Adenylosuccinate synthetase and adenylosuccinate lyase from plant tissues

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Abstract
Enzymes that convert IMP into adenylosuccinate (adeny-losuccinate synthetase) and adenylosuccinate into AMP (adenylosuccinate lyase) were isolated from wheat germ and pea seeds and their properties are described. These enzymes were purified approx. 200-fold from wheat-germ extracts. A heat treatment provided adenylosuccinate lyase free of adenylosuccinate synthetase but the behavior of the two enzymes was almost identical in a number of fractionation procedures. The two activities were finally separated by filtration on Sephadex G-100. The identification of these enzymes in plant tissues is discussed in relation to the pathway of purine synthesis.