Sandbox Reserved 1758: Difference between revisions

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== Function of your protein ==
== Function of your protein ==
   
   
Mevalonate 3,5-biphosphate decarboxylase is found in ''Picrophilus Torridus'', a thermoacidophilic archaeon of the order Thermoplasmatales. The enzyme catalyzes the elimination of the 3-phosphate group from mevalonate3,5-biphosphate as well as concomitant decarboxylation of the substrate, GGPP.  
<scene name='93/934002/Cartoon_image/1'>Mevalonate 3,5-biphosphate decarboxylase</scene> is found in ''Picrophilus Torridus'', a thermoacidophilic archaeon of the order Thermoplasmatales. The enzyme catalyzes the elimination of the 3-phosphate group from mevalonate3,5-biphosphate as well as concomitant decarboxylation of the substrate, GGPP.  
== Biological relevance and broader implications ==  
== Biological relevance and broader implications ==  
''Picrophilus Torridus'' undergoes Thermoplasma-type MVA (mevalonate). This is relevant because the journal is analyzing a distinction between a novel variant of the eukaryotic MVA pathway.
''Picrophilus Torridus'' undergoes Thermoplasma-type MVA (mevalonate). This is relevant because the journal is analyzing a distinction between a novel variant of the eukaryotic MVA pathway.