Arginase 1 (ARG1) is a 35-40kD member of the arginase family of enzymes. It is expressed in multiple cell types, including erythrocytes, hepatocytes, neutrophils, smooth muscle and macrophages. ARG1 demonstrates two distinct functions: in the hepatocyte cytoplasm, it catalyzes the conversion of arginine to ornithine and urea, while in multiple cells, it degrades arginine, thus indirectly down-regulating NO synthase (NOS) activity by depriving this enzyme of its substrate. Human ARG1 is 322aa in length. Its enzyme region comprises aa9-309 and contains two Mn atoms. ARG1 is modestly active as a monomer, but highly active as a 105kD homotrimer. Trimerization is promoted by nitrosylation of Cys303, creating a regulatory feedback loop with NOS. There are two isoform variants, one that shows an eight aa insertion after Gln43, and another that shows a deletion of aa204-289. Full-length human ARG1 shares 87% aa identity with mouse and rat ARG1.
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