EC Number | Crystallization (Comment) | Organism |
---|---|---|
5.1.2.2 | - |
Pseudomonas putida |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
5.1.2.2 | H297N | H297N has no detectable mandelate racemase activity. However, H297N catalyzes the stereospecific elimination of Br- from racemic p-(bromomethyl)mandelate to give p-(methyl)benzoylformate in 45% yield at a rate equal to that measured for wild type enzyme | Pseudomonas putida |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.2.2 | Pseudomonas putida | - |
mutant gene H297N overexpressed in Pseudomonas aeruginosa | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
5.1.2.2 | (S)-mandelate = (R)-mandelate | reaction proceeds via a two-base mechanism in which Lys166 abstracts the alpha-proton from (S)-mandelate and His297 abstracts the alpha-proton from (R)-mandelate | Pseudomonas putida | |
5.1.2.2 | (S)-mandelate = (R)-mandelate | the enzyme contains two distinct general acid/base catalysts: Lys166 which abstracts the alpha-proton from (S)-mandelate, and His297, which abstracts the alpha-proton from (R)-mandelate | Pseudomonas putida |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.2.2 | D-mandelate | - |
Pseudomonas putida | L-mandelate | - |
? | |
5.1.2.2 | p-(bromomethyl)mandelate | - |
Pseudomonas putida | p-(methyl)benzoylformate + Br- | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.2.2 | additional information | - |
additional information | dependence of turnover number on pH | Pseudomonas putida |