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Literature summary extracted from

  • Steeghs, L.; Jennings, M.P.; Poolman, J.T.; van der Ley, P.
    Isolation and characterization of the Neisseria meningitidis lpxD-fabZ-lpxA gene cluster involved in lipid A biosynthesis (1997), Gene, 190, 263-270.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.191 by complementation of a temperature-sensitive Escherichia coli lpxD mutant, a meningococcal chromosomal fragment is cloned that carries the lpxD homologue Neisseria meningitidis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.191 (3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine Neisseria meningitidis a comparison of the lipid A structures shows that in Escherichia coli and Neisseria meningitidis, LpxD can be expected to have the same specificity, both adding 3-hydroxymyristoyl chains UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
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Organism

EC Number Organism UniProt Comment Textmining
2.3.1.191 Neisseria meningitidis P95377
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.191 (3R)-3-hydroxymyristoyl-[acyl-carrier protein] + UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine a comparison of the lipid A structures shows that in Escherichia coli and Neisseria meningitidis, LpxD can be expected to have the same specificity, both adding 3-hydroxymyristoyl chains Neisseria meningitidis UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + holo-[acyl-carrier protein]
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