Sandbox Reserved 322: Difference between revisions

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[[Image:Arginine.jpg|thumb|right|300px|Figure 2: General reaction of arginase hydrolyzing L-arginine to urea and L-ornithine.]]

In general arginase is a homotrimeric enzyme, which is present in the fifth and final step of the urea cycle for mammals. In humans, hAI converts L-arginine into L-orinithine and urea as shown in figure 2. Human arginase II plays a role in L-arginine homeostasis, by regulating L-arginine concentrations from cellular biosynthetic reactions such as nitric oxide (NO) biosynthesis<ref name="c"/>. Additionally Plasmodium falciparum arginase is comparable to human arginase, due to the fact that it is 27% identical with human aginase I and II<ref name="b"/>.

In general arginase is a homotrimeric enzyme, which is present in the fifth and final step of the urea cycle for mammals. In humans, hAI converts L-arginine into L-orinithine and urea as shown in figure 2. Human arginase II plays a role in L-arginine homeostasis, by regulating L-arginine concentrations from cellular biosynthetic reactions such as nitric oxide (NO) biosynthesis<ref name="c"/>. Additionally ''Plasmodium falciparum'' arginase is comparable to human arginase, due to the fact that it is 27% identical with human aginase I and II<ref name="b"/>.

Overall arginase is a homotrimeric metallo-enzyme with a binuclear manganese <scene name='Sandbox_Reserved_322/Mn/5'>MN</scene> cluster in each monomer as shown in the PDB identifier 3mmr<ref name="c"/>. The overall fold of the arginase monomer belongs to the α/β protein class with a globular structure<ref name="d">PMID: 8849731 </ref>.

Sandbox Reserved 322: Difference between revisions

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@@ Line 16: / Line 16: @@
 [[Image:Arginine.jpg|thumb|right|300px|Figure 2: General reaction of arginase hydrolyzing L-arginine to urea and L-ornithine.]]
-In general arginase is a homotrimeric enzyme, which is present in the fifth and final step of the urea cycle for mammals. In humans, hAI converts L-arginine into L-orinithine and urea as shown in figure 2. Human arginase II plays a role in L-arginine homeostasis, by regulating L-arginine concentrations from cellular biosynthetic reactions such as nitric oxide (NO) biosynthesis<ref name="c"/>. Additionally Plasmodium falciparum arginase is comparable to human arginase, due to the fact that it is 27% identical with human aginase I and II<ref name="b"/>.
+In general arginase is a homotrimeric enzyme, which is present in the fifth and final step of the urea cycle for mammals. In humans, hAI converts L-arginine into L-orinithine and urea as shown in figure 2. Human arginase II plays a role in L-arginine homeostasis, by regulating L-arginine concentrations from cellular biosynthetic reactions such as nitric oxide (NO) biosynthesis<ref name="c"/>. Additionally ''Plasmodium falciparum'' arginase is comparable to human arginase, due to the fact that it is 27% identical with human aginase I and II<ref name="b"/>.
 Overall arginase is a homotrimeric metallo-enzyme with a binuclear manganese <scene name='Sandbox_Reserved_322/Mn/5'>MN</scene> cluster in each monomer as shown in the PDB identifier 3mmr<ref name="c"/>. The overall fold of the arginase monomer belongs to the α/β protein class with a globular structure<ref name="d">PMID: 8849731 </ref>.