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Information on EC 2.4.1.87 - N-acetyllactosaminide 3-alpha-galactosyltransferase and Organism(s) Bos taurus and UniProt Accession P14769
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2.4.1.87 N-acetyllactosaminide 3-alpha-galactosyltransferaseIUBMB Comments
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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Word Map
- 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
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
ggta1, alpha1,3-galactosyltransferase, alpha1,3gt, alpha-1,3-galactosyltransferase, alpha-galactosyltransferase, alpha1,3galactosyltransferase, igb3s, alpha3gt, alpha1,3galt, igb3 synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-galactosyltransferase
-
-
-
-
beta-D-galactosyl-N-acetylglucosaminylglycopeptide alpha-1,3-galactosyltransferase
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-acetyllactosamine
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-acetyllactosamine alpha1-->3-
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-galactosylacetylglucosamine alpha-1,3-
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-galactosylacetylglucosaminylgalactosylglucosylceramide
-
-
-
-
glucosaminylglycopeptide alpha-1,3-galactosyltransferase
-
-
-
-
N-acetyllactoseaminide 3-alpha-D-galactosyltransferase
-
-
-
-
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
-
-
-
-
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)
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-
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.
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
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-2-acetonyl-2-deoxy-galactose + asialofetuin
UDP + ?
mutant enzymes SGG and AGG, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
-
-
?
UDP-2-acetonyl-2-deoxy-galactose + N-acetyllactosaminyl-chitotriose
UDP + ?
mutant enzymes SGG, AGG, and TGG, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
-
-
?
UDP-galactose + D-galactose
UDP + alpha-D-galactosyl-1,3-D-galactoside
-
-
-
?
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-N-acetyl-azido-galactosamine + N-acetyllactosaminyl-chitotriose
UDP + ?
mutant enzymes SGG, AGG, and TGG, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
-
-
?
UDP-N-acetylgalactosamine + N-acetyllactosamine
UDP + ?
no reaction of wild-type, only of AGGL mutant
-
-
?
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
-
-
-
?
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
-
-
-
-
?
UDP-galactose + asialo-alpha1-acid glycoprotein
UDP + alpha-D-galactosyl-asialo-alpha1-acid glycoprotein
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
UDP-galactose + beta-D-galactosyl-1,4-D-glucose
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-D-glucose
-
-
-
-
?
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 + lactose
UDP + alpha-D-galactosyl-(1-3)-beta-D-galactosyl-(1-4)-beta-D-glucose
-
-
-
-
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
UDP-galactose + lactose
UDP + ?
wild-type enzyme, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
-
-
?
UDP-galactose + lactose
UDP + ?
wild-type enzyme, and mutant enzymes AAA, GAG, AGG, SGG, TGG, LGG, VGG, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
-
-
?
UDP-N-acetylgalactosamine + lactose
UDP + ?
mutant enzymes AAA, GAG, AGG, SGG, TGG, LGG, VGG, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
-
-
?
UDP-N-acetylgalactosamine + lactose
UDP + ?
no reaction of wild-type, only of AGGL mutant
-
-
?
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 + 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 + 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 + 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 + 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
-
enzyme introduces galactosyl residues in alpha anomeric configuration to the Galbeta(1-4)GlcNAc units on the acceptor substrate
-
?
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
-
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
-
?
UDP-galactose + glycoprotein
UDP + alpha-D-galactosylglycoprotein
-
-
-
-
?
UDP-galactose + glycoprotein
UDP + alpha-D-galactosylglycoprotein
-
the nonreducing terminal N-acetyllactosamine residue of glycoproteins can act as acceptor
-
-
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
-
-
-
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
i.e. beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
?
UDP-galactose + N-acetyllactosamine
UDP + alpha-D-galactosyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
i.e. beta-D-galactosyl-1,4-N-acetyl-D-glucosamine
-
?
additional information
?
-
-
structural basis of UDP-galactose binding at the catalytic domain of alpha3GT, overview
-
-
?
additional information
?
-
structural basis of UDP-galactose binding at the catalytic domain of alpha3GT, overview
-
-
?
additional information
?
-
-
functions in the biosynthesis of calf thymocyte cell-surface glycoconjugates including glycoproteins
-
-
?
additional information
?
-
-
functions in biosynthesis of calf thymocyte cell-surface glycoconjugates including glycoproteins
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-galactose + lactose
UDP + ?
wild-type enzyme, 37°C, MnCl2, 25 mM Tris-HCl, pH 7.0
-
-
?
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
-
-
-
?
additional information
?
-
-
functions in the biosynthesis of calf thymocyte cell-surface glycoconjugates including glycoproteins
-
-
?
additional information
?
-
-
functions in biosynthesis of calf thymocyte cell-surface glycoconjugates including glycoproteins
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
MnCl2
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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 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 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 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 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 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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme is a family 6 glycosyltransferase, family members have a nucleophilic residue (Glu317) situated close to the anomeric carbon
additional information
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GGTA1_BOVIN
368
1
43247
Swiss-Prot
Secretory Pathway (Reliability: 1), other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
crystal structure of the Glu317Gln mutant in complex with UDP-Gal is reported
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D316E
site-directed mutagenesis, a catalytic domain mutant, crystal structure determination with bound UDP-Gal and Mn2+
D316N
site-directed mutagenesis, a catalytic domain mutant, crystal structure determination with bound UDP-Gal and Mn2+
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
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
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
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
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
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
W249G
-
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
-
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
-
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
-
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
-
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
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
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
-
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli and COS-7 cells as a His-tagged fusion protein
mutants W249G, W250Y, W250F, W315Y anf W356T, of catalytic domain are constructed and expressed in Escherichia coli BL21
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
identification of N-acetyllactosamine moiety of glycoproteins and glycolipids by chemiluminescence with mutated enzymes
synthesis
synthesis
-
enzymic synthesis of octadecameric saccharides of mutiply branched blood group I-type, carrying 4 distal alpha-1,3-galactose residues
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Bos taurus, Mus musculus
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
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
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
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
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
Bos taurus, Mus musculus
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)
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
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)
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)
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
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)
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
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
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
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