complex with substrate UDP-2F-Gal, crystal structure fold-type A, PDB ID 2VFZ
structure analysis of the enzyme in ternary complex with substrates UDP and lactose, crystal structure fold-type A, PDB ID 1GWF
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D316E
D316N
E317A
relative activity of mutant protein: 0.1% (compared to wild-type 100%)
E317C
relative activity of mutant protein: 0.8% (compared to wild-type 100%)
E317D
relative activity of mutant protein: 0.4% (compared to wild-type 100%)
E317H
relative activity of mutant protein: 0.1% (compared to wild-type 100%)
E317Q
H280A/A281A/A282A
mutant AAA, 20 or 200 mM lactose as acceptor, 14 and 41% galactosyltransferase activity (UDP-galactose as donor), 4 and 6% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
H280A/A281G/A282G
mutant AGG, 20 or 200 mM lactose as acceptor, 0.4 and 1% galactosyltransferase activity (UDP-galactose as donor), 0.3 and 2% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0, among the mutants with highest N-acetylgalactosamnine transferase activity and ability to transfer C2-modified sugars
H280A/A281G/A282G/L283I
AGGI-mutant, instable, leucin 283 is important for enzyme stability
H280A/A281G/A282G/L283L
AGGL-mutant, higher N-acetylgalactosamine transferase activity than galactosyltransferase activity, leucin 283 is important for enzyme stability
H280A/A281G/A282G/L283V
AGGV-mutant, instable, leucin 283 is important for enzyme stability
H280G/A281A/A282G
mutant GAG, 20 or 200 mM lactose as acceptor, 5 and 27% galactosyltransferase activity (UDP-galactose as donor), 4 and 6% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
H280G/A281G/A282G/L283I
GGGI-mutant, instable, leucin 283 is important for enzyme stability
H280G/A281G/A282G/L283L
GGGL-mutant, higher N-acetylgalactosamine transferase activity than galactosyltransferase activity, leucin 283 is important for enzyme stability
H280G/A281G/A282G/L283V
GGGV-mutant, instable, leucin 283 is important for enzyme stability
H280L/A281G/A282G
mutant LGG, 20 or 200 mM lactose as acceptor, 2 and 1% galactosyltransferase activity (UDP-galactose as donor), 3 and 2% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
H280R/A281A/A282A/L283I
RAAI-mutant, no catalytic activity, crystallisation
H280S/A281G/A282G
mutant SGG, 20 or 200 mM lactose as acceptor, 5 and 5% galactosyltransferase activity (UDP-galactose as donor), 2 and 11% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0, among the mutants with highest GalNac transferase activity and ability to transfer C2-modified sugars
H280T/A281G/A282G
mutant TGG, 20 or 200 mM lactose as acceptor, 3 and 15% galactosyltransferase activity (UDP-galactose as donor), 1 and 6% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
H280V/A281G/A282G
mutant VGG, 20 or 200 mM lactose as acceptor, 4 and 16% galactosyltransferase activity (UDP-galactose as donor), 0.5 and 3% N-acetylgalactosamine transferase activity (UDP-N-acetylgalactosamine as donor), 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
H315Q
mutant protein shows modest changes in kinetic parameters for lactose
H315R
mutant shows a major losss in catalytic activity arising from a 500fold reduction in kcat
Q247E
50fold reduction in turnover number for transferase reaction, unchanged hydrolase activity, Km-values for UDP-galactose and lactose are similar to the wild-type values
R365K
mutation reduces turnover-number for UDP-galactose hydrolysis about 10fold but has no significant effect on the affinity for UDP-galactose
W249G
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1.95fold increase in Km-value for UDP-galactose in galactosyltransferase reaction, turnover number of hydrolase reaction is identical to wild-type value, 2.1fold increase in Km-value for UDP-galactose in hydrolase reaction. Mutation does not affect the overall structure of the enzyme or its interactions with ligands
W250F
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2.6fold increase in turnover number of galactosyltransferase reaction, 9.3fold increase in Km-value for UDP-galactose in galactosyltransferase reaction, 1.1fold decrease in Km-value for lactose, 1.4fold increase in turnover number of hydrolase reaction, 1.5fold increase in Km-value for UDP-galactose in hydrolase reaction
W250Y
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1.2fold increase in turnover number of galactosyltransferase reaction, 5.2fold increase in Km-value for UDP-galactose in galactosyltransferase reaction, 2fold decrease in Km-value for lactose, 1.8fold increase in turnover number of hydrolase reaction, 2.3fold increase in Km-value for UDP-galactose in hydrolase reaction
W314Y
