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Literature summary extracted from

  • Siddiqi, F.; Bourque, J.R.; Jiang, H.; Gardner, M.; St Maurice, M.; Blouin, C.; Bearne, S.L.
    Perturbing the hydrophobic pocket of mandelate racemase to probe phenyl motion during catalysis (2005), Biochemistry, 44, 9013-9021.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
5.1.2.2 F52W compared to wild-type enzyme the catalytic preference of the mutant enzyme is reversed and catalytic efficiency is reduced. Mutant enzyme exhibits higher affinity for (R)-mandelate than for (S)-mandelate, and a higher turnover number with (S)-mandelate as the substrate, relative to that with (R)-mandelate Pseudomonas putida
5.1.2.2 F52W/Y54W compared to wild-type enzyme the catalytic preference of the mutant enzyme is reversed and catalytic efficiency is reduced. Mutant enzyme exhibits higher affinity for (R)-mandelate than for (S)-mandelate, and a higher turnover number with (S)-mandelate as the substrate, relative to that with (R)-mandelate Pseudomonas putida
5.1.2.2 Y54Q compared to wild-type enzyme the catalytic preference of the mutant enzyme is reversed and catalytic efficiency is reduced. Mutant enzyme exhibits higher affinity for (R)-mandelate than for (S)-mandelate, and a higher turnover number with (S)-mandelate as the substrate, relative to that with (R)-mandelate Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.2.2 (R)-2-hydroxybutyrate
-
 Pseudomonas putida
5.1.2.2 (R)-2-naphthylglycolate
-
 Pseudomonas putida
5.1.2.2 (S)-2-hydroxybutyrate
-
 Pseudomonas putida
5.1.2.2 (S)-2-naphthylglycolate
-
 Pseudomonas putida
5.1.2.2 (S)-cyclohexylphenylglycolate
-
 Pseudomonas putida
5.1.2.2 benzilate
-
 Pseudomonas putida
5.1.2.2 diphenylacetate
-
 Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.2.2 0.29
-
 (R)-mandelate mutant enzyme F52W/Y64W Pseudomonas putida
5.1.2.2 0.35
-
 (R)-2-naphthylglycolate mutant enzyme F52W/Y54W Pseudomonas putida
5.1.2.2 0.41
-
 (S)-2-naphthylglycolate wild-type enzyme Pseudomonas putida
5.1.2.2 0.46
-
 (R)-2-naphthylglycolate wild-type enzyme Pseudomonas putida
5.1.2.2 0.54
-
 (S)-Mandelate wild-type enzyme Pseudomonas putida
5.1.2.2 0.7
-
 (R)-mandelate wild-type enzyme Pseudomonas putida
5.1.2.2 1.1
-
 (R)-mandelate mutant enzyme Y54W Pseudomonas putida
5.1.2.2 1.5
-
 (S)-2-naphthylglycolate mutant enzyme F52W/Y54W Pseudomonas putida
5.1.2.2 2.5
-
 (R)-mandelate mutant enzyme F52W Pseudomonas putida
5.1.2.2 2.9
-
 (S)-Mandelate mutant enzyme Y54W Pseudomonas putida
5.1.2.2 3.3
-
 (S)-Mandelate mutant enzyme F52W Pseudomonas putida
5.1.2.2 3.8
-
 (S)-Mandelate mutant enzyme F52W/Y64W Pseudomonas putida

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)-2-naphthylglycolate
-
 Pseudomonas putida (S)-2-naphthylglycolate
-
 r
5.1.2.2 (R)-mandelate wild-type enzyme shows slightly higher affinity for (S)-mandelate than for (R)-mandelate, but catalyzes the turnover of (R)-mandelate slightly more rapidly Pseudomonas putida (S)-mandelate
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1.2.2 1
-
 (R)-mandelate mutant enzyme F52W/Y64W Pseudomonas putida
5.1.2.2 2 8 (S)-Mandelate mutant enzyme Y54W Pseudomonas putida
5.1.2.2 10
-
 (R)-mandelate mutant enzyme Y54W Pseudomonas putida
5.1.2.2 12
-
 (S)-Mandelate mutant enzyme F52W/Y64W Pseudomonas putida
5.1.2.2 159
-
 (R)-mandelate mutant enzyme F52W Pseudomonas putida
5.1.2.2 248
-
 (S)-Mandelate mutant enzyme F52W Pseudomonas putida
5.1.2.2 467
-
 (S)-Mandelate wild-type enzyme Pseudomonas putida
5.1.2.2 526
-
 (R)-mandelate wild-type enzyme Pseudomonas putida

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
5.1.2.2 0.16
-
 (R)-2-naphthylglycolate mutant enzyme F52W/Y54W Pseudomonas putida
5.1.2.2 0.48
-
 (S)-2-naphthylglycolate mutant enzyme F52W/Y54W Pseudomonas putida
5.1.2.2 0.5
-
 (S)-cyclohexylphenylglycolate wild-type enzyme Pseudomonas putida
5.1.2.2 0.67
-
 benzilate wild-type enzyme Pseudomonas putida
5.1.2.2 2 5 (S)-2-naphthylglycolate wild-type enzyme Pseudomonas putida
5.1.2.2 4.5
-
 diphenylacetate wild-type enzyme Pseudomonas putida
5.1.2.2 11.4
-
 (S)-2-hydroxybutyrate wild-type enzyme Pseudomonas putida
5.1.2.2 17.3
-
 (R)-2-hydroxybutyrate wild-type enzyme Pseudomonas putida
5.1.2.2 33
-
 (R)-2-naphthylglycolate wild-type enzyme Pseudomonas putida
5.1.2.2 45
-
 benzilate mutant enzyme F52W/Y54W Pseudomonas putida
5.1.2.2 71
-
 (S)-2-hydroxybutyrate mutant enzyme F52W/Y54W Pseudomonas putida
5.1.2.2 98
-
 (R)-2-hydroxybutyrate mutant enzyme F52W/Y54W Pseudomonas putida