Sandbox Reserved 1758: Difference between revisions
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== Function of your protein == | == Function of your protein == | ||
<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. | <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. The protein binds to an amphipathic fatty acid, Oleic Acid. This is the ligand represented in the structure however the authors noted that archaea do not tend to synthesize fatty acids. The authors found that GGPP or related compounds are possible physiological ligands. | ||
== 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. | ||
