Abstract
The phosphate esters of oestradiol and stilboestrol compete with pyridoxal 5-phosphate for the apoenzyme in the reconstitution reaction of two pyridoxal phosphate-dependent enzymes, namely kynurenine aminotransferase and aspartate amino-transferase. The esters, however, are without action on the enzymic transamination itself. The phosphate esters are compared with the sulphate esters as inhibitors of the combination of apoamino-transferase with coenzyme.