Abstract
This chapter discusses regulation, genetics, and the properties of adenylosuccinate synthetase. Adenylosuccinate formed by adenylosuccinate synthetase is cleaved by adenylosuccinate lyase to form adenosine monophosphate (AMP). The two-step conversion of inosine 5' monophosphate (IMP) to AMP is similar to both the conversion of citrulline to arginine, which involves formation of argininosuccinate as an intermediate, and formation of 5-amino-imidazole 4-carboxamide ribonucleotide from 5-aminoimidazole 4-carboxylate ribonucleotide as part of IMP biosynthesis. Adenylosuccinate lyase is a dual-function enzyme catalyzing the cleavage of both adenylosuccinate and 5-aminoimidazole 4-N-succinocarboxamide ribonucleotide. The determination of the enzymatic activity of adenylosuccinate synthetase is most easily accomplished by observing the increase in absorbance at 280 nm, accompanying the conversion of IMP to adenylosuccinate. The most versatile system for the synthetase assay utilizes endogenous or added lyase and adenylate kinase to trap the adenylosuccinate into adenosine diphosphate and adenosine monophosphate. Adenylosuccinate synthetase is subject to feedback and product inhibition by AMP, adenylosuccinate, guanosine diphosphate, and guanosine monophosphate.
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