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29fold decrease in turnover number of galactosyltransferase reaction, 1.67fold increase in Km-value for UDP-galactose in galactosyltransferase reaction, 2fold decrease in Km-value for lactose, 1.1fold increase in turnover number of hydrolase reaction, 1.4fold increase in Km-value for UDP-galactose in hydrolase reaction. Mutation does not affect the overall structure of the enzyme or its interactions with ligands
W356T
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12.3fold decrease in turnover number of galactosyltransferase reaction, 2fold increase in Km-value for UDP-galactose in galactosyltransferase reaction, 6.3fold increase in Km-value for lactose, 14.5fold decrease in turnover number of hydrolase reaction, 2.5fold increase in Km-value for UDP-galactose in hydrolase reaction
additional information
D316E
mutant show modest reduction in kcat and Km for lactose. Strucutural studies with mutant D316E show that the negative charge is crucial for catalytic activity and needed for its interaction with Arg202 for an active site structure that facilitates the binding of UDP-gal in a catalytically competent conformation
D316E
site-directed mutagenesis, a catalytic domain mutant, crystal structure determination with bound UDP-Gal and Mn2+
D316N
mutant is inactive. Strucutural studies with mutant D316N show that the negative charge is crucial for catalytic activity and needed for its interaction with Arg202 for an active site structure that facilitates the binding of UDP-gal in a catalytically competent conformation
D316N
site-directed mutagenesis, a catalytic domain mutant, crystal structure determination with bound UDP-Gal and Mn2+
E317Q
turnover number for transferase reaction is approximately 2400times lower than that of the wild-type enzyme 120fold reduction in hydrolysis of UDP-galactose. Km-value for UDP-galactose is unchanged
E317Q
crystal structure of the complex of mutant E317Q with UDP-galactose exhibiting a bent configuration stabilized by interactions of the galactose with multiple residues in the enzyme including those in a highly conserved region (His315 to Ser318) is shown
E317Q
site-directed mutagenesis, a catalytic domain mutant, crystal structure determination with bound UDP-Gal and Mn2+
additional information
attaching beta p-nitrophenyl to galactose converts the complex from a poor into a good substrate, the group mimics a monosaccharide like N-acetylglucosamine
additional information
mutated enzymes transfer N-acetylgalactosamine or C2-modified galactose from their UDP derivatives, mutations on the sugar-donor-binding residues (histidine 280, alanine 281, alanine 282) to establish changed specificity, 5-19% of original galactose transferase activity remains, , acceptor affinity is affected by mutation of histidine 280, additional mutation of S347A in all mutants does not affect the enzyme activity and kinetic parameter by itself but resembles the human blood group A and B glycosyltransferases more closely
additional information
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mutated enzymes transfer N-acetylgalactosamine or C2-modified galactose from their UDP derivatives, mutations on the sugar-donor-binding residues (histidine 280, alanine 281, alanine 282) to establish changed specificity, 5-19% of original galactose transferase activity remains, , acceptor affinity is affected by mutation of histidine 280, additional mutation of S347A in all mutants does not affect the enzyme activity and kinetic parameter by itself but resembles the human blood group A and B glycosyltransferases more closely
additional information
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truncation of 3 amino acid residues from the C-terminus, and a frame shift mutation result in a complete loss of activity
additional information
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porcine aortic endothelial cells from control (Gal+/+) and Gal-deficient (Gal-/-) pigs are incubated with human lepirudin anticoagulated whole blood from healthy donors. E-selectin expression is measured by flow cytometry. The C3 inhibitor compstatin and a C5aR antagonist is used to study the role of complement. Gal+/+ porcine aortic endothelial cells incubated with human whole blood show a marked complement C5b-9 dependent up-regulation of E-selectin and secretion of porcine IL-6 and IL-8. Gal-/- cells respond with weak E-selectin and cytokine expression so that the role of complement can not be determined. Human IL-6, IL-8, IFN-gamma, MIP-1alpha, MIP-1beta, eotaxin, and RANTES are detected in the Gal+/+ system, but no responses is seen in the Gal-/- system
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
detergent: rapid and irreversible inactivation in absence of detergent, more than 50% loss of activity after 4-6 weeks
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mutants are not stable under assay conditions (10 mM Tris-HCl, pH 7.4, 37°C), but for 20 min with 10 mM MES, pH 6.0, at 30°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM MES, pH 6.2, 50 mM NaCl, detergent, glycerol, stable for several months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
