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Literature summary for 2.3.1.157 extracted from

  • Pompeo, F.; Bourne, Y.; Van Heijenoort, J.; Fassy, F.; Mengin-Lecreulx, D.
    Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth (2001), J. Biol. Chem., 276, 3833-3839.
    View publication on PubMed
Search for more literature for 2.3.1.157

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24700
-
 1 * 37100 + 1 * 24700, uridyltransferase and acetyltransferase in separate domains, SDS-PAGE Escherichia coli
37100
-
 1 * 37100 + 1 * 24700, uridyltransferase and acetyltransferase in separate domains, SDS-PAGE Escherichia coli
50100
-
-
 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 Escherichia coli
-
 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
Escherichia coli
-
 JM83
-
Escherichia coli JM83
-
 JM83
-

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
0.004
-
 mutant JM83(pFP3-Tr331), acetyltransferase activity Escherichia coli
0.014
-
 mutant JM83(pTrcHis30), uridyltransferase activity Escherichia coli
0.11
-
 mutant JM83(pTrcHis30), acetyltransferase activity Escherichia coli
0.12
-
 mutant JM83(pFP3-Tr331), uridyltransferase activity Escherichia coli
2.85
-
 mutant JM83(pFP3-Tr331) + IPTG, uridyltransferase activity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucosamine 1-phosphate + acetyl-CoA
-
 Escherichia coli 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 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

Subunits

Subunits Comment Organism
trimer 1 * 37100 + 1 * 24700, uridyltransferase and acetyltransferase in separate domains, SDS-PAGE Escherichia coli

Synonyms

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