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Literature summary extracted from

  • Nagar, M.; Narmandakh, A.; Khalak, Y.; Bearne, S.L.
    Redefining the minimal substrate tolerance of mandelate racemase. Racemization of trifluorolactate (2011), Biochemistry, 50, 8846-8852.
    View publication on PubMed

Activating Compound

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.2.2 overexpression in Escherichia coli strain BL21(DE3) Pseudomonas putida

KM Value [mM]

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.2.2 Mg2+ dependent on Pseudomonas putida

Natural Substrates/ Products (Substrates)

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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.1.2.2 Pseudomonas putida P11444
-
-

Substrates and Products (Substrate)

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 ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.2.2 25
-
 assay at Pseudomonas putida

Turnover Number [1/s]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.2.2 7.5
-
 assay at Pseudomonas putida

kcat/KM [mM/s]

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