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Literature summary for 2.7.7.23 extracted from

  • Mengin-Lecreulx, D.; van Heijenoort, J.
    Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis (1994), J. Bacteriol., 176, 5788-5795.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
overexpression in host strain Escherichia coli

General Stability

General Stability Organism
completely insensitive to millimolar concentrations of thiol reagents Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
UDP-N-acetyl-D-glucosamine slight product inhibition in reverse reaction Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
 N-acetyl-D-glucosamine 1-phosphate pH 8.2, 37°C Escherichia coli
0.1
-
 UTP pH 8.2, 37°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for maximum activity Escherichia coli
Mg2+ optimum activity at 3 mM Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49000
-
 SDS-PAGE, corresponds very well with molecular weight expected from DNA sequence Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diphosphate + UDP-N-acetyl-D-glucosamine Escherichia coli amino sugar metabolism UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r
diphosphate + UDP-N-acetyl-D-glucosamine Escherichia coli involved in synthesis of peptidoglycan and lipopolysaccharide UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r
diphosphate + UDP-N-acetyl-D-glucosamine Escherichia coli JM83 amino sugar metabolism UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
15.1
-
 purified enzyme, pH 8.2, 37°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + UDP-N-acetyl-D-glucosamine
-
 Escherichia coli UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r
diphosphate + UDP-N-acetyl-D-glucosamine amino sugar metabolism Escherichia coli UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r
diphosphate + UDP-N-acetyl-D-glucosamine involved in synthesis of peptidoglycan and lipopolysaccharide Escherichia coli UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r
diphosphate + UDP-N-acetyl-D-glucosamine
-
 Escherichia coli JM83 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r
diphosphate + UDP-N-acetyl-D-glucosamine amino sugar metabolism Escherichia coli JM83 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
 r

Synonyms

Synonyms Comment Organism
More acetyltransferase 5 times higher than uridyltransferase activity Escherichia coli
More bifunctional enzyme with activity of: glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
-
-
 Escherichia coli