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Results 1 - 6 of 6
EC Number Protein Variants Commentary Reference
Show all pathways known for 4.1.2.40Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.40K124A strongly reduced aldolase activity 679492
Show all pathways known for 4.1.2.40Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.40K204A mutation results in more than 98% decrease in aldolase activity 679492
Show all pathways known for 4.1.2.40Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.40L165E the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate 715040
Show all pathways known for 4.1.2.40Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.40L165E/L275S the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate 715040
Show all pathways known for 4.1.2.40Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.40L275S the mutant shows enhanced substrate specificity toward fructose-1,6-bisphosphate 715040
Show all pathways known for 4.1.2.40Display the word mapDisplay the reaction diagram Show all sequences 4.1.2.40more construction of chimeras of isoforms LacD.1 and LacD.2. The C-terminus of LacD.1 contributes to its differential enzymatic activity, as replacing of its C-terminal half with 162 amino acid residues from the C-terminus of LacD.2 leads to an enzyme very similarly to LacD.2 in the cleavage of tagatose bisphosphate but over 3 times more efficient than LacD.2 at cleaving fructose bisphosphate. In addition, loop 1 and turn 2 influence the differential enzymatic activity of LacD.1 -, 727768
Results 1 - 6 of 6