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Galbeta(1-3)Gal(6-O-sulfate)beta(1-4)Xyl(2-O-phosphate)beta1-O-Ser + UDP-GlcUA
GlcUAbeta(1-3)Galbeta(1-3)Gal(6-O-sulfate)beta(1-4)Xyl(2-O-phosphate)beta1-O-Ser + UDP
-
-
-
-
?
Galbeta(1-3)Gal(6-O-sulfate)beta(1-4)Xylbeta1-O-Ser + UDP-GlcUA
GlcUAbeta(1-3)Galbeta(1-3)Gal(6-O-sulfate)beta(1-4)Xylbeta1-O-Ser + UDP
-
-
-
-
?
Galbeta(1-3)Galbeta(1-4)Xyl(2-O-phosphate)beta1-O-Ser + UDP-GlcUA
GlcUAbeta(1-3)Galbeta(1-3)Galbeta(1-4)Xyl(2-O-phosphate)beta1-O-Ser + UDP
-
-
-
-
?
Galbeta(1-3)Galbeta(1-4)Xylbeta1-O-Ser + UDP-GlcUA
GlcUAbeta(1-3)Galbeta(1-3)Galbeta(1-4)Xylbeta1-O-Ser + UDP
-
-
-
-
?
UDP-alpha-D-glucuronate + Galbeta1,3Galbeta-O-naphthalenemethanol
?
-
-
-
?
UDP-alpha-D-glucuronate + Galbeta1,3GalNAcbeta-O-naphthalenemethanol
?
-
-
-
?
UDP-alpha-D-glucuronate + [protein]-3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-serine
UDP + [protein]-3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine
-
-
-
?
UDP-Gal + Galbeta(1-3)Gal
Galbeta(1-3)Galbeta(1-3)Gal + UDP
no activity with wild-type enzyme, weak activity with mutant enzyme H308R
-
-
?
UDP-galacturonic acid + Galbeta(1-3)Gal
Galbeta(1-3)Galbeta(1-3)Gal + UDP
-
-
-
?
UDP-GlcNAc + Galbeta(1-3)Gal
GlcNAcbeta(1-3)Galbeta(1-3)Gal + UDP
no activity with wild-type enzyme, activity with mutant enzyme H308R is nearly equal to activity with UDP-Glc
-
-
?
UDP-glucose + galactosyl-1,3-thiogalactose
?
-
-
-
?
UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
UDP-glucuronate + Galbeta(1-3)Gal
GlcAbeta(1-3)Galbeta(1-3)Gal + UDP
-
-
-
?
UDP-glucuronate + Galbeta(1-3)Gal(6-sulfate)beta1-O-methoxyphenyl
UDP + ?
-
-
-
?
UDP-glucuronate + Galbeta(1-3)Gal-O-benzyl
UDP + ?
best substrate
-
-
?
UDP-glucuronate + Galbeta(1-3)Gal-O-naphthalenemethanol
UDP + ?
best substrate
-
-
?
UDP-glucuronate + Galbeta(1-3)Galbeta(1-4)Xyl
UDP + GlcAbeta(1-3)-Galbeta(1-3)Galbeta(1-4)Xyl
UDP-glucuronate + Galbeta(1-3)Galbeta(1-4)Xyl-1-O-Ser
UDP + GlcAbeta(1-3)Galbeta(1-3)Galbeta(1-4)Xyl-1-O-Ser
-
-
-
-
?
UDP-glucuronate + Galbeta(1-3)Galbeta1-O-methoxyphenyl
UDP + ?
-
-
-
?
UDP-glucuronate + Galbeta(1-3)GlcNAcalpha-O-benzyl
UDP + ?
-
-
-
?
UDP-glucuronate + Galbeta(1-3)GlcNAcalpha-O-naphthalenemethanol
UDP + ?
-
-
-
?
UDP-glucuronate + Galbeta(1-3)GlcNAcbeta-O-naphthalenemethanol
UDP + ?
-
-
-
?
UDP-glucuronate + Galbeta(1-4)Glcbeta-O-naphthalenemethanol
UDP + ?
-
-
-
?
UDP-glucuronate + Galbeta(1-4)GlcNAcbeta-O-naphthalenemethanol
UDP + ?
-
-
-
?
UDP-glucuronate + Galbeta-O-1-naphthol
UDP + GlcAbeta(1-3)Galbeta-O-1-naphthol
-
-
-
?