centrifugation of cell culture, pellet lysed with EasyLyse, loaded onto Ni-chelate column, washing and elution with 20 mM Tris-HCl, pH 7.9, containing NaCl and imidazole
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned from cDNA library, expression of full-length and truncated DNA in Escherichia coli and COS-1 cells, the truncated sequences are fused to protein A sequence resulting in expression of soluble chimeric proteins, DNA sequence determination and analysis
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cloned from genomic and cDNA library and macrophages, DNA sequence analysis, alternative splicing
expressed in Escherichia coli and COS-7 cells as a His-tagged fusion protein
expression in COS-7 cells, promotor sequences A-C determination and analysis, gene regulation and regulatory sequences, alternative splicing
AF415202
expression in Escherichia coli
gene GGTA1, partial sequence comparisons and phylogenetic analysis
murine alpha(1,3)GT gene is cloned into the Moloney murine leukemia retroviral vector, pLNCX, giving rise to pLNCKG expression in A549 human lung tumor cells
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mutants W249G, W250Y, W250F, W315Y anf W356T, of catalytic domain are constructed and expressed in Escherichia coli BL21
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
identification of N-acetyllactosamine moiety of glycoproteins and glycolipids by chemiluminescence with mutated enzymes
medicine
synthesis
medicine
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protection against tumors by immunization with AdaGT-transduced tumor cells (replication deficient adenovirus containing the alpha1,3GT gene) is studied in alpha1,3GT knockout (KO) mice, challenged with the highly tumorigenic BL6 melanoma cells. These mice lack alpha-gal epitopes and can produce anti-Gal. Immunization of KO mice with AdaGT-transduced BL6 cells protects many of the mice against challenge with live BL6 cells lacking alpha-gal epitopes. Immunization with AdalphaGT transduced autologous tumor cells may serve as adjuvant immunotherapy delivered after completion of standard therapy
medicine
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the Bacillus thuringiensis phosphatidylinositol-specific phospholipase C and the alpha(1,3)GT genes are engineered to be delivered to cells in two separate retroviral vectors. Activity of phosphatidylinositol-specific phospholipase C, secreted from transduced A549 human lung tumor cells shows a synergistic increase in alphagal mediated complement killing in an in vitro assay. When applied to in vivo therapy of solid tumors, this approach may enhance anti-tumor immune responses
medicine
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Galalpha(1,3)Gal synthesized by iGb3S is immunogenic and elicits antibodies in GGTA1-/- mice. Galalpha(1,3)Gal synthesized by iGb3S may affect survival of pig transplants in humans
medicine
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application of pig liver for extracorporeal blood circulation in conditions of acute liver failure. GalT knockout hepatocytes and wild-type cells diplay no tumorigenicity. GalT knockout cells show less apoptosis and more viability than wild-type cells when exposed to complement and xenogeneic serum
medicine
development of alpha-1,3-galactosyltransferase (GGTA1) and cytidine monophosphate-N-acetylneuraminic acid hydroxylase (CMAH) double-knockout piglets as donor animals for xenotransplantation. Compared to cells from GGTA1-knockout pigs, human antibody binding and antibody-mediated complement-dependent cytotoxicity are significantly reduced in cells from GGTA1/CMAH double-knockout pigs
medicine
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in patients with pretreated metastatic renal cell carcinoma, HyperAcute Renal immunotherapy, i.e. treatment with two allogeneic renal cancer cell lines genetically modified to express alpha(1,3)Gal, is well tolerated and demonstrates antitumor activity
synthesis
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enzymic synthesis of octadecameric saccharides of mutiply branched blood group I-type, carrying 4 distal alpha-1,3-galactose residues
synthesis
-
useful tool for production of a range of compounds to further investigate the binding site of anti-Gal and other proteins with Galalpha(1-3)Gal binding sites
synthesis
attaching beta p-nitrophenyl to galactose converts the complex from a poor into a good substrate, the group mimics a monosaccharide like N-acetylglucosamine
synthesis
production of novel complex glycans with role in biological recognition processes with engineered enzyme with modified substrate specificity
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Basu, M.; Basu, S.
