Protein Variants | Comment | Organism |
---|---|---|
S124A | mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values of Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively | Escherichia coli |
S124T | mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values of Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively | Escherichia coli |
S124V | mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values of Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively | Escherichia coli |
Y149F | mutant forms Y149F, S124A, S124V, and S124T. The least active mutant is Y149F, with a turnover number 0.010% of that for the wild type enzyme. The activity of S124A is also very low, with a turnover number 0.035% of that of the wild type enzyme. The Km values form Y149F and S124A are 12% and 21% of that of the wild type enzyme, respectively. The turnover number for S124T is about 30% of that of the wild type enzyme, and the Km value is similar. Second-order rate constants for reductive inactivation by NaBH3CN are similar to that for the wild type enzyme in the cases of S124A, S124T, and S124V. Y149F reacts with NaBH3- 12-20fold faster than the wild type enzyme at pH 8.5 and 7.0, respectively | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.026 | - |
UDPgalactose | mutant Y149F | Escherichia coli | |
0.048 | - |
UDPgalactose | mutant S124A | Escherichia coli | |
0.225 | - |
UDPgalactose | wild type enzyme | Escherichia coli | |
0.256 | - |
UDPgalactose | mutant S124T | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
wild type and mutant enzymes Y149F, S124A, S124V, and S124T | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-galactose | - |
Escherichia coli | UDP-glucose | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.073 | - |
UDPgalactose | mutant Y149F | Escherichia coli | |
0.265 | - |
UDPgalactose | ,mutant S124A | Escherichia coli | |
248 | - |
UDPgalactose | mutant S124T | Escherichia coli | |
760 | - |
UDPgalactose | wild type enzyme | Escherichia coli |