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EC Number Cloned (Commentary)
Show all pathways known for 2.7.6.3Display the word mapDisplay the reaction diagram Show all sequences 2.7.6.3bifunctional protein 6-hydroxymethyl-7,8-dihydroxypterin pyrophosphokinase/7,8-dihydropteroate synthase is involved in tetrahydrofolate expressed in Escherichia coli
Show all pathways known for 2.7.6.3Display the word mapDisplay the reaction diagram Show all sequences 2.7.6.3expressed in Escherichia coli BL21 cells
Show all pathways known for 2.7.6.3Display the word mapDisplay the reaction diagram Show all sequences 2.7.6.3expressed in Escherichia coli BL21(DE3) cells
Show all pathways known for 2.7.6.3Display the word mapDisplay the reaction diagram Show all sequences 2.7.6.3expression in Escherichia coli
Show all pathways known for 2.7.6.3Display the word mapDisplay the reaction diagram Show all sequences 2.7.6.3expression in Escherichia coli and Saccharomyces cerevisiae
Show all pathways known for 2.7.6.3Display the word mapDisplay the reaction diagram Show all sequences 2.7.6.3expression of His6-tagged enzyme in Escherichia coli
Show all pathways known for 2.7.6.3Display the word mapDisplay the reaction diagram Show all sequences 2.7.6.3expression of His6-tagged maltose-binding-protein fusion HPPK in Escherichia coli strain BL21(DE3)
Show all pathways known for 2.7.6.3Display the word mapDisplay the reaction diagram Show all sequences 2.7.6.3expression of the bifunctional 6-hydroxymethyl-7,8-dihydropterin diphosphokinase/dihydropteroate synthase in Escherichia coli
Show all pathways known for 2.7.6.3Display the word mapDisplay the reaction diagram Show all sequences 2.7.6.3gene folK, sequence comparisons, recombinant expression of His6-tagged and maltose-binding-protein-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
Show all pathways known for 2.7.6.3Display the word mapDisplay the reaction diagram Show all sequences 2.7.6.3hydroxymethyldihydropterin diphosphokinase from Plasmodium falciparum complements a folK-knockout mutant in Escherichia coli when expressed as a separate polypeptide detached from dihydropteroate synthase. Hydroxymethyldihydropterin diphosphokinase part of the bifunctional protein can function by itself but that a larger part of the polypeptide is needed to ensure full functionality
Results 1 - 10 of 14 > >>