EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
5.1.2.2 | sucrose | higher viscosity by addition of up to 35% sucrose elevates the enzyme activity | Pseudomonas putida |
EC Number | Cloned (Comment) | Organism |
---|---|---|
5.1.2.2 | overexpression in Escherichia coli strain BL21(DE3) | Pseudomonas putida |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.2.2 | additional information | - |
additional information | Michaelis-Menten kinetics | Pseudomonas putida | |
5.1.2.2 | 1 | - |
(S)-Mandelate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida | |
5.1.2.2 | 1.2 | - |
(R)-mandelate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida | |
5.1.2.2 | 1.2 | - |
(R)-trifluorolactate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida | |
5.1.2.2 | 1.74 | - |
(S)-trifluorolactate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
5.1.2.2 | Mg2+ | dependent on | Pseudomonas putida |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.2.2 | (S)-mandelate | Pseudomonas putida | - |
(R)-mandelate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.2.2 | Pseudomonas putida | P11444 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.2.2 | (R)-trifluorolactate | racemization | Pseudomonas putida | trifluorolactate | - |
? | |
5.1.2.2 | (S)-mandelate | - |
Pseudomonas putida | (R)-mandelate | - |
? | |
5.1.2.2 | (S)-trifluorolactate | racemization | Pseudomonas putida | (R)-trifluorolactate | - |
? | |
5.1.2.2 | additional information | substrate recognition and binding method, overview. Mandelate racemase from Pseudomonas putida catalyzes the interconversion of the enantiomers of mandelic acid and a variety of aryl- and heteroaryl-substituted mandelate derivatives. beta,gamma-Unsaturation is not an absolute requirement for catalysis and that mandelate racemase can bind and catalyze the racemization of (S)- and (R)-trifluorolactate. The enzyme catalyzes hydrogen-deuterium exchange at the alpha-postion of trifluorolactate | Pseudomonas putida | ? | - |
? |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
5.1.2.2 | 25 | - |
assay at | Pseudomonas putida |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.2.2 | 2 | - |
(R)-trifluorolactate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida | |
5.1.2.2 | 2.5 | - |
(S)-trifluorolactate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida | |
5.1.2.2 | 637 | - |
(S)-Mandelate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida | |
5.1.2.2 | 792 | - |
(R)-mandelate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
5.1.2.2 | 7.5 | - |
assay at | Pseudomonas putida |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.2.2 | 1.4 | - |
(S)-trifluorolactate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida | |
5.1.2.2 | 1.6 | - |
(R)-trifluorolactate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida | |
5.1.2.2 | 620 | - |
(S)-Mandelate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida | |
5.1.2.2 | 650 | - |
(R)-mandelate | pH 7.5, 25°C, recombinant wild-type enzyme | Pseudomonas putida |