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Literature summary for 2.3.1.241 extracted from
- Site-specific acylation changes in the lipid A of Escherichia coli lpxL mutants grown at high temperatures (2014), Innate Immun., 20, 269-282.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| htrB | - |
Escherichia coli |
| LpxL | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | at 37°C and 42°C, lpxL mutants appear to activate different acyltransferases or biosynthetic pathways that generate atypical penta- and hexaacyl lipid A structures by incorporating longer fatty acids, such as a secondary palmitoleic acid (2'-O-position, distal) and a secondary palmitic acid (2-O-position, proximal), respectively. E.scherichia coli (lpxL) lipid A biosynthesis, and specifically the late acylation of lipid A, is temperature dependent and highly regulated | Escherichia coli |
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Release 2023.1 (January 2023)
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