Enzymatic synthesis of a blood group B-related pentaglycosylceramide by an alpha-galactosyltransferase from rabbit bone marrow
J. Biol. Chem.
248
1700-1706
1973
Oryctolagus cuniculus
brenda
Blake, D.A.; Goldstein, I.J.
An alpha-D-galactosyltransferase activity in Ehrlich ascites tumor cells. Biosynthesis and characterization of a trisaccharide (alpha-D-galactose-(1-3)-N-acetyllactosamine)
J. Biol. Chem.
256
5387-5393
1981
Mus musculus
brenda
Van den Eijnden, D.H.; Blanken, W.M.; Winterwerp, H.; Schiphorst, W.E.C.M.
Identification and characterization of an UDP-Gal: N-acetyllactosaminide alpha-1,3-D-galactosyltransferase in calf thymus
Eur. J. Biochem.
134
523-530
1983
Bos taurus
brenda
Elices, M.J.; Goldstein, I.J.
Glycosyltransferase activities of Ehrlich ascites tumor cells: detection, isolation, and characterization using oligosaccharide-Synsorb beads
Arch. Biochem. Biophys.
254
329-341
1987
Mus musculus, Bos taurus
brenda
Blanken, W.M.; van den Eijnden, D.H.
Biosynthesis of terminal Gal alpha (1-3)Gal beta 1-4)GlcNAc-R oligosaccharide sequences on glycoconjugates. Purification and acceptor specificity of a UDP-Gal:N-acetyllactosaminide alpha(1-3)galactosyltransferase from calf thymus
J. Biol. Chem.
260
12927-12934
1985
Bos taurus
brenda
Beyer, T.A.; Sadler, J.E.; Rearick, J.I.; Paulson, J.C.; Hill, R.L.
Glycosyltransferases and their use in assessing oligosaccharide structure and structure-function relationships
Adv. Enzymol. Relat. Areas Mol. Biol.
52
23-175
1981
Bos taurus
brenda
Elices, M.J.; Goldstein, I.J.
Biosynthesis of bi-, tri-, and tetraantennary oligosaccharides containing alpha-D-galactosyl residues at their nonreducing termini. Branch specificity of the Ehrlich tumor cell alpha(1,3)-galactosyltransferase
J. Biol. Chem.
264
1375-1380
1989
Mus musculus
brenda
Joziasse, D.H.; Shaper, N.L.; Kim, D.; van den Eijnden, D.H.; Shaper, J.H.
Murine alpha 1,3-galactosyltransferase. A single gene locus specifies four isoforms of the enzyme by alternative splicing
J. Biol. Chem.
267
5534-5541
1992
Mus musculus (P23336)
brenda
Joziasse, D.H.; Shaper, J.H.; van den Eijnden, D.H.; van Tunen, A.J.; Shaper, N.L.
Bovine alpha 1,3-galactosyltransferase: isolation and characterization of a cDNA clone. Identification of homologous sequences in human genomic DNA
J. Biol. Chem.
264
14290-14297
1989
Bos taurus
brenda
Elices, M.J.; Blake, D.A.; Goldstein, I.J.
