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Metabolism of Formiminoglycine

FORMIMINOTETRAHYDROFOLATE CYCLODEAMINASE

From the ¹ From the Department of Biochemistry, University of California, Berkeley, California 94720

Formiminotetrahydrofolate cyclodeaminase has been purified approximately 40-fold from lyophilized cells of Clostridium cylindrosporum. The purified enzyme is homogeneous by ultracentrifugation, and the molecular weight is estimated as approximately 38,000. The affinity constant for (-)-formiminotetrahydrofolate is 2.8 x 10^-5 m. The formimino derivatives of tetrahydropteroyl-l-aspartate and tetrahydropteroyltri-l-glutamate ( linkage) were synthesized, and the kinetic constants were determined. The activity of the enzyme is inhibited strongly by (±)-tetrahydrofolate and several other pteridine derivatives, as well as by metal ions. The enzyme has optimum activity at pH 7.2. The spectral evidence obtained suggested that the reaction is reversible to a small extent at pH 8.2.

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