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Results 1 - 10 of 10
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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4C102S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent 14932
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4C12S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent 14932
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4C29S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent 14932
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4C33S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent 14932
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4C36S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent 14932
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4C94S mutant enzymes C12S, C94S, C102S display full holoactivase activity, albeit absolute values are slightly lower, by a factor of 2 than the value of the wild type enzyme. Mutant enzymes C29S, C33S and C36S are catalytically incompetent 14932
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4D104A site-directed mutagenesis, mutation of the cation binding site, the D104A variant has very low activity in presence of KCl compared to the wild-type, S-adenosyl-L-methionine does not bind well in this variant 745175
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4D129A site-directed mutagenesis, mutation of the cation binding site, the mutant retains the ability to bind cations, the variant binds M+ and SAM in a manner similar to wild-type 745175
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4more for activity assay, the enzyme PFL-AE is attached to a CM5 sensor chip using standard thiol coupling procedures 745316
Display the word mapDisplay the reaction diagram Show all sequences 1.97.1.4more recombinant coexpression of the enzyme with pyruvate format lyase and flavodoxin or ferredoxin in Saccharomyces cerevisiae leads to over 20fold increased expression of endogenous formate dehydrogenases FDH1 and FDH2 744943
Results 1 - 10 of 10
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