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Results 1 - 10 of 13 > >>
EC Number General Information Commentary Reference
Show all pathways known for 3.5.1.108Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.108metabolism a model for the biosynthesis of the outer membrane in Escherichia coli is presented. Lipopolysaccharide is an endotoxin that elicits a strong immune response from humans, and its biosynthesis is in part regulated via degradation of LpxC and WaaA enzymes by the protease FtsH. Addition of palmitic acid to the growth medium of wild-type Escherichia coli elevates the levels of LpxC by 1.7fold. Palmitoyl-CoA induces a strong inhibitory effect on FabI. Due to the inhibition of FabI, LpxC would be stabilized. Thus, elevated cellular palmitoyl-CoA concentrations has an opposite effect on LpxC stability than the free-form of palmitic acid -, 760065
Show all pathways known for 3.5.1.108Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.108metabolism essential enzyme in Gram-negative bacteria 752972
Show all pathways known for 3.5.1.108Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.108metabolism first committed step in the biosynthesis of lipid A 754390
Show all pathways known for 3.5.1.108Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.108metabolism LpxC enzyme catalyzes the committed step of lipopolysaccharide biosynthesis 734239
Show all pathways known for 3.5.1.108Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.108metabolism the enzyme catalyzes the first committed step of biosynthesis of lipid A 735205
Show all pathways known for 3.5.1.108Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.108metabolism the enzyme catalyzes the first committed step of lipid A biosynthesis -, 753359
Show all pathways known for 3.5.1.108Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.108metabolism the enzyme plays an important role in the biosynthesis of lipid A 735298, 735299
Show all pathways known for 3.5.1.108Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.108metabolism the membrane-anchored FtsH protease is essential in Escherichia coli as it adjusts the cellular amount of LpxC, the key enzyme in lipopolysaccharide biosynthesis. Both accumulation and depletion of LpxC are toxic to Escherichia coli. By continuous proteolysis of LpxC, FtsH maintains a low concentration of LpxC and, hence, the proper equilibrium between lipopolysaccharide and phospholipids. The C terminus of LpxC is required for turnover. Detailed mutational analysis revealed six non-polar residues in the C terminus of LpxC that are critical for degradation -, 681452
Show all pathways known for 3.5.1.108Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.108more cocrystal structure of Aquifex aeolicus LpxC with bound UDP-3-O-(acyl)-glucosamine and Pseudomonas aeruginosa with bound 27b docking model, overview 732992
Show all pathways known for 3.5.1.108Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.108more cocrystal structure of Aquifex aeolicus LpxC with bound UDP-3-O-(acyl)-glucosamine and Pseudomonas. aeruginosa with bound 27b docking model, overview 732992
Results 1 - 10 of 13 > >>