UDP-glucuronate + Galbeta-O-2-naphthol
UDP + GlcAbeta(1-3)Galbeta-O-2-naphthol
-
-
-
?
UDP-glucuronate + Galbeta1-3Gal
UDP + Galbeta1-3Galbeta1-3Gal
-
the enzyme exhibits a strict selectivity towards Galbeta1-3Gal structures
-
-
?
UDP-Man + Galbeta(1-3)Gal
Manbeta(1-3)Galbeta(1-3)Gal + UDP
no activity with wild-type enzyme, efficient reaction with mutant enzyme H308R
-
-
?
UDPglucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
?
UDPglucuronate + 3-beta-D-galactosyl-D-galactose
UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-D-galactose
UDPglucuronate + 3-beta-D-galactosyl-D-galactosyl-4-xylose
UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-D-galactosyl-4-xylose
-
-
-
?
UDPglucuronate + 3-beta-D-galactosyl-D-galactosyl-4-xylosylserine
UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-D-galactosyl-4-xylosylserine
-
-
-
?
additional information
?
-
UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
-
-
-
-
?
UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
-
plays a key role in glycosaminoglycan biosynthesis
-
-
?
UDP-glucuronate + Galbeta(1-3)Galbeta(1-4)Xyl
UDP + GlcAbeta(1-3)-Galbeta(1-3)Galbeta(1-4)Xyl
-
-
-
-
?
UDP-glucuronate + Galbeta(1-3)Galbeta(1-4)Xyl
UDP + GlcAbeta(1-3)-Galbeta(1-3)Galbeta(1-4)Xyl
-
high expression of the GlcAT-I gene renders the cells capable of synthesizing the HNK-1 epitope
-
-
?
UDPglucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
?
-
involved in the biosynthesis of the polysaccharide-protein-linkage region of proteochondroitin sulfate
-
-
?
UDPglucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
?
-
involved in the biosynthesis of the heparin-polypeptide linkage region
-
-
?
UDPglucuronate + 3-beta-D-galactosyl-D-galactose
UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-D-galactose
-
transfer to non-reducing terminal
-
?
UDPglucuronate + 3-beta-D-galactosyl-D-galactose
UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-D-galactose
-
-
-
?
additional information
?
-
-
mutant lacking glucuronosyltransferase I fails to make both heparan sulfate and chondroitin sulfate
-
-
?
additional information
?
-
no activity with Galalpha-O-p-nitrophenol, Galbeta-O-p-nitrophenol, Galalpha-O-a-naphthol, GalNAcalpha-O-p-nitrophenol, GalNAcbeta-O-p-nitrophenol
-
-
?
additional information
?
-
-
no activity with Galalpha-O-p-nitrophenol, Galbeta-O-p-nitrophenol, Galalpha-O-a-naphthol, GalNAcalpha-O-p-nitrophenol, GalNAcbeta-O-p-nitrophenol
-
-
?
additional information
?
-
analysis of glycan structure by mass spectrometry. Activity analysis of enzyme splicing variants, overview
-
-
-
additional information
?
-
-
the uridine diphosphate binding region plays an important role in enzyme activity of the enzyme
-
-
?
additional information
?
-
-
galactosyl-beta-1,6-galactose is a less effective acceptor substrate
-
-
?
additional information
?
-
-
galactosyl-beta-1,4-galactose is a less effective acceptor substrate
-
-
?
additional information
?
-
-
negligible activity with Galbeta(1-3)galbeta1-O-benzyl, galbeta(1-4)GlcNAc and galbeta(1-4)Glc
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans
-
-
?
additional information
?
-
the enzyme forms the glycosaminoglycan-protein linkage region, GlcAbeta(1-3)Galbeta(1-3)Galbeta(1-4)Xylbeta1-O-Ser, of the proteoglycans
-
-
?
additional information
?
-
-
the enzyme forms the glycosaminoglycan-protein linkage region, GlcAbeta(1-3)Galbeta(1-3)Galbeta(1-4)Xylbeta1-O-Ser, of the proteoglycans
-
-
?
additional information
?
-
-
enzyme is involved in heparan sulfate and chondroitin sulfate biosynthesis
-
-
?
additional information
?
-
-
central enzyme in the initial steps of proteoglycan synthesis
-
-
?
additional information
?
