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Literature summary for 2.7.7.23 extracted from

  • Olsen, L.R.; Roderick, S.L.
    Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites (2001), Biochemistry, 40, 1913-1921.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ binds to enzyme 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

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ACC7
-
-

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

Subunits

Subunits Comment Organism
trimer
-
Escherichia coli

Synonyms

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