CLEAVAGE OF BENZOYLALANINE AND ACETYL- 

 GLYCINE BY MOLD ENZYMES* 



ARTHUR W. DOX and W. EUGENE RUTH 

 (Chemical Section of the Iowa State College, Arnes, Iowa) 



The readiness with which certain aromatic acids, in which the 

 carboxyl group is attached to a cydic nucleus, conjugate with gly- 

 cine in the animal body is well known. Among the substances 

 which undergo this synthesis the most familiär is benzoic acid and 

 its Substitution products. The reaction is, however, not limited to 

 homocyclic Compounds, since both five and six membered heterocyc- 

 lic derivatives, among which may be mentioned pyromucic, thio- 

 phenic and pyridinic acids, also unite with glycine. 



A reversal of this reaction takes place under the influence of 

 certain enzymes. Such enzymes occur in plants as well as in animal 

 tissues. One of us, in collaboration with Neidig, has shown that 

 enzyme preparations from some of the lov/er fungi can bring about 

 the hydrolysis of hippuric acid^ and also that of pyromucuric acid.^ 



It was thought possible, however, that the enzymic hydrolysis 

 might be of wider application than the corresponding synthesis. In 

 the animal organism the best known conjugations are those in which 

 the substance to be excreted is united with glycine, glucuronic acid, 

 sulfuric acid or cysteine. Homologues of glycine do not enter into 

 synthetic reactions with the formation of excretory products, nor do 

 acid radicals of the aliphatic series unite with glycine. Consider- 

 ing the diversity of aromatic radicals capable of combining in this 

 way with glycine and not with the other amino acids, the question 

 arises as to what determines the specificity of the reaction, and 

 whether the corresponding hydrolysis would be equally specific. 

 For instance, is the cleavage of such Compounds dependent upon the 



♦Read at the Rochester meeting of the American Chemical Society, Sep. 

 10, 1913. (Page 83.) 



^Dox and Neidig: Zeitschr. f. physiol. Chem., 1913, Ixxxv, p. 68. 

 2 Dox and Neidig : Biochem. Bull., 1913, ii, p. 407. 



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