arginine decarboxylase

α-(difluoromethyl)-DL-Arginine (RMI 71897) is an enzyma-activated, irreversible inhibitor of arginine decarboxylase for E. coli (Ki = 800 μM), Pseudomonas aeruginosa, and Klebsiella pneumoniae. At 0.01 mM, it has been shown to prevent osmotic stress-induced increases in arginine decarboxylase activity and putrescine synthesis in oat leaf cells. When combined with a variety of polyamine analogues, α-(difluoromethyl)-DL-Arginine inhibited the growth of Trypanosoma Crui in mammalian host cells at a minimum concentration of 10 mM and prevented the growth of Trypanosoma Crui in T-cell receptor alpha-deficient mouse models.

L-Arginine Decarboxylase, Escherichia coli (EC 4.1.1.19), is a carboxy-lyase enzyme that cleaves carbon-carbon bonds. It utilizes L-arginine as a substrate and produces two products: agmatine and CO2.

D-Arginine is the D-isomer and inactive form of L-Arginine.D-Arginine is an endogenous metabolite and inhibitor of EC 4.1.1.19 (arginine decarboxylase), has broad-spectrum toxicity to microorganisms, and acts as a regulator of microbial subpopulations.

Monofluoromethylagmatine is an arginine decarboxylase inhibitor.

Leucine dehydrogenase, Bacillus sp. (EC 1.4.1.9), is a carboxy-lyase capable of cleaving carbon-carbon bonds. L-Arginine Decarboxylase has one substrate, L-arginine, and produces two products: guanidine butyric acid and CO2.