Purification and characterization of a UDP-Gal:beta-D-Gal(1,4)-D-GlcNAc alpha(1,3)-galactosyltransferase from Ehrlich ascites tumor cells
J. Biol. Chem.
261
6064-6072
1986
Mus musculus
brenda
Van Halbeek, H.; Vliegenthart, J.F.G.
alpha-D-Galactosyltransferase activity in calf thymus. A high-resolution 1H-NMR study
Biochem. Biophys. Res. Commun.
110
124-131
1983
Bos taurus
brenda
Van den Eijnden, D.H.; Winterwerp, H.; Smeeman, P.; Schiphorst, W.E.C.M.
Novikoff ascites tumor cells contain N-acetyllactosaminide beta 1-3 and beta 1-6 N-acetylglucosaminyltransferase activity
J. Biol. Chem.
258
3435-3437
1983
Rattus norvegicus
brenda
Henion, T.R.; Macher, B.A.; Anaraki, F.; Galili, U.
Defining the minimal size of catalytically active primate alpha 1,3 galactosyltransferase: structure-function studies on the recombinant truncated enzyme
Glycobiology
4
193-201
1994
no activity in african green monkey, Callithrix jacchus
brenda
Seppo, A.; Penttila, L.; Niemela, R.; Maaheimo, H.; Renkonen, O.; Keane, A.
Enzymic synthesis of octadecameric saccharides of multiply branched blood group I-type, carrying four distal alpha1,3-galactose or beta1,3-GlcNAc residues
Biochemistry
34
4655-4661
1995
Mus musculus, Bos taurus
brenda
Meldgaard, P.; Holmes, E.H.; Bennett, E.P.; Clausen, H.; Zeuthen, J.; Wolf, H.O.T.F.
Blood group ABO-related glycosylation of urothelial cell lines: immunocytological, enzymic, and genetic characterization
Cancer Res.
54
2440-2447
1994
Homo sapiens
brenda
Imberty, A.; Monier, C.; Bettler, E.; Morera, S.; Freemont, P.; Sippl, M.; Flockner, H.; Ruger, W.; Breton, C.
Fold recognition study of alpha3-galactosyltransferase and molecular modeling of the nucleotide sugar-binding domain
Glycobiology
9
713-722
1999
Sus scrofa (P50127), Sus scrofa
brenda
Stults, C.L.M.; Macher, B.A.; Bhatti, R.; Srivastava, O.P.; Hindsgaul, O.
Characterization of the substrate specificity of alpha1,3-galactosyltransferase utilizing modified N-acetyllactosamine disaccharides
Glycobiology
9
661-668
1999
Mus musculus
brenda
Mercier, D.; Charreau, B.; Wierinckx, A.; Keijser, R.; Adriaensens, L.; Van den Berg, R.; Joziasse, D.H.
Regulation of alpha1,3galactosyltransferase expression in pig endothelial cells: Implications for xenotransplantation
Eur. J. Biochem.
269
1464-1473
2002
Sus scrofa (AF415202), Sus scrofa
brenda
Zhang, Y.; Swaminathan, G.J.; Deshpande, A.; Boix, E.; Natesh, R.; Xie, Z.; Acharya, K.R.; Brew, K.
Roles of individual enzyme-substrate interactions by alpha-1,3-galactosyltransferase in catalysis and specificity
Biochemistry
42
13512-13521
2003
Bos taurus (P14769)
brenda
Taylor, S.G.; McKenzie, I.F.; Sandrin, M.S.
Characterization of the rat alpha(1,3)galactosyltransferase: evidence for two independent genes encoding glycosyltransferases that synthesize Galalpha(1,3)Gal by two separate glycosylation pathways
Glycobiology
13
327-337
2003
Rattus norvegicus
brenda
Zhang, Y.; Deshpande, A.; Xie, Z.; Natesh, R.; Acharya, K.R.; Brew, K.
Roles of active site tryptophans in substrate binding and catalysis by alpha-1,3 galactosyltransferase
Glycobiology
14
1295-1302
2004
Bos taurus
brenda
Deriy, L.; Ogawa, H.; Gao, G.P.; Galili, U.
In vivo targeting of vaccinating tumor cells to antigen-presenting cells by a gene therapy method with adenovirus containing the alpha1,3galactosyltransferase gene
Cancer Gene Ther.
