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Literature summary for 2.4.1.135 extracted from

  • 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 (2002), J. Biol. Chem., 277, 25439-25445.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Homo sapiens

Protein Variants

Protein Variants Comment Organism
H308A mutation abrogates the activity towards UDP-GlcA Homo sapiens
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 Homo sapiens
H308R/R277A mutant enzyme shows no activity with UDP-GlcA as donor substrate, mutant enzyme is active with UDP-Gly as donor Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2,3-Butanedione irreversible. UDP-glucuronic acid protects, no protection by UDP-glucose. Activity of H308R towards UDP-glucose is unaffected by the reagent Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0499
-
UDP-GlcA pH 5.0, 37°C, mutant enzyme H308R Homo sapiens
0.059
-
UDP-GlcA pH 5.0, 37°C, wild-type enzyme Homo sapiens
0.074
-
UDP-Man pH 5.0, 37°C, mutant enzyme H308R Homo sapiens
0.108
-
UDP-GlcNAc pH 5.0, 37°C, mutant enzyme H308R Homo sapiens
0.233
-
UDP-glucose pH 5.0, 37°C, mutant enzyme H308R Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens 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 ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9P2W7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Homo sapiens ?
-
?
additional information no activity with wild-type enzyme: UDP-Glc, IDP-Gal, UDP-Man and UDP-GlcNAc Homo sapiens ?
-
?
UDP-Gal + Galbeta(1-3)Gal no activity with wild-type enzyme, weak activity with mutant enzyme H308R Homo sapiens Galbeta(1-3)Galbeta(1-3)Gal + UDP
-
?
UDP-galacturonic acid + Galbeta(1-3)Gal
-
Homo sapiens Galbeta(1-3)Galbeta(1-3)Gal + UDP
-
?
UDP-GlcNAc + Galbeta(1-3)Gal no activity with wild-type enzyme, activity with mutant enzyme H308R is nearly equal to activity with UDP-Glc Homo sapiens GlcNAcbeta(1-3)Galbeta(1-3)Gal + UDP
-
?
UDP-glucose + galactosyl-1,3-thiogalactose
-
Homo sapiens ?
-
?
UDP-glucuronate + Galbeta(1-3)Gal
-
Homo sapiens GlcAbeta(1-3)Galbeta(1-3)Gal + UDP
-
?
UDP-Man + Galbeta(1-3)Gal no activity with wild-type enzyme, efficient reaction with mutant enzyme H308R Homo sapiens Manbeta(1-3)Galbeta(1-3)Gal + UDP
-
?

Synonyms

Synonyms Comment Organism
beta1,3-glucuronosyltransferase I
-
Homo sapiens
GlcAT-I
-
Homo sapiens