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Literature summary extracted from

  • Gerlt, J.A.; Kenyon, G.L.; Kozarich, J.W.; Neidhart, D.J.; Petsko, G.A.; Powers, V.M.
    Mandelate racemase and class-related enzymes (1992), Curr. Opin. Struct. Biol., 2, 736-742.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.2.2 crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
5.1.2.2 H297N H297N, which is inactive as a racemase catalyzes the stereospecific exchange of the alpha-proton of S- but not R-mandelate with solvent D2O at a rate that is 30% of that of the wild type enzyme Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.2.2 2-Hydroxybutyrate competitive Pseudomonas putida
5.1.2.2 DL-alpha-Phenylglycidate irreversible Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.2.2 0.25
-
 D-mandelate L-mandelate Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.2.2 Divalent metal ions the required divalent metal ion is ligated by the carboxyl groups of Asp195, Glu221, and Glu247, which emanate from the carboxy-terminal ends of strands 3, 4 and 5, respectively Pseudomonas putida
5.1.2.2 Mg2+ required Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.2.2 39000
-
 8 * 39000 Pseudomonas putida

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
5.1.2.2 (S)-mandelate = (R)-mandelate two-base mechanism in which the conjugate acid of the R-specific base is monoprotic and in which the S-specific base may be an amino group Pseudomonas putida
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.2.2 (S)-2-hydroxy-3-butenoic acid maximal racemization rate is 35% relative to mandelate Pseudomonas putida (R)-2-hydroxy-3-butenoic acid
-
 ?
5.1.2.2 D-mandelate
-
 Pseudomonas putida L-mandelate
-
 ?

Subunits

EC Number Subunits Comment Organism
5.1.2.2 More striking structural similarity of mandelate racemase with muconate lactonizing enzyme Pseudomonas putida
5.1.2.2 octamer 8 * 39000 Pseudomonas putida