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Gaudy, Elizabeth T. (University of Illinois, Urbana),and R. S. Wolfe . Ureidoglycolate synthetase ofStreptococcus allantoicus . II. Properties of the enzyme and reaction equilibrium. J. Bacteriol.90: 1531–1536. 1965.—The properties of ureidoglycolate synthetase fromStreptococcus allantoicus grown on allantoin were studied, by use of the purified enzyme preparation and crystalline sodium ureidoglycolate. Ureidoglycolate synthetase activity was maximal over thep H range of 8.4 to 8.8. No cofactors were required for the reaction. Enzyme activity was inhibited byp -chloromercuribenzoate at relatively high concentrations, by Hg++ or Zn++ ions, and to a lesser extent by several other metal cations. The maximal velocity for the purified ureidoglycolate synthetase, determined graphically from a Lineweaver-Burk plot, was 220 μmoles of glyoxylate formed per min per mg of protein. The substrate concentration required for half-maximal velocity was 3.3 × 10−2 m . The equilibrium constant for the synthesis of ureidoglycolate was determined in a series of reaction mixtures covering a wide range of initial concentrations of reactants. The position of the equilibrium was not affected by a change inp H or by the presence of enzyme. The equilibrium constant for the reaction in the direction of synthesis was 7.6, corresponding to a negative free energy change of 1,230 cal per mole.

Ureidoglycolate Synthetase of Streptococcus allantoicus II. Properties of the Enzyme and Reaction Equilibrium