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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
outer membrane | - |
Escherichia coli | 19867 | - |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P10441 | - |
- |
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 | Comment | Organism |
---|---|---|
LpxB | - |
Escherichia coli |
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 |