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Literature summary for 2.7.7.23 extracted from

  • Wang, S.; Fu, X.; Liu, Y.; Liu, X.W.; Wang, L.; Fang, J.; Wang, P.G.
    Probing the roles of conserved residues in uridyltransferase domain ofEscherichia coli K12 GlmU by site-directed mutagenesis (2015), Carbohydr. Res., 413, 70-74.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
D105A site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme Escherichia coli
E154D site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme Escherichia coli
E154K site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 90% reduced activity compared to the wild-type enzyme Escherichia coli
E154L site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 70% reduced activity compared to the wild-type enzyme Escherichia coli
N169A site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 50% reduced activity compared to the wild-type enzyme Escherichia coli
N169D site-directed mutagenesis in the GlcNAc-binding region, the mutant shows unaltered activity compared to the wild-type enzyme Escherichia coli
N169Q site-directed mutagenesis in the GlcNAc-binding region, the mutant shows unaltered activity compared to the wild-type enzyme Escherichia coli
N169R site-directed mutagenesis in the GlcNAc-binding region, the mutant shows 1.4fold increased activity compared to the wild-type enzyme. The N169R mutant caused a slightly secondary structure changes, thus facilitating GlcNAc-1-phosphate to enter the active pocket through the additional interaction with N-acetyl arm of GlcNAc moiety Escherichia coli
Q76A site-directed mutagenesis in the uridine-binding region, the mutant has a catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc which is distinct from the wild-type, altered nucleotide specificity compared to wild-type, overview Escherichia coli
Q76E site-directed mutagenesis in the uridine-binding region, the mutant has a catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc which is distinct from the wild-type, altered nucleotide specificity compared to wild-type, overview Escherichia coli
Q76P site-directed mutagenesis in the uridine-binding region, the mutant has a catalytic activity to convert CTP and GlcNAc-1P into unnatural sugar nucleotide CDP-GlcNAc which is distinct from the wild-type, altered nucleotide specificity compared to wild-type, overview Escherichia coli
T82G site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 65% reduced activity compared to the wild-type enzyme Escherichia coli
T82Q site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme Escherichia coli
T82S site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme Escherichia coli
Y103F site-directed mutagenesis of the residue located nearby the uridyltransferase active pocket,the mutant shows increased activity compared to the wild-type enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Escherichia coli
-
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ACC7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
Escherichia coli diphosphate + CDP-N-acetyl-alpha-D-glucosamine
-
?
additional information the uridyltransferase domain of GlmU exhibits a flexible substrate specificity, roles of several highly conserved amino acid residues involved in substrate binding and recognition, overview. Besides UTP, the enzyme also shows activity with CTP, ATP, and slightly with dATP Escherichia coli ?
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
Escherichia coli diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
?

Synonyms

Synonyms Comment Organism
GlmU
-
Escherichia coli
N-acetylglucosamine-1-phosphate uridyltransferase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli

General Information

General Information Comment Organism
metabolism N-acetylglucosamine-1-phosphate uridyltransferase is a bifunctional enzyme that catalyzes both acetyltransfer and uridyltransfer reactions in the prokaryotic UDP-GlcNAc biosynthesis pathway Escherichia coli
additional information the Tyr103-Asp105 segment is located at the floor of the uridyltransferase active pocket and is involved in interactions with UTP and GlcNAc-1-P substrates Escherichia coli
physiological function N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme, its N- and C-terminal domains catalyze uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively. Final product of GlmU catalyzed reaction Escherichia coli