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 mevalonate 3,5-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 determined that GGPP or related compounds are possible physiological ligands. | <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 mevalonate 3,5-biphosphate as well as concomitant decarboxylation of the substrate. The protein binds to an amphipathic fatty acid, Oleic Acid. This is the <scene name='93/934002/Ligand/2'>ligand</scene> represented in the structure however the authors noted that archaea do not tend to synthesize fatty acids. The authors determined 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) pathway, the enzyme produces ADP in this pathway. This is relevant because the journal is analyzing a distinction between a novel variant of the eukaryotic MVA pathway. When the enzyme binds to a fatty-acid-like structure there is no ATP required for the reaction. There is an evolutionary route from ATP dependent to ATP-independent with the loss of kinase ability. | ''Picrophilus Torridus'' undergoes Thermoplasma-type MVA (mevalonate) pathway, the enzyme produces ADP in this pathway. This is relevant because the journal is analyzing a distinction between a novel variant of the eukaryotic MVA pathway. When the enzyme binds to a fatty-acid-like structure there is no ATP required for the reaction. There is an evolutionary route from ATP dependent to ATP-independent with the loss of kinase ability. | ||
== Important amino acids== | == Important amino acids== | ||
The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>. | The <scene name='93/934002/Asp_281_asp_309/1'>catalytic dyad</scene> is composed of Asp 281 and Asp 309<ref>PMID:35690147</ref>.<scene name='93/934002/Ligand/2'>ligand</scene> | ||
== Structural highlights == | == Structural highlights == | ||
Secondary Structure | Secondary Structure | ||
