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Results 1 - 10 of 98 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.20.1.1more 12 x PTDH mutant, saturation mutagenesis performed separately on each of the following residues in the parent PTDH template: V71, E130, Q132, Q137, I150, Q215, R275, L276, I313, V315, A319, and A325. The most thermostabilizing mutation discovered for each particular site is incorporated into the 12 x PTDH mutant, performed for K132, H137, L275, and C276, forming an optimized thermally stable phosphite dehydrogenase termed Opt12. Addition of A146S to Opt12 leads to the Opt13 variant, and the further addition of F198M leads to Opt14 691424
Display the word mapDisplay the reaction diagram Show all sequences 1.20.1.1H292F almost complete loss of activity 658120
Display the word mapDisplay the reaction diagram Show all sequences 1.20.1.1H292K almost complete loss of activity 658120
Display the word mapDisplay the reaction diagram Show all sequences 1.20.1.1H292N almost complete loss of activity -, 658120
Display the word mapDisplay the reaction diagram Show all sequences 1.20.1.1R237H almost complete loss of activity 658120
Display the word mapDisplay the reaction diagram Show all sequences 1.20.1.1R237L almost complete loss of activity 658120
Display the word mapDisplay the reaction diagram Show all sequences 1.20.1.1R237Q almost complete loss of activity 658120
Display the word mapDisplay the reaction diagram Show all sequences 1.20.1.1E175A/A176R double mutant, 3.6-fold higher efficiency with NAD+, 1000-fold higher efficiency with NADP+, 3-fold favor for NADP+ over NAD+ as cofactor -, 657956, 658259
Display the word mapDisplay the reaction diagram Show all sequences 1.20.1.1D79N has kinetic parameters more similar to those of wild-type 690884
Display the word mapDisplay the reaction diagram Show all sequences 1.20.1.1E266Q higher activity, steady-state and pre-steady-state rates are comparable -, 690884
Results 1 - 10 of 98 > >>