12
528-539
2005
Mus musculus
brenda
Hellrung, D.J.; Kisselev, S.; Link, C.J.
Co-expression of alpha(1,3)galactosyltransferase and Bacillus thuringiensis PIPLC enhances hyperacute rejection of tumor cells
Cancer Immunol. Immunother.
56
25-34
2007
Mus musculus
brenda
Milland, J.; Christiansen, D.; Lazarus, B.D.; Taylor, S.G.; Xing, P.X.; Sandrin, M.S.
The molecular basis for galalpha(1,3)gal expression in animals with a deletion of the alpha1,3galactosyltransferase gene
J. Immunol.
176
2448-2454
2006
Mus musculus
brenda
Jamaluddin, H.; Tumbale, P.; Withers, S.G.; Acharya, K.R.; Brew, K.
Conformational changes induced by binding UDP-2F-galactose to alpha-1,3galactosyltransferase - implications for catalysis
J. Mol. Biol.
369
1270-1281
2007
Bos taurus (P14769)
brenda
Koike, C.; Uddin, M.; Wildman, D.E.; Gray, E.A.; Trucco, M.; Starzl, T.E.; Goodman, M.
Functionally important glycosyltransferase gain and loss during catarrhine primate emergence
Proc. Natl. Acad. Sci. USA
104
559-564
2007
Lemur catta (Q8HYB2), Loris tardigradus (A1YGR6), Alouatta caraya (A1YGR5)
brenda
Tumbale, P.; Jamaluddin, H.; Thiyagarajan, N.; Brew, K.; Acharya, K.R.
Structural basis of UDP-galactose binding by alpha-1,3-galactosyltransferase (alpha3GT): role of negative charge on aspartic acid 316 in structure and activity
Biochemistry
47
8711-8718
2008
Bos taurus, Bos taurus (P14769)
brenda
Molina, P.; Knegtel, R.M.; Macher, B.A.
Site-directed mutagenesis of glutamate 317 of bovine alpha -1,3Galactosyltransferase and its effect on enzyme activity: Implications for reaction mechanism
Biochim. Biophys. Acta
1770
1266-1273
2007
Bos taurus (P14769), Bos taurus
brenda
Saethre, M.; Schneider, M.K.; Lambris, J.D.; Magotti, P.; Haraldsen, G.; Seebach, J.D.; Mollnes, T.E.
Cytokine secretion depends on Galalpha (1,3)Gal expression in a pig-to-human whole blood model
J. Immunol.
180
6346-6353
2008
Sus scrofa
brenda
Jamaluddin, H.; Tumbale, P.; Ferns, T.A.; Thiyagarajan, N.; Brew, K.; Acharya, K.R.
Crystal structure of alpha-1,3-galactosyltransferase (alpha3GT) in a complex with p-nitrophenyl-beta-galactoside (pNPbetaGal)
Biochem. Biophys. Res. Commun.
385
601-604
2009
Bos taurus (P14769)
brenda
Pasek, M.; Ramakrishnan, B.; Boeggeman, E.; Manzoni, M.; Waybright, T.; Qasba, P.
Bioconjugation and detection of lactosamine moiety using l, 3-galactosyltransferase mutants that transfer C2-modified galactose with a chemical handle
Bioconjug. Chem.
20
608-618
2009
Bos taurus (P14769), Bos taurus
brenda
Tumbale, P.; Jamaluddin, H.; Thiyagarajan, N.; Acharya, K.R.; Brew, K.
Screening a limited structure-based library identifies UDP-GalNAc-specific mutants of alpha-1,3-galactosyltransferase
Glycobiology
18
1036-1043
2008
Bos taurus (P14769), Bos taurus
brenda
Shoemaker, G.; Soya, N.; Palcic, M.; Klassen, J.
Temperature-dependent cooperativity in donor-acceptor substrate binding to the human blood group glycosyltransferases
Glycobiology
18
587-592
2008
Homo sapiens
brenda
Han, W.; Cai, L.; Wu, B.; Li, L.; Xiao, Z.; Cheng, J.; Wang, P.G.
