Abstract
As yet histidinase has been found only in extracts of the liver. It is not the same as arginase. Histidine is broken down to 2 molecules of ammonia, one of glutamic acid and probably one of formic acid. The reaction proceeds by way of intermediates as yet unknown, possibly through pyrollidon carboxylic acid as a precursor of glutamic acid. The enzyme has decided specificity, attacking only the naturally occurring optical isomer, but not imidazole, imidazole-lactic acid, imidazole-ethylamine, methylhisti-dine, and probably not carnosine and the methyl ester of histidine. Since no reaction occurs on the optically active carbon atom, it seems evident that the naturally occurring 1-histidine and d-glutamic acid belong to the same stereochemical group.