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Literature summary extracted from

  • Kallarakal, A.T.; Mitra, B.; Kozarich, J.W.; Gerlt, J.A.; Clifton, J.G.; Petsko, G.A.; Kenyon, G.L.
    Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant (1995), Biochemistry, 34, 2788-2797.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.2.2 of mutant K166R Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
5.1.2.2 K166E K166R retains low level of racemase activity. K166R mutant catalyzes the elimination of Br- from only the (R)-enantiomer of (R,S)-p-(bromomethyl)mandelate Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.2.2 0.34
-
 (R)-mandelate wild type Pseudomonas putida
5.1.2.2 0.35
-
 (S)-Mandelate wild type Pseudomonas putida
5.1.2.2 0.59
-
 (S)-Mandelate mutant K166R Pseudomonas putida
5.1.2.2 1.4
-
 (S)-Mandelate mutant K166R Pseudomonas putida

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.2.2 wild type and mutant K166R Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.2.2 D-mandelate
-
 Pseudomonas putida L-mandelate
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.2.2 0.46
-
 (S)-Mandelate mutant K166R Pseudomonas putida
5.1.2.2 480
-
 (R)-mandelate wild type enzyme Pseudomonas putida