Sandbox Reserved 646
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This Sandbox is Reserved from 30/08/2012, through 01/02/2013 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 636 through Sandbox Reserved 685. |
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More help: Help:Editing For more help, look at this link: http://proteopedia.org/w/Help:Getting_Started_in_Proteopedia ArginaseArginase is an enzyme found within the important urea cycle. Arginase is the final enzyme that allows the Urea cycle to complete its fifth and last step. Arginase takes on two distinct forms: Class I and II. The grouping into classes refers to the catalytic activity that the enzyme is capable of performing. In addition, each class are encoded by a different gene. Arginase I (arg1) is found in the cytoplasm of liver cells functioning in the urea cycle, while arginase II (arg2) is found in the mitochondria and functions in the kidney. In interest of our studies, we will refer to arginase I as arginase. Arginase belongs to the enzymatic class hydrolase. Arginase functions by cleaving the amino acid arginine with water to produce urea. When one studies enzymes, he pays careful attention the it’s specific activity. Specific activity quantifies the amount of product formed by the enzyme in reference to a given time per concentration of a protein. Arginase is known to have high specific activity and functions to produce a good amount of urea.[1] In addition, this enzyme allows the regeneration of ornithine which is the final product of the urea cycle. When there is a deficiency in the arg1 gene it is understood that one is undergoing an urea cycle disorder. In people with arginase deficiency, arginase is either missing or harmed, therefore arginine is not metabolized correctly. In lieu of this, it is impossible for urea to be formed, leaving the excess nitrogen to accumulate in the blood in the form of ammonia. Which leads to serious problems in the body.[2] |