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Literature summary for 5.1.2.2 extracted from

  • Maggio, E.T.; Kenyon, G.L.; Mildvan, A.S.; Hegeman, G.D.
    Mandelate racemase from Pseudomonas putida. Magnetic resonance and kinetic studies of the mechanism of catalysis (1975), Biochemistry, 14, 1131-1139.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
3-Hydroxy-2-naphthoic acid noncompetitive inhibition Pseudomonas putida
4-Hydroxycoumarin noncompetitive Pseudomonas putida
benzoate mixed-type inhibition Pseudomonas putida
DL-alpha-Phenylglycerate competitive Pseudomonas putida
naphthoate mixed-type inhibition Pseudomonas putida
salicylate competitive Pseudomonas putida

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ enzyme binds 0.9 mol Mn2+ per mol of subunit with a dissociation constant of 0.008 mM. Also six additional Mn2+ bind to the enzyme much more weakly, with a dissociation constant of 1.5 mM Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

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