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Literature summary for 2.3.1.157 extracted from

  • Pompeo, F.; Van Heijenoort, J.; Mengin-Lecreulx, D.
    Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes (1998), J. Bacteriol., 180, 4799-4803.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.157

General Stability

General Stability Organism
acetyl-CoA protects from inactivation Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
2-Nitro-5-thiocyanobenzoic acid
-
 Escherichia coli
DTNB
-
 Escherichia coli
iodoacetamide
-
 Escherichia coli
N-ethylmaleimide
-
 Escherichia coli
p-hydroxymercuribenzoate
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
 D-glucosamine 1-phosphate mutant His6-GlmU C296A Escherichia coli
0.09
-
 acetyl-CoA mutant His6-GlmU C307A Escherichia coli
0.12
-
 D-glucosamine 1-phosphate mutant His6-GlmU C324A Escherichia coli
0.14
-
 acetyl-CoA mutant His6-GlmU C324A Escherichia coli
0.15
-
 D-glucosamine 1-phosphate
-
 Escherichia coli
0.2
-
 D-glucosamine 1-phosphate mutant His6GlmU Escherichia coli
0.2
-
 acetyl-CoA mutant His6GlmU, mutant His6-GlmU C296A, mutant His6-GlmU C385A Escherichia coli
0.25
-
 D-glucosamine 1-phosphate mutant His6-GlmU C307A Escherichia coli
0.25
-
 acetyl-CoA mutant His6-GlmU C385A Escherichia coli
0.6
-
 acetyl-CoA
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucosamine 1-phosphate + acetyl-CoA Bacillus subtilis
-
 N-acetyl-D-glucosamine 1-phosphate + CoA
-
 ?
D-glucosamine 1-phosphate + acetyl-CoA Escherichia coli
-
 N-acetyl-D-glucosamine 1-phosphate + CoA
-
 ?
D-glucosamine 1-phosphate + acetyl-CoA Neisseria gonorrhoeae
-
 N-acetyl-D-glucosamine 1-phosphate + CoA
-
 ?
D-glucosamine 1-phosphate + acetyl-CoA Escherichia coli JM83
-
 N-acetyl-D-glucosamine 1-phosphate + CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Escherichia coli
-
 JM83
-
Escherichia coli JM83
-
 JM83
-
Neisseria gonorrhoeae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucosamine 1-phosphate + acetyl-CoA
-
 Bacillus subtilis N-acetyl-D-glucosamine 1-phosphate + CoA
-
 ?
D-glucosamine 1-phosphate + acetyl-CoA
-
 Escherichia coli N-acetyl-D-glucosamine 1-phosphate + CoA
-
 ?
D-glucosamine 1-phosphate + acetyl-CoA
-
 Neisseria gonorrhoeae N-acetyl-D-glucosamine 1-phosphate + CoA
-
 ?
D-glucosamine 1-phosphate + acetyl-CoA
-
 Escherichia coli JM83 N-acetyl-D-glucosamine 1-phosphate + CoA
-
 ?
N-acetyl-D-glucosamine 1-phosphate + UTP
-
 Bacillus subtilis UDP-N-acetylglucosamine + ?
-
 ?
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
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

Synonyms

Synonyms Comment Organism
bifunctional GlmU protein
-
 Escherichia coli
GlcNAc-1-P uridyltransferase
-
 Bacillus subtilis
GlcNAc-1-P uridyltransferase
-
 Escherichia coli
GlcNAc-1-P uridyltransferase
-
 Neisseria gonorrhoeae
GlmU enzyme
-
 Escherichia coli