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Literature summary for 2.4.99.12 extracted from
- Replacement of lipopolysaccharide with free lipid A molecules in Escherichia coli mutants lacking all core sugars (2009), Biochemistry, 48, 9627-9640.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Kdo transferase | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | kdtA deletion mutants are viable when lpxL and lpxM (the lauroyl- or the myristoyltransferase of lipid A biosynthesis) are overexpressed, encoded by deletion of kdtA in strains overexpressing LpxM causes accumulation of pentaacylated lipid A with a secondary myristate moiety. None of the strains lacking kdtA grow in the presence of bile salts at any temperature or on nutrient broth at 42°C | Escherichia coli |
| physiological function | the main function of Kdo transferase is to provide the right substrates for the acyltransferases LpxL and LpxM, resulting in the synthesis of penta- and hexaacylated lipid A, which is optimal for the MsbA flippase | Escherichia coli |
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Release 2023.1 (January 2023)
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