Sandbox Reserved 322: Difference between revisions
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==='''Introduction'''=== | ==='''Introduction'''=== | ||
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[[Image:Arginases_homotrimer.jpg|thumb| | [[Image:Arginases_homotrimer.jpg|thumb|right|300px|Figure 1: Liver arginase illustrating that the general homotrimeric strucutre of arginase<ref name="Homotrimer">accessed April 3,2011: http://en.wikipedia.org/wiki/Arginase.</ref>.]] | ||
Arginase is a 105 kD homotrimeric metallo-protein, as shown in figure 1, and catalysis the hydrolysis of arginine to ornithine and urea by means of a binuclear spin-coupled Mn<sup>2+</sup> cluster in the active site<ref name="a">PMID: 19456858 </ref>. Many organisms contain the enzyme arginase, for example ''Homo sapiens'' and [http://en.wikipedia.org/wiki/Plasmodium_falciparum ''Plasmodium falciparum''], a parasite that causes cerebral malaria<ref name="b">PMID: 20527960 </ref>. In humans there are two forms of arginases that have evolved with differing tissue distributions and sub-cellular locations in mammals<ref name="c">PMID: 15766238 </ref>. | Arginase is a 105 kD homotrimeric metallo-protein, as shown in figure 1, and catalysis the hydrolysis of arginine to ornithine and urea by means of a binuclear spin-coupled Mn<sup>2+</sup> cluster in the active site<ref name="a">PMID: 19456858 </ref>. Many organisms contain the enzyme arginase, for example ''Homo sapiens'' and [http://en.wikipedia.org/wiki/Plasmodium_falciparum ''Plasmodium falciparum''], a parasite that causes cerebral malaria<ref name="b">PMID: 20527960 </ref>. In humans there are two forms of arginases that have evolved with differing tissue distributions and sub-cellular locations in mammals<ref name="c">PMID: 15766238 </ref>. | ||