-
-
expressed in Pichia pastoris
-
-
?
additional information
?
-
enzyme plays a key role in proteoglycan biosynthesis by catalyzing the transfer of glucuronic acid onto the trisaccharide-protein linkage structure Galbeta(1-3)Galbeta(1-4)Xyl-O-Ser, a prerequisite step for polymerization of glycosaminoglycan chains
-
-
?
additional information
?
-
-
enzyme plays a key role in proteoglycan biosynthesis by catalyzing the transfer of glucuronic acid onto the trisaccharide-protein linkage structure Galbeta(1-3)Galbeta(1-4)Xyl-O-Ser, a prerequisite step for polymerization of glycosaminoglycan chains
-
-
?
additional information
?
-
the enzyme is responsible for the complementation of the glycosaminoglycan primer sequence
-
-
?
additional information
?
-
-
the enzyme is responsible for the complementation of the glycosaminoglycan primer sequence
-
-
?
additional information
?
-
no activity with wild-type enzyme: UDP-Glc, IDP-Gal, UDP-Man and UDP-GlcNAc
-
-
?
additional information
?
-
-
no activity with wild-type enzyme: UDP-Glc, IDP-Gal, UDP-Man and UDP-GlcNAc
-
-
?
additional information
?
-
-
no substrate Gal(6-O-sufate)beta(1-3)Galbeta(1-4)Xyl(2-O-phosphate)beta1-O-Ser
-
-
?
additional information
?
-
-
no substrate Gal(6-O-sufate)beta(1-3)Galbeta(1-4)Xylbeta1-O-Ser
-
-
?
additional information
?
-
-
galactosyl-beta-1,4-xylose, galactosyl-beta-1,4-glucose is a less effective acceptor substrate
-
-
?
additional information
?
-
-
galactosyl-beta-1,6-galactose is a less effective acceptor substrate
-
-
?
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UDP-alpha-D-glucuronate + [protein]-3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-serine
UDP + [protein]-3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine
-
-
-
?
UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
-
plays a key role in glycosaminoglycan biosynthesis
-
-
?
UDP-glucuronate + Galbeta(1-3)Galbeta(1-4)Xyl
UDP + GlcAbeta(1-3)-Galbeta(1-3)Galbeta(1-4)Xyl
-
high expression of the GlcAT-I gene renders the cells capable of synthesizing the HNK-1 epitope
-
-
?
UDP-glucuronate + Galbeta(1-3)Galbeta(1-4)Xyl-1-O-Ser
UDP + GlcAbeta(1-3)Galbeta(1-3)Galbeta(1-4)Xyl-1-O-Ser
-
-
-
-
?
UDPglucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
?
additional information
?
-
UDPglucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
?
-
involved in the biosynthesis of the polysaccharide-protein-linkage region of proteochondroitin sulfate
-
-
?
UDPglucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
?
-
involved in the biosynthesis of the heparin-polypeptide linkage region
-
-
?
additional information
?
-
-
mutant lacking glucuronosyltransferase I fails to make both heparan sulfate and chondroitin sulfate
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans
-
-
?
additional information
?
-
the enzyme forms the glycosaminoglycan-protein linkage region, GlcAbeta(1-3)Galbeta(1-3)Galbeta(1-4)Xylbeta1-O-Ser, of the proteoglycans
-
-
?
additional information
?
-
-
the enzyme forms the glycosaminoglycan-protein linkage region, GlcAbeta(1-3)Galbeta(1-3)Galbeta(1-4)Xylbeta1-O-Ser, of the proteoglycans
-
-
?
additional information
?
-
-
enzyme is involved in heparan sulfate and chondroitin sulfate biosynthesis
-
-
?
additional information
?
-
-
central enzyme in the initial steps of proteoglycan synthesis
-
-
?
additional information
?
-
-
expressed in Pichia pastoris
-
-
?
additional information
?
-
enzyme plays a key role in proteoglycan biosynthesis by catalyzing the transfer of glucuronic acid onto the trisaccharide-protein linkage structure Galbeta(1-3)Galbeta(1-4)Xyl-O-Ser, a prerequisite step for polymerization of glycosaminoglycan chains
-
-
?
additional information
?
-
-
enzyme plays a key role in proteoglycan biosynthesis by catalyzing the transfer of glucuronic acid onto the trisaccharide-protein linkage structure Galbeta(1-3)Galbeta(1-4)Xyl-O-Ser, a prerequisite step for polymerization of glycosaminoglycan chains
-
-
?
additional information
?
-
the enzyme is responsible for the complementation of the glycosaminoglycan primer sequence
-
-
?
additional information
?
-
-
the enzyme is responsible for the complementation of the glycosaminoglycan primer sequence
-
-
?
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0.0091
3-beta-galactosyl-galactose
-
-
0.035
Galbeta(1-3)Gal(6-O-sulfate)beta(1-4)Xyl(2-O-phosphate)beta1-O-Ser
-
pH 6.5, 2 mM MnCl2, 37°C
0.049
Galbeta(1-3)Gal(6-O-sulfate)beta(1-4)Xylbeta1-O-Ser
-
pH 6.5, 2 mM MnCl2, 37°C
0.0804
Galbeta(1-3)Galbeta(1-4)Xyl
-
-
0.025
Galbeta(1-3)Galbeta(1-4)Xyl(2-O-phosphate)beta1-O-Ser
-
pH 6.5, 2 mM MnCl2, 37°C
0.046
Galbeta(1-3)Galbeta(1-4)Xylbeta1-O-Ser
-
pH 6.5, 2 mM MnCl2, 37°C
0.67
Galbeta1,3Galbeta-O-naphthalenemethanol
pH 6.5, 37°C
3.2
Galbeta1,3GalNAcbeta-O-naphthalenemethanol
pH 6.5, 37°C
2.9
Galbeta1,3GlcNAcbeta-O-naphthalenemethanol
pH 6.5, 37°C
1.8
Galbeta1,4GlcNAcbeta-O-naphthalenemethanol
pH 6.5, 37°C
4.48
Galbeta1-3Gal
-
37°C, pH 6.5
0.108
UDP-GlcNAc
pH 5.0, 37°C, mutant enzyme H308R
0.233
UDP-glucose
pH 5.0, 37°C, mutant enzyme H308R
0.04 - 1.27
UDP-glucuronate
0.074
UDP-Man
pH 5.0, 37°C, mutant enzyme H308R
0.00025 - 0.287
UDPglucuronate
additional information
additional information
-
-
-
0.0499
UDP-GlcA
pH 5.0, 37°C, mutant enzyme H308R
0.059
UDP-GlcA
pH 5.0, 37°C, wild-type enzyme
0.04
UDP-glucuronate
-
37°C, pH 6.5, mutant enzyme R310Q
0.06
UDP-glucuronate
-
37°C, pH 6.5, mutant enzyme R310K
0.06
UDP-glucuronate
-
37°C, pH 6.5, wild-type enzyme
0.14
UDP-glucuronate
-
37°C, pH 6.5, mutant enzyme Y84H
0.18
UDP-glucuronate
-
37°C, pH 6.5, mutant enzyme Y84F
0.19
UDP-glucuronate
-
37°C, pH 6.5, mutant enzyme D113E
0.21
UDP-glucuronate
-
37°C, pH 6.5, mutant enzyme R310A
0.6
UDP-glucuronate
-
37°C, pH 6.5
0.76
UDP-glucuronate
-
37°C, pH 6.5, mutant enzyme D113N
1.27
UDP-glucuronate
-
37°C, pH 6.5, mutant enzyme R161K
0.00025
UDPglucuronate
-
-
0.0293
UDPglucuronate
-
-
0.09489
UDPglucuronate
-
wild-type enzyme
0.287
UDPglucuronate
-
mutant enzyme C33A
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V111M
-
mutation renders glycosaminoglycan biosynthesis temperature-sensitive, greater synthesis at 33°C compared with 37°C
C301A
-
mutant is not N-glycosylated, molecular weight is about 4000 Da less than that of the wild-type protein, enzyme is completely inactive
C33A
-
mutation abolishes the ability of the protein to form dimers
D113A
-
inactive mutant enzyme. Mutant enzyme is produced in a slightly lower amount compared with the wild-type enzyme
D113E
-
KM-value for UDP-glucuronate is 3.2fold higher than wild-type value
D113N
-
KM-value for UDP-glucuronate is 12.7fold higher than wild-type value
D194A
about 85% of wild-type activity
D194A/D195A
inactive mutant protein
D194A/D196A
inactive mutant protein
D194E
about 85% of wild-type activity
D195A
about 25% of wild-type activity
D195A/D196A
inactive mutant protein
D195E
about 30% of wild-type activity
D196A
about 30% of wild-type activity
D196E
about 25% of wild-type activity
G222A
activity towards Galbeta(1-3)Galbeta1-O-methoxyphenyl is reduced 3.7fold and activity towards Galbeta(1-3)Gal(6-sulfate)beta1-O-methoxyphenyl is reduced 7.1fold
G222A/G223A
nearly complete loss of activity towards Galbeta(1-3)Galbeta1-O-methoxyphenyl and Galbeta(1-3)Gal(6-sulfate)beta1-O-methoxyphenyl
G223a
nearly complete loss of activity towards Galbeta(1-3)Galbeta1-O-methoxyphenyl and Galbeta(1-3)Gal(6-sulfate)beta1-O-methoxyphenyl
H308A
mutation abrogates the activity towards UDP-GlcA
H308R
mutation induces a major change in specificity. In contrast to wild-type enzyme the mutant is able to efficiently transfer Glc from UDP-Glc onto acceptor substrate Galbeta(1-3)Gal. The mutant enzyme remains able to catalyze the transfer of GlcA from UDP-GlyA onto Galbeta(1-3)Gal. UDP-GlcNAc is used at about the same rate as UDP-Glc. UDP-Gal is a weak donor substrate. UDP-Man is efficiently used as cosubstrate. No activity with GDP-Man
H308R/R277A
mutant enzyme shows no activity with UDP-GlcA as donor substrate, mutant enzyme is active with UDP-Gly as donor
K317A
complete loss of activity towards Galbeta(1-3)Galbeta1-O-methoxyphenyl and Galbeta(1-3)Gal(6-sulfate)beta1-O-methoxyphenyl
K317R
activity towards Galbeta(1-3)Galbeta1-O-methoxyphenyl is reduced 7.2fold and activity towards Galbeta(1-3)Gal(6-sulfate)beta1-O-methoxyphenyl is reduced 6.5fold
Q318A
activity towards Galbeta(1-3)Galbeta1-O-methoxyphenyl is reduced 1.4fold and activity towards Galbeta(1-3)Gal(6-sulfate)beta1-O-methoxyphenyl is nearly identical to wild-type enzyme
R156A
-
inactive mutant enzyme
R156K
-
inactive mutant enzyme
R161A
-
inactive mutant enzyme
R161K
-
KM-value for UDP-glucuronate is 21.2fold higher than wild-type value
R310A
-
KM-value for UDP-glucuronate is 3.5fold higher than wild-type value
R310K
-
KM-value for UDP-glucuronate is identical to wild-type value
R310Q
-
KM-value for UDP-glucuronate is 1.5fold lower than wild-type value
W243A
inactive mutant protein
W243F
activity towards Galbeta(1-3)Galbeta1-O-methoxyphenyl is reduced 12fold and activity towards Galbeta(1-3)Gal(6-sulfate)beta1-O-methoxyphenyl is reduced 29fold
Y84A
-
inactive mutant enzyme, slightly less expressed than wild-type enzyme
Y84F
-
mutant enzyme shows 60% of wild-type activity. Mutant enzyme is produced at higher level than the wild-type protein. KM-value for UDP-glucuronate is 3fold higher than wild-type value
Y84H
-
mutant retains 21% of the activity with a KM value double that of the wild type. KM-value for UDP-glucuronate is 2.3fold higher than wild-type value
additional information
creation of dGlcAT-P null mutants, mutant larvae show lower expression of glucuronylated T antigen on the muscles and at NMJs. Mislocalization of neuromuscular junction (NMJ) boutons and a partial loss of the basement membrane components collagen IV (Col IV) and nidogen (Ndg) at the muscle 6/7 boundary are observed. Those two phenotypes are correlated and identical to previously described phenotypes in dC1GalT1 mutant larvae. In addition, dGlcAT-P null mutants exhibit fewer NMJ branches on muscles 6/7. Ultrastructural analysis reveals that basement membranes that lacks Col IV and Ndg are significantly deformed. The loss of dGlcAT-P expression causes ultrastructural defects in NMJ boutons
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Helting, T.; Roden, L.
Biosynthesis of chondroitin sulfate. II. Glucuronosyl transfer in the formation of the carbohydrate-protein linkage region
J. Biol. Chem.
244
2799-2805
1969
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