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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.23 D105A site-directed mutagenesis, the mutant shows 50% reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.23 E154D site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.23 E154K site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 90% reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.23 E154L site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 70% reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.23 N169A site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 50% reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.23 N169D site-directed mutagenesis in the GlcNAc-binding region, the mutant shows unaltered activity compared to the wild-type enzyme Escherichia coli
2.7.7.23 N169Q site-directed mutagenesis in the GlcNAc-binding region, the mutant shows unaltered activity compared to the wild-type enzyme Escherichia coli
2.7.7.23 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
2.7.7.23 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
2.7.7.23 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
2.7.7.23 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
2.7.7.23 T82G site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 65% reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.23 T82Q site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.23 T82S site-directed mutagenesis in the GlcNAc-binding region, the mutant shows about 80% reduced activity compared to the wild-type enzyme Escherichia coli
2.7.7.23 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

EC Number Metals/Ions Comment Organism Structure
2.7.7.23 Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.23 Escherichia coli P0ACC7
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.23 CTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Escherichia coli diphosphate + CDP-N-acetyl-alpha-D-glucosamine
-
 ?
2.7.7.23 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 ?
-
 ?
2.7.7.23 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 Escherichia coli diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
 ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.23 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.23 7.5
-
 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
2.7.7.23 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
2.7.7.23 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
2.7.7.23 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