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Literature summary for 5.1.3.14 extracted from

  • Blume, A.; Benie, A.J.; Stolz, F.; Schmidt, R.R.; Reutter, W.; Hinderlich, S.; Peters, T.
    Characterization of ligand binding to the bifunctional key enzyme in the sialic acid biosynthesis by NMR: I. Investigation of the UDP-GlcNAc 2-epimerase functionality (2004), J. Biol. Chem., 279, 55715-55721.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-D-glucosamine Rattus norvegicus key enzyme of sialic acid biosynthesis UDP-N-acetyl-D-mannosamine
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Purification (Commentary)

Purification (Comment) Organism
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Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-D-glucosamine key enzyme of sialic acid biosynthesis Rattus norvegicus UDP-N-acetyl-D-mannosamine
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?
UDP-N-acetyl-D-glucosamine characterization of ligand binding to the bifunctional enzyme Rattus norvegicus UDP-N-acetyl-D-mannosamine
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Synonyms

Synonyms Comment Organism
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase bifunctional Rattus norvegicus