Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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]

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

Localization

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.182 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

EC Number Organism UniProt Comment Textmining
2.3.1.191 Escherichia coli
-
-
-
2.4.1.182 Escherichia coli P10441
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.182 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 ?
-
 ?
2.4.1.182 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

EC Number Synonyms Comment Organism
2.4.1.182 LpxB
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.3.1.191 metabolism quantitative model of the nine enzyme-catalyzed steps of Escherichia coli lipid A biosynthesis. Biosynthesis regulation occurs through regulated degradation of the LpxC and WaaA enzymes. LpxC, EC 3.5.1.108, is the rate-limiting enzyme if pathway regulation is ignored, but LpxK, EC 2.7.1.130, is the rate-limiting enzyme if pathway regulation is present, as it is in real cells Escherichia coli
2.4.1.182 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