Protein Variants | Comment | Organism |
---|---|---|
D270N | structure of D270N with (S)-atrolactate bound in the active site reveals no geometric alterations when compared to the structure of the wild type enzyme complexed with (S)-atrolactate, with the exception that the side chain of His297 is tilted and displaced about 0.5A away from Asn270 and towards the (S)-atrolactate. The turnover number for both (R)-mandelate and (S)-mandelate are reduced 10000fold | Pseudomonas putida |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.5 | - |
(R)-mandelate | D270N mutant | Pseudomonas putida | |
2.1 | - |
(S)-Mandelate | D270N mutant | Pseudomonas putida |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | P11444 | wild type and mutant D270N | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(S)-mandelate = (R)-mandelate | His297 and Asp270 function together as a catalytic dyad | Pseudomonas putida |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-mandelate | - |
Pseudomonas putida | L-mandelate | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | dependence of turnover number on pH | Pseudomonas putida | |
0.018 | - |
(R)-mandelate | D270N mutant | Pseudomonas putida | |
0.037 | - |
(S)-Mandelate | D270N mutant | Pseudomonas putida | |
0.21 | - |
(R)-mandelate | mutant K166R | Pseudomonas putida |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | 8.5 | wild type enzyme | Pseudomonas putida |