Adenine Phosphoribosyltransferase in Plant Tissues: Some Effects of Kinetin on Enzymic Activity

Abstract
Adenine phospor-ibusyltransferase activity was measured in extracts of soybean (Glycine max cv. Acme) callus and of senescing barley leaves (Hordeum disticlion cv. Prior). The enzyme from soybean callus had Michaelis constants for adenine and 5-phosphoribosyl pyrophosphate of 1.5 and 7.5 [mu]M respectively, and was inhibited by AMP and stimulated by ATP.~The presence of kinetin was found to considerably increase the actibity of adenine phosphoribosyltransferase in extracts of soybean callus and senescing barley leaves.