arginine deiminase

Arginine deiminase is an enzyme that catalyzes the irreversible hydrolysis of L-arginine to citrulline and ammonia, representing the first step in the anaerobic degradation of arginine[4][6]. It is not present in high eukaryotes but is found in certain bacteria such as Pseudomonas aeruginosa[4][6]. Arginine deiminase has been investigated as a potential antimicrobial and antiparasitic drug target due to its absence in humans and essential role in microbial metabolism[4]. In oncology, pegylated forms of this enzyme (pegylated arginine deiminase) are being studied for their ability to deprive tumor cells of extracellular arginine, which some cancers require for growth[1][3]. The mechanism involves enzymatic depletion of systemic L-arginine, leading to inhibition of tumor cell proliferation.

Other names

arginine dihydrolase