Sandbox Reserved 322: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Brian Huang (talk | contribs) No edit summary |
Brian Huang (talk | contribs) No edit summary |
||
| Line 8: | Line 8: | ||
---- | ---- | ||
[[Image:Arginases_homotrimer.jpg|thumb|left|300px|Figure 1: Liver arginase illustrating that the general homotrimeric strucutre of arginase.]] | [[Image:Arginases_homotrimer.jpg|thumb|left|300px|Figure 1: Liver arginase illustrating that the general homotrimeric strucutre of arginase.]] | ||
Arginase is a 105 kD homotrimeric metallo-protein, as shown in figure 1, that 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 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, that 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 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>. | ||