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Literature summary for 2.3.1.242 extracted from
- A triple mutant of Escherichia coli lacking secondary acyl chains on lipid A (2002), J. Biol. Chem., 277, 14194-14205.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0ACV2 | - |
- |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | strains lacking lpxP fail to incorporate palmitoleate into their lipid A at 12°C but make normal amounts of hexa-acylated lipid A and are viable. MKV15, an Eschertichia coli lpxL lpxM lpxP triple mutant, that grows slowly on minimal medium at all temperatures but not on nutrient broth at any temperature. MKV15 synthesizes a lipid A molecule containing only the four primary (R)-3-hydroxymyristoyl chains. The outer membrane localization and content of lipid A are nearly normal in MKV15, as is the glycerophospholipid and membrane protein composition. However, the rate at which the tetra-acylated lipid A of MKV15 is exported to the outer membrane is reduced compared with wild type. The integrity of the outer membrane of MKV15 is compromised, as judged by antibiotic hypersensitivity, and MKV15 undergoes lysis following centrifugation. MKV15 may prove useful as a host strain for expressing late acyltransferase genes from other Gram-negative bacteria, facilitating the re-engineering of lipid A structure in living cells and the design of novel vaccines | Escherichia coli |
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