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The Enzymatic Cleavage of the Carbon-Nitrogen Bond in 3,7,12-Trihydroxy-5ß-cholan-24-oylglycine

From the ¹ From the Biochemistry Research Division and Departments of Medicine and Pathology, Sinai Hospital of Baltimore, Inc., Baltimore, Maryland 21215

An enzyme from Clostridium perfringens capable of catalyzing the cleavage of the carbon-nitrogen bond in 3,7, 12-trihydroxy-5ß-cholan-24-oylglycine is described. The 15-fold purified enzyme hydrolyzes 3,12-dihydroxy-5ß-cholan-24-oylglycine at a slightly faster rate than glycocholic acid. The K_m for glycocholic acid in 0.01 m acetate buffer, pH 5.6, is approximately 8.0 x 10^-3 m. 3,7,12-Triketo-5ß-cholan-24-oylglycine, a substrate analogue, and 3,7,12-triketo-5ß-cholanoic acid are enzyme inhibitors. Cholic acid exhibited competitive product inhibition in the present system. The enzyme is inhibited by sulfhydryl group inhibitors.

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