The wciN gene encodes an alpha-1,3-galactosyltransferase involved in the biosynthesis of the capsule repeating unit of Streptococcus pneumoniae serotype 6B
Biochemistry
51
5804-5810
2012
Streptococcus pneumoniae
brenda
Ohashi, T.; Fujiyama, K.; Takegawa, K.
Identification of novel alpha1,3-galactosyltransferase and elimination of alpha-galactose-containing glycans by disruption of multiple alpha-galactosyltransferase genes in Schizosaccharomyces pombe
J. Biol. Chem.
287
38866-38875
2012
Schizosaccharomyces pombe, Schizosaccharomyces pombe ARC039
brenda
Gomez, H.; Lluch, J.; Masgrau, L.
Substrate-assisted and nucleophilically assisted catalysis in bovine alpha1,3-galactosyltransferase. Mechanistic implications for retaining glycosyltransferases
J. Am. Chem. Soc.
135
7053-7063
2013
Bos taurus
brenda
Ardevol, A.; Rovira, C.
Reaction mechanisms in carbohydrate-active enzymes: glycoside hydrolases and glycosyltransferases. Insights from ab initio quantum mechanics/molecular mechanics dynamic simulations
J. Am. Chem. Soc.
137
7528-7547
2015
Bos taurus (P14769), Micrococcus luteus
brenda
Galili, U.
Significance of the evolutionary alpha1,3-galactosyltransferase (GGTA1) gene inactivation in preventing extinction of apes and old world monkeys
J. Mol. Evol.
80
1-9
2014
Callithrix jacchus (Q8SQ20), Homo sapiens (Q4G0N0), Metatheria, Platyrrhini, Ateles sp., Saimiri sp., Erythrocebus patas, Chlorocebus sabaeus, Macaca mulatta, Pongo pygmaeus, Pongo abelii, Gorilla gorilla, Pan troglodytes, Hominoidea, Cercopithecoidea, Lemuridae, Eutheria
brenda
Park, H.; Kim, Y.; Kim, K.; Kim, Y.; Yang, Y.; Jin, J.; Kim, Y.; Kim, B.; Shim, H.; Kim, Y.
Comparative n-linked glycan analysis of wild-type and alpha1,3-galactosyltransferase gene knock-out pig fibroblasts using mass spectrometry approaches
Mol. Cells
38
65-74
2015
Sus scrofa
brenda
Chen, C.; Liu, B.; Xu, Y.; Utkina, N.; Zhou, D.; Danilov, L.; Torgov, V.; Veselovsky, V.; Feng, L.
Biochemical characterization of the novel alpha-1, 3-galactosyltransferase WclR from Escherichia coli O3
Carbohydr. Res.
430
36-43
2016
Escherichia coli (B5T072), Escherichia coli O3 (B5T072)
brenda
Gao, H.; Zhao, C.; Xiang, X.; Li, Y.; Zhao, Y.; Li, Z.; Pan, D.; Dai, Y.; Hara, H.; Cooper, D.K.; Cai, Z.; Mou, L.
Production of alpha1,3-galactosyltransferase and cytidine monophosphate-N-acetylneuraminic acid hydroxylase gene double-deficient pigs by CRISPR/Cas9 and handmade cloning
J. Reprod. Dev.
63
17-26
2017
Sus scrofa (P50127)
brenda
Hahn, A.; Drake, C.; Denmeade, S.; Zakharia, Y.; Maughan, B.; Kennedy, E.; Link, C.J.; Vahanian, N.; Hammers, H.; Agarwal, N.
A Phase I study of alpha-1,3-galactosyltransferase-expressing allogeneic renal cell carcinoma immunotherapy in patients with refractory metastatic renal cell carcinoma
Oncologist
25
121-e213
2020
Homo sapiens
brenda
Wang, Q.; Zhang, X.; Wang, B.; Bai, G.; Pan, D.; Yang, P.; Tao, K.; Li, X.; Dou, K.
Immortalization of porcine hepatocytes with a alpha-1,3-galactosyltransferase knockout background
Xenotransplantation
27
e12550
2020
Sus scrofa
brenda
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