3.5.3.1	L-arginine + H2O	-	
3.5.3.1	L-arginine + H2O	enzyme is involved in acid resistance and inhibits host nitric oxide production	
3.5.3.1	L-arginine + H2O	enzyme is involved in net production of ornithine, a precursor of polyamines, glutamate, and proline, enzyme is also involved in regulation of nitric oxide biosynthesis by modulating arginine availability for nitric oxide synthase	
3.5.3.1	L-arginine + H2O	enzyme is involved in regulating L-arginine bioavailability to NO synthase in human penile corpus cavernosum smooth muscle, and in clitoral corpus cavernosum and vagina, enzyme plays a role in both female and male sexual arousal	
3.5.3.1	L-arginine + H2O	enzyme is involved in regulation of nitric oxide biosynthesis by modulating arginine availability for nitric oxide synthase	
3.5.3.1	L-arginine + H2O	arginase competes with nitric oxide synthases for L-arginine as the common substrate	
3.5.3.1	L-arginine + H2O	arginase catalyzes the first committed step in the biosynthesis of polyamines	
3.5.3.1	L-arginine + H2O	the enzyme catalyses the catabolism of L-arginine to L-ornithine and urea	
3.5.3.1	L-arginine + H2O	the enzyme involved in urea cycle	
3.5.3.1	additional information	enzyme may be involved in cellular proliferation in atherosclerosis, inhibiton of enzyme expression by 17beta-estradiol as mechanism in attenuating atherogenensis	
3.5.3.1	additional information	mitochondrial isoform arginase II negatively regulates NO synthase 1 activity by limiting substrate availability in its microdomain	
3.5.3.1	additional information	presence of arginine pools, which are accessible to NO synthase and enzyme, but not exchangeable	
3.5.3.1	additional information	the wild type enzyme does not hydrolyze 1-amino-4-guanidinobutane (agmatine)	
3.5.3.1	additional information	arginase II is constitutively expressed in the airways of normal mice, whereas arginase I is undetectable in normal airways, while its expression is increased in airways of mice exposed to ovalbumin	
3.5.3.1	additional information	complex regulation of natural killer cell functions by arginine availability	
3.5.3.1	additional information	hereditary defects in arginase compromise structure and catalysis, which results in an accumulation of arginine in the blood known as hyperarginemia. Arginase deficiency can also result in the accumulation of nitrogen in the form of ammonia, which results in hyperammonemia	
3.5.3.1	additional information	infection of mice with Schistosoma mansoni cercariae elevates arginase activity	
3.5.3.1	additional information	recombinant human arginase I (rhArg-PEG), an arginine-depleting enzyme, can inhibit the growth of arginine-dependent tumors