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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.23 overexpression in host strain Escherichia coli

General Stability

EC Number General Stability Organism
2.3.1.157 acetyltransferase activity rapidly lost when the enzyme is stored in the absence of reducing thiols or acetyl coenzyme A or is treated with thiol-alkylating agents Escherichia coli
2.7.7.23 completely insensitive to millimolar concentrations of thiol reagents Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.157 2-Nitro-5-thiocyanobenzoic acid
-
Escherichia coli
2.3.1.157 DTNB
-
Escherichia coli
2.3.1.157 N-acetylglucosamine-1-phosphate acetyltransferase activity inhibited by its reaction product Escherichia coli
2.3.1.157 UDP-MurNAc 1 mM, relative enzyme activity 2% Escherichia coli
2.7.7.23 UDP-N-acetyl-D-glucosamine slight product inhibition in reverse reaction Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.157 0.07
-
N-acetyl-D-glucosamine 1-phosphate uridyltransferase activity Escherichia coli
2.3.1.157 0.1
-
UTP uridyltransferase activity Escherichia coli
2.3.1.157 0.15
-
D-glucosamine 1-phosphate
-
Escherichia coli
2.3.1.157 0.6
-
acetyl-CoA
-
Escherichia coli
2.7.7.23 0.07
-
N-acetyl-D-glucosamine 1-phosphate pH 8.2, 37°C Escherichia coli
2.7.7.23 0.1
-
UTP pH 8.2, 37°C Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.1.157 Mg2+ absolute requirement for both activities in the sharp range from 1-10 mM with an optimal value of 3 mM Escherichia coli
2.7.7.23 Mg2+ required for maximum activity Escherichia coli
2.7.7.23 Mg2+ optimum activity at 3 mM Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.157 49000
-
gel filtration Escherichia coli
2.7.7.23 49000
-
SDS-PAGE, corresponds very well with molecular weight expected from DNA sequence Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.157 Bacillus subtilis
-
-
-
2.3.1.157 Escherichia coli
-
JM83
-
2.3.1.157 Escherichia coli JM83
-
JM83
-
2.7.7.23 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.157 GlmU gene product, bifunctional enzyme with glucosamine-1-phosphate acetyltransferase and uridyltransferase activity Escherichia coli
2.7.7.23
-
Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.157 acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate the enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.157 2.2
-
GlcN-1-P acetyltransferase activity Escherichia coli
2.3.1.157 15.1
-
GlcNAc-1-P uridyltransferase activity Escherichia coli
2.7.7.23 15.1
-
purified enzyme, pH 8.2, 37°C Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.157 D-glucosamine 1-phosphate + acetyl-CoA
-
Bacillus subtilis N-acetyl-D-glucosamine 1-phosphate + CoA
-
?
2.3.1.157 D-glucosamine 1-phosphate + acetyl-CoA
-
Escherichia coli N-acetyl-D-glucosamine 1-phosphate + CoA
-
?
2.3.1.157 D-glucosamine 1-phosphate + acetyl-CoA
-
Escherichia coli JM83 N-acetyl-D-glucosamine 1-phosphate + CoA
-
?
2.3.1.157 N-acetyl-D-glucosamine 1-phosphate + UTP
-
Bacillus subtilis UDP-N-acetylglucosamine + ?
-
?
2.3.1.157 N-acetyl-D-glucosamine 1-phosphate + UTP glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis Escherichia coli UDP-N-acetylglucosamine + ?
-
r
2.3.1.157 N-acetyl-D-glucosamine 1-phosphate + UTP glmU gene product, bifunctional enzyme catalyzing 2 subsequent steps in the pathway for UDP-GlcNAc synthesis Escherichia coli JM83 UDP-N-acetylglucosamine + ?
-
r
2.3.1.157 UDP-N-acetyl-alpha-D-glucosamine + H2O
-
Escherichia coli N-acetyl-D-glucosamine 1-phosphate + UMP
-
r
2.3.1.157 UDP-N-acetyl-alpha-D-glucosamine + H2O
-
Escherichia coli JM83 N-acetyl-D-glucosamine 1-phosphate + UMP
-
r
2.7.7.23 diphosphate + UDP-N-acetyl-D-glucosamine
-
Escherichia coli UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r
2.7.7.23 diphosphate + UDP-N-acetyl-D-glucosamine amino sugar metabolism Escherichia coli UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r
2.7.7.23 diphosphate + UDP-N-acetyl-D-glucosamine involved in synthesis of peptidoglycan and lipopolysaccharide Escherichia coli UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r
2.7.7.23 diphosphate + UDP-N-acetyl-D-glucosamine
-
Escherichia coli JM83 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r
2.7.7.23 diphosphate + UDP-N-acetyl-D-glucosamine amino sugar metabolism Escherichia coli JM83 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r

Subunits

EC Number Subunits Comment Organism
2.3.1.157 trimer 2 * 49000 or 3 * 49000, dimer or trimer of identical subunits, gel filtration Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.3.1.157 GlmU enzyme
-
Escherichia coli
2.3.1.157 GlmU uridyltransferase
-
Escherichia coli
2.3.1.157 UDP-GlcNAc pyrophosphorylase
-
Escherichia coli
2.7.7.23 More acetyltransferase 5 times higher than uridyltransferase activity Escherichia coli
2.7.7.23 More bifunctional enzyme with activity of: glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.157 12.4
-
N-acetyl-D-glucosamine 1-phosphate GmlU uridyltransferase Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.157 8.2
-
for both acetyltransferase and uridyltransferase Escherichia coli
2.7.7.23 8.2
-
-
Escherichia coli