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Literature summary for 2.3.1.129 extracted from

  • Raetz, C.R.H.; Roderick, S.L.
    A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase (1995), Science, 270, 997-1000.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine Escherichia coli involved with EC 2.4.1.182 and 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid and outer membrane component, Lipid A [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine involved with EC 2.4.1.182 and 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid and outer membrane component, Lipid A Escherichia coli [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
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?
(R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N-acetyl-alpha-D-glucosamine
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Escherichia coli [acyl-carrier protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine
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?