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Literature summary for 5.1.2.2 extracted from

  • St Maurice, M.; Bearne, S.L.
    Hydrophobic nature of the active site of mandelate racemase (2004), Biochemistry, 43, 2524-2532.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
(R,S)-1-naphthylglycolate competitive Pseudomonas putida
(R,S)-2-naphthylglycolate
-
Pseudomonas putida
2-naphthohydroxamate
-
Pseudomonas putida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.41
-
(S)-2-naphthylglycolate 25°C, pH 7.5 Pseudomonas putida
0.46
-
(R)-2-naphthylglycolate 25°C, pH 7.5 Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida P11444
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-2-naphthylglycolate
-
Pseudomonas putida (S)-2-naphthylglycolate
-
?
(R)-mandelate
-
Pseudomonas putida (S)-mandelate
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
25
-
(S)-2-naphthylglycolate 25°C, pH 7.5 Pseudomonas putida
33
-
(R)-2-naphthylglycolate 25°C, pH 7.5 Pseudomonas putida

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.057
-
2-naphthohydroxamate 25°C, pH 7.5 Pseudomonas putida
0.52
-
(R,S)-2-naphthylglycolate 25°C, pH 7.5 Pseudomonas putida
1.9
-
(R,S)-1-naphthylglycolate 25°C, pH 7.5 Pseudomonas putida