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Literature summary extracted from

  • Mitra, B.; Kallarakal, A.T.; Kozarich, J.W.; Gerlt, J.A.; Clifton, J.G.; Petsko, G.A.; Kenyon, G.L.
    Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317 (1995), Biochemistry, 34, 2777-2787.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.2.2 mutant E317Q Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
5.1.2.2 E317Q E317Q with 3400fold reduced turnover number for (R)-mandelate and 29000fold reduced turnover number for (S)-mandelate. E317Q mutant enzyme does not catalyze detectable elimination of Br- from either enantiomer of p-(bromomethyl)mandelate. E317Q mutant enzyme is irreversibly inactivated by racemic alpha-phenylglycidate at a rate comparable to that measured for wild type enzyme Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.2.2 DL-alpha-Phenylglycidate wild type enzyme and mutant E317Q Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.2.2 0.4
-
 (R)-mandelate wild type enzyme Pseudomonas putida
5.1.2.2 2.4
-
 (R)-mandelate E317Q mutant 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 E317Q 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 0.012
-
 (S)-Mandelate mutant E317Q Pseudomonas putida
5.1.2.2 350
-
 (S)-Mandelate wild type enzyme Pseudomonas putida
5.1.2.2 500
-
 (R)-mandelate wild type enzyme Pseudomonas putida