Arginine succinatase is an enzyme that is synthesized from arginine and succinate and catalyzes the reverse reaction to form L-arginine. The enzyme plays a key role in the biosynthesis of urea from ammonia, but is also involved in the regulation of arginine levels in the blood. Decreased arginine succinate lyase activity can lead to impaired arginine production, decreased DNA synthesis, protein synthesis, and cell division.
Argininosuckinatase was found in extracts of muscle tissue from monkeys and leprosy, and was later isolated as an independent protein. Its structural characteristics were first identified during amino acid analysis and its function determined when it was demonstrated to inhibit its amidation by an NH2OH/NH4OH complex that contained a monoclonal antiserum product and