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Results 1 - 10 of 24 > >>
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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.1C17S visible and CD spectra are very similar to that of the wild-type domain, thermal stability is slightly decreased compared to the wild-type domain 392915
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.1C191A enzyme is still produced, but it is inactive 392921
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.1C191S enzyme is still produced, but it is inactive 392921
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.1C240A decrease of diaphorase activity 392915
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.1C240G decrease of diaphorase activity 392915
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.1C240S decrease of diaphorase activity, thermal stability is slightly decreased compared to the wild-type domain, the oxidation reduction midpoint potential for the FAD/FADH2 couple is -219 mV compared to -268 mV in the wild-type domain 392915
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.1C54S visible and CD spectra are very similar to that of the wild-type domain, thermal stability is slightly decreased compared to the wild-type domain,the oxidation reduction midpoint potential for the FAD/FADH2 couple is -197 mV compared to -268 mV in the wild-type domain 392915
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.1C62S visible and CD spectra are very similar to that of the wild-type domain, thermal stability is decreased compared to the wild-type domain, the oxidation reduction midpoint potential for the FAD/FADH2 couple is -226 mV compared to -268 mV in the wild-type domain 392915
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.1K714A functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order 392917
Display the word mapDisplay the reaction diagram Show all sequences 1.7.1.1K741E functional flavoprotein which retains FAD as the sole prosthetic group and exhibits spectroscopic properties comparable to that of the wild-type enzyme. Altered NADH:ferricyanide reductase activity with mutations affecting both turnover number and the Km-value for NADH. At pH 7.0 the turnover number decreases in the order wild-type, K741R, K741A, K741H, K741E, K741M, K741Q. Km-value for NADH increases in the same order 392917
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