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Literature summary for 2.4.1.182 extracted from

  • Emiola, A.; George, J.; Andrews, S.S.
    A complete pathway model for lipid A biosynthesis in Escherichia coli (2014), PLoS ONE, 10, e0121216.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information bi-substrate Michaelis-Menten kinetics for enzyme LpxB, overview Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
outer membrane
-
Escherichia coli 19867
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli LpxB combines lipid X with the preceding lipid metabolite, UDP-2,3-bis(beta-hydroxymyristoyl)-D-glucosamine, to form lipid A disaccharide ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P10441
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information LpxB combines lipid X with the preceding lipid metabolite, UDP-2,3-bis(beta-hydroxymyristoyl)-D-glucosamine, to form lipid A disaccharide Escherichia coli ?
-
?
additional information LpxB only consumes lipid X in a 1:1 ratio with UDP-2,3-bis(beta-hydroxymyristoyl)-D-glucosamine. Near irreversibility of the LpxB enzyme Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
LpxB
-
Escherichia coli

General Information

General Information Comment Organism
metabolism the enzyme is involved in the lipid A biosynthesis catalyzing the fifth step, LpxH and LpxB may form a complex that performs metabolic channeling. LpxB combines lipid X with the preceding lipid metabolite, UDP-2,3-bis(beta-hydroxymyristoyl)-D-glucosamine, to form lipid A disaccharide. Development of a quantitative model of the nine enzyme-catalyzed steps of Escherichia coli lipid A biosynthesis, modelling, detailed overview Escherichia coli