EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.2.1.46 | K164A | 15fold increase in Km-value for dTDP-glucose, 820fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 34fold decrease in turnover-number for dTDP-glucose | Escherichia coli |
4.2.1.46 | K164M | 8.7fold increase in Km-value for dTDP-glucose, 837fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 96fold decrease in turnover-number for dTDP-glucose | Escherichia coli |
4.2.1.46 | T134A | 1.2fold increase in Km-value for dTDP-glucose, 283fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 233fold decrease in turnover-number for dTDP-glucose | Escherichia coli |
4.2.1.46 | T134S | 3.7fold increase in Km-value for dTDP-glucose, 7.5fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 2fold decrease in turnover-number for dTDP-glucose | Escherichia coli |
4.2.1.46 | T134V | 3.3fold increase in Km-value for dTDP-glucose, 788fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 237fold decrease in turnover-number for dTDP-glucose | Escherichia coli |
4.2.1.46 | Y160A | 2.8fold increase in Km-value for dTDP-glucose, 683fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 247fold decrease in turnover-number for dTDP-glucose | Escherichia coli |
4.2.1.46 | Y160F | 1.2fold increase in Km-value for dTDP-glucose, 234fold decrease in ratio of turnover number to Km-value for dTDP-glucose, 190fold decrease in turnover-number for dTDP-glucose | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.46 | 0.006 | - |
dTDP-glucose | pH 7.5, 37°C, wild-type enzyme | Escherichia coli | |
4.2.1.46 | 0.007 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme T134A | Escherichia coli | |
4.2.1.46 | 0.0073 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme Y160F | Escherichia coli | |
4.2.1.46 | 0.017 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme Y160A | Escherichia coli | |
4.2.1.46 | 0.02 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme T134V | Escherichia coli | |
4.2.1.46 | 0.022 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme T134S | Escherichia coli | |
4.2.1.46 | 0.052 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme K164M | Escherichia coli | |
4.2.1.46 | 0.09 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme K164A | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.46 | Escherichia coli | P27830 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.46 | dTDP-glucose | - |
Escherichia coli | dTDP-4-dehydro-6-deoxy-D-glucose + H2O | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.46 | 0.0198 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme Y160A | Escherichia coli | |
4.2.1.46 | 0.0207 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme T134V | Escherichia coli | |
4.2.1.46 | 0.021 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme T134A | Escherichia coli | |
4.2.1.46 | 0.0258 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme Y160F | Escherichia coli | |
4.2.1.46 | 0.051 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme K164M | Escherichia coli | |
4.2.1.46 | 0.14 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme K164A | Escherichia coli | |
4.2.1.46 | 2.4 | - |
dTDP-glucose | pH 7.5, 37°C, mutant enzyme T134S | Escherichia coli | |
4.2.1.46 | 4.9 | - |
dTDP-glucose | pH 7.5, 37°C, wild-type enzyme | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.46 | NADH | purified enzyme contains coenzyme in the reduced form. The bound NADH is oxidized to NAD+ by adding dTDP-4-keto-6-deoxyglucose. When all the coenzyme is in the oxidized form, the dTDP-sugars remove from the enzyme. In the Y160A variant, almost 98% of the coenzyme is tightly bound NADH. Variants K164M, T134V and Y160F contain 62%, 56% and 35% of bound NADH respectively | Escherichia coli |