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Literature summary for 5.1.2.2 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)

Crystallization (Comment) Organism
of mutant K166R Pseudomonas putida

Protein Variants

Protein Variants Comment Organism
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]

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

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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