Stereospecificity of conversion of @entity414 into XXXX by enzymes of Canadida utilis.

@entity1133 @entity13579 @entity56964 @entity717 @entity375 @entity414
1. Allantoinase [EC 3.5.2.5] was isolated from cells of Candida utilis and unpurified by chromatography on columns of DEAE-cellulose and Sephadex G-200 after treatment with @entity1133 to remove @entity414 oxidase [EC 1.7.3.3.]. 2. The purified allantoinase catalyzed the hydrolysis of @entity13579 into @entity56964 . However, only half of the @entity13579 produced from @entity414 by @entity414 oxidase was converted. The rest of the @entity13579 was unchanged, and showed a negative @entity717 . 3. On the other hand, the combined action of crude @entity414 oxidase and allantoinase resulted in nearly complete conversion of @entity414 into @entity56964 . Furthermore, the unpurified allantoinase preparation hydrolyzed racemic @entity13579 to @entity56964 completely. 4. These results indicate that the @entity414 oxidase produces racemic @entity13579 from @entity414 and that the allantoinase attacks only @entity13579 of positive @entity717 . The results also suggest that @entity13579 racemase is present in the @entity375 cells.
