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Synonyms
glcat-i, glcat-p, glcat-1, glucuronosyltransferase i, beta1,3-glucuronosyltransferase i, glucuronyltransferase-i, glcuat-i, glcati, beta-1,3-glucuronyltransferase 1, beta1,3-glucuronosyltransferase-i,
more
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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 + Galbeta(1-3)Gal
GlcAbeta(1-3)Galbeta(1-3)Gal + UDP
-
-
-
?
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
-
-
?
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-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)Gal(6-sulfate)beta1-O-methoxyphenyl
UDP + ?
-
-
-
?
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)Galbeta1-O-methoxyphenyl
UDP + ?
-
-
-
?
UDP-glucuronate + Galbeta1-3Gal
UDP + Galbeta1-3Galbeta1-3Gal
-
the enzyme exhibits a strict selectivity towards Galbeta1-3Gal structures
-
-
?
additional information
?
-
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
-
-
?
additional information
?
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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
?
-
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
?
-
-
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
?
-
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 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
-
-
?
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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
-
-
?
additional information
?
-
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 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
?
-
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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0.108
UDP-GlcNAc
pH 5.0, 37°C, mutant enzyme H308R
0.233
UDP-glucose
pH 5.0, 37°C, mutant enzyme H308R
0.074
UDP-Man
pH 5.0, 37°C, mutant enzyme H308R
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
4.48
Galbeta1-3Gal
-
37°C, pH 6.5
0.04 - 1.27
UDP-glucuronate
0.0293 - 0.287
UDPglucuronate
additional information
additional information
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-
-
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
0.0293
UDPglucuronate
-
-
0.09489
UDPglucuronate
-
wild-type enzyme
0.287
UDPglucuronate
-
mutant enzyme C33A
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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
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
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
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
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
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Pedersen, L.C.; Darden, T.A.; Negishi, M.
Crystal structure of beta 1,3-glucuronyltransferase I in complex with active donor substrate UDP-GlcUA
J. Biol. Chem.
277
21869-21873
2002
Homo sapiens
brenda
Tone, Y.; Kitagawa, H.; Imiya, K.; Oka, S.; Kawasaki, T.; Sugahara, K.
Characterization of recombinant human glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans
FEBS Lett.
459
415-420
1999
Homo sapiens
brenda
Pedersen, L.C.; Tsuchida, K.; Kitagawa, H.; Sugahara, K.; Darden, T.A.; Negishi, M.
Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I
J. Biol. Chem.
275
34580-34585
2000
Homo sapiens
brenda
Ouzzine, M.; Gulberti, S.; Netter, P.; Magdalou, J.; Fournel-Gigleux, S.
Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues
J. Biol. Chem.
275
28254-28260
2000
Homo sapiens
brenda
Kitagawa, H.; Tone, Y.; Tamura, J.; Neumann, K.W.; Ogawa, T.; Oka, S.; Kawasaki, T.; Sugahara, K.
Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans
J. Biol. Chem.
273
6615-6618
1998
Homo sapiens (O94766), Homo sapiens
brenda
Negishi, M.; Dong, J.; Darden, T.A.; Pedersen, L.G.; Pedersen, L.C.
Glucosaminylglycan biosynthesis: what we can learn from the X-ray crystal structures of glycosyltransferases GlcAT1 and EXTL2
Biochem. Biophys. Res. Commun.
303
393-398
2003
Homo sapiens
brenda
Kitagawa, H.; Taoka, M.; Tone, Y.; Sugahara, K.
Human glycosaminoglycan glucuronyltransferase I gene and a related processed pseudogene: genomic structure, chromosomal mapping and characterization
Biochem. J.
358
539-546
2001
Homo sapiens (Q9P2W7), Homo sapiens
brenda
Ouzzine, M.; Gulberti, S.; Levoin, N.; Netter, P.; Magdalou, J.; Fournel-Gigleux, S.
The donor substrate specificity of the human beta1,3-glucuronosyltransferase I toward UDP-glucuronic acid is determined by two crucial histidine and arginine residues
J. Biol. Chem.
277
25439-25445
2002
Homo sapiens (Q9P2W7), Homo sapiens
brenda
Gulberti, S.; Fournel-Gigleux, S.; Mulliert, G.; Aubry, A.; Netter, P.; Magdalou, J.; Ouzzine, M.
The functional glycosyltransferase signature sequence of the human beta 1,3-glucuronosyltransferase is a XDD motif
J. Biol. Chem.
278
32219-32226
2003
Homo sapiens (Q9P2W7), Homo sapiens
brenda
Gulberti, S.; Lattard, V.; Fondeur, M.; Jacquinet, J.C.; Mulliert, G.; Netter, P.; Magdalou, J.; Ouzzine, M.; Fournel-Gigleux, S.
Phosphorylation and sulfation of oligosaccharide substrates critically influence the activity of human beta1,4-galactosyltransferase 7 (GalT-I) and beta1,3-glucuronosyltransferase I (GlcAT-I) involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans
J. Biol. Chem.
280
1417-1425
2005
Homo sapiens (O94766), Homo sapiens
brenda
Lattard, V.; Fondeur-Gelinotte, M.; Gulberti, S.; Jacquinet, J.C.; Boudrant, J.; Netter, P.; Magdalou, J.; Ouzzine, M.; Fournel-Gigleux, S.
Purification and characterization of a soluble form of the recombinant human galactose-beta1,3-glucuronosyltransferase I expressed in the yeast Pichia pastoris
Protein Expr. Purif.
47
137-143
2006
Homo sapiens
brenda
Fondeur-Gelinotte, M.; Lattard, V.; Oriol, R.; Mollicone, R.; Jacquinet, J.C.; Mulliert, G.; Gulberti, S.; Netter, P.; Magdalou, J.; Ouzzine, M.; Fournel-Gigleux, S.
Phylogenetic and mutational analyses reveal key residues for UDP-glucuronic acid binding and activity of beta1,3-glucuronosyltransferase I (GlcAT-I)
Protein Sci.
15
1667-1678
2006
Homo sapiens
brenda
Tone, Y.; Pedersen, L.C.; Yamamoto, T.; Izumikawa, T.; Kitagawa, H.; Nishihara, J.; Tamura, J.; Negishi, M.; Sugahara, K.
2-o-phosphorylation of xylose and 6-o-sulfation of galactose in the protein linkage region of glycosaminoglycans influence the glucuronyltransferase-I activity involved in the linkage region synthesis
J. Biol. Chem.
283
16801-16807
2008
Homo sapiens
brenda