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Results 1 - 8 of 8
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 5.1.3.20D210N mutant display activity similar to that of the wild type 672239
Display the word mapDisplay the reaction diagram Show all sequences 5.1.3.20E210G site-directed mutagenesis, structure compared to the wild-type enzyme -, 726590
Display the word mapDisplay the reaction diagram Show all sequences 5.1.3.20K178M mutant has severely compromised epimerase activities that are more than 3 orders of magnitude lower than that of the wild type 672239
Display the word mapDisplay the reaction diagram Show all sequences 5.1.3.20K178M site-directed mutagenesis, structure compared to the wild-type enzyme -, 726590
Display the word mapDisplay the reaction diagram Show all sequences 5.1.3.20K208M mutant display activity similar to that of the wild type 672239
Display the word mapDisplay the reaction diagram Show all sequences 5.1.3.20more construction of the mutant Escherichia coli strains WBB06 and WJW00, that can synthesize Kdo2-lipid A, by deleting the rfaD gene from the genome of Escherichia coli wild-type strain W3110. 3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo)2-lipid A is the conserved structure domain of lipopolysaccharide found in most Gram-negative bacteria, and is believed to stimulate the human innate immune system through the TLR4/MD2 complex. Kdo2-lipid A is an important stimulator for studying the mechanism of the innate immune system and for developing bacterial vaccine adjuvants. Compared with the wild-type strain W3110, WJW00 shows increased hydrophobicity, higher cell permeability, greater autoaggregation and decreased biofilm-forming ability -, 748527
Display the word mapDisplay the reaction diagram Show all sequences 5.1.3.20Y140F mutant has severely compromised epimerase activities that are more than 3 orders of magnitude lower than that of the wild type 672239
Display the word mapDisplay the reaction diagram Show all sequences 5.1.3.20Y140F the mutant shows 0.08% epimerase activity compared to the wild type enzyme 716848
Results 1 - 8 of 8