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Literature summary extracted from

  • Nagar, M.; Wyatt, B.N.; St Maurice, M.; Bearne, S.L.
    Inactivation of mandelate racemase by 3-hydroxypyruvate reveals a potential mechanistic link between enzyme superfamilies (2015), Biochemistry, 54, 2747-2757 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.2.2 3-Fluoropyruvate
-
 Pseudomonas putida
5.1.2.2 3-hydroxypyruvate an irreversible, time-dependent inhibitor, causes inactivation of mandelate racemase. Protection from inactivation by the competitive inhibitor benzohydroxamate. 3-Hydroxypyruvate undergoes Schiff-base formation with Lys166 at the active site, followed by formation of an aldehyde/enol(ate) adduct Pseudomonas putida
5.1.2.2 benzohydroxamate competitive inhibitor Pseudomonas putida
5.1.2.2 mesoxalate
-
 Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.2.2 Mg2+ dependent on Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
5.1.2.2 Pseudomonas putida P11444
-
-

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
5.1.2.2 1.3
-
 3-Fluoropyruvate pH and temperature not specified in the publication Pseudomonas putida
5.1.2.2 1.8
-
 mesoxalate pH and temperature not specified in the publication Pseudomonas putida

General Information

EC Number General Information Comment Organism
5.1.2.2 evolution mandelate racemase is a member of the enolase superfamily. The ability of the enzyme to form and deprotonate a Schiff-base intermediate furnishes a mechanistic link to other alpha/beta-barrel enzymes utilizing Schiff-base chemistry and is in accord with the sequence- and structure-based hypothesis that members of the metal-dependent enolase superfamily and the Schiff-base-forming N-acetylneuraminate lyase superfamily and aldolases share a common ancestor Pseudomonas putida