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Literature summary for 2.7.7.23 extracted from

  • Brown, K.; Pompeo, F.; Dixon, S.; Mengin-Lecreulx, D.; Cambillau, C.; Bourne, Y.
    Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily (1999), EMBO J., 18, 4096-4107.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.23

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Escherichia coli 5737
-

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

Organism

Organism UniProt Comment Textmining
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

Synonyms

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