Human arginase isozymes.
Studies in experimental animals and humans demonstrate the existence of two arginase isozymes. One, designated AI (or A1), has a high pI, is located in the cytosol, is most abundant in liver, and is thought to be primarily responsible for ammonia detoxification as urea. The gene coding for this isozyme is mutated in human hyperargininemia. A second isozyme, designated AII (or A4), has a neutral pI, is located in the mitochondrial matrix, and is thought to be involved primarily in the production of ornithine as a precursor of proline and glutamate. It appears to be expressed in most but not all tissues and in more nearly equal amounts. The two isozymes are immunologically distinct and are coded for by two separate genes. The great similarity in all measured kinetic and some physicochemical properties implies a high degree of structural similarity at the active site, but the lack of immunological cross-reactivity and DNA cross-hybridization implies substantial compositional differences in other parts of the enzyme molecules.
D000818:Animals; D001119:Arginase / Q000235:genetics / Q000378:metabolism*; D001120:Arginine / Q000378:metabolism; D005786:Gene Expression Regulation; D006801:Humans; D020162:Hyperargininemia; D007527:Isoenzymes / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology; D009952:Ornithine / Q000378:metabolism; D013045:Species Specificity; D014508:Urea / Q000378:metabolism
D007527:Isoenzymes; D014508:Urea; D001120:Arginine; D009952:Ornithine; D001